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Conserved domains on  [gi|1958765569|ref|XP_038962357|]
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titin isoform X45 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
31762-32038 1.41e-175

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 543.30  E-value: 1.41e-175
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14104       1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14104      81 VDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLKPGDKFRLQYT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKE 32001
Cdd:cd14104     161 SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKE 240
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1958765569 32002 RKSRMTASEALKHPWLKQRMDRVSTKVIRTLRHRRYY 32038
Cdd:cd14104     241 RKSRMTAQEALNHPWLKQGMETVSSKDIKTTRHRRYY 277
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
32081-32170 6.69e-56

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


:

Pssm-ID: 409521  Cd Length: 90  Bit Score: 192.56  E-value: 6.69e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32081 PVSGQIMHAIGEEGGYVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYG 32160
Cdd:cd20927       1 PVSGQIMHAVGEEGGHVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYG 80
                            90
                    ....*....|
gi 1958765569 32161 EDSSYAELFV 32170
Cdd:cd20927      81 EDSSYAELFV 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
33070-33161 2.33e-53

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


:

Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 185.25  E-value: 2.33e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33070 TLAARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVEN 33149
Cdd:cd05747       1 TLPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVEN 80
                            90
                    ....*....|..
gi 1958765569 33150 TDGKQEAQFTLT 33161
Cdd:cd05747      81 SEGKQEAQFTLT 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6-98 1.99e-48

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


:

Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 171.00  E-value: 1.99e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNG 85
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569    86 SGQATSTAELLVT 98
Cdd:cd20974      81 SGQATSTAELLVL 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
103-193 3.04e-45

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20972:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 91  Bit Score: 161.98  E-value: 3.04e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   103 PPNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSV 182
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569   183 GRATSTADLLV 193
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
18713-18806 8.54e-42

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20974:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 93  Bit Score: 152.12  E-value: 8.54e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18713 PVLDLKLSGVLtVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATN 18792
Cdd:cd20974       1 PVFTQPLQSVV-VLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569 18793 PAGSFVAYATVNVL 18806
Cdd:cd20974      80 GSGQATSTAELLVL 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2038-2129 1.81e-39

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


:

Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 145.64  E-value: 1.81e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERS--DRIYWYWPEDNVCELVIRDVTAEDSASIMVKAIN 2115
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSsiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  2116 IAGETSSHAFLLVQ 2129
Cdd:cd20951      81 IHGEASSSASVVVE 94
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
14277-14730 9.48e-34

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 143.99  E-value: 9.48e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14277 AVNVCGRATAVVEVNVLDKPGPPAAFdITDVTNESCLLTWNPPRDDGGSKITNYVVERKATDSDVWHKLSSTVKDTNfka 14356
Cdd:COG3401     121 AVGTATTATAVAGGAATAGTYALGAG-LYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGG--- 196
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14357 TKLTPNKEYIFRVAAENmyGVGEPVQATPIIAKYQFDPPGPPTRLEPSDITKDAVTLTWcepDDDGGSPITGYWVERLDP 14436
Cdd:COG3401     197 GDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW---DPVTESDATGYRVYRSNS 271
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14437 DTDKWVRCNKmpVKDTTYRVKGLTNKKKYRFRVLAENLAGpgKPSRSTEPILIKDPIDPPWPPGKPTVKDIGKTSLVLNW 14516
Cdd:COG3401     272 GDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW 347
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14517 TKPEhdgGAKIESYVIEMLKTGTDDWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKAG-ESEPSEPSDPvlcrEKLYP 14595
Cdd:COG3401     348 TASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSA----TTASA 420
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14596 PSPPRWLEVINITKNTADLKWTVPEKDGGSPITNYIVEKRDVRRKGWQTVDTTVKDtkcTVTPLTEGSLYVFRVAAENAI 14675
Cdd:COG3401     421 ASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSST---VTATTTDTTTANLSVTTGSLV 497
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 14676 GQSDYTEIGDSVLAKDTFTTPGPPYALTVVDVTKRHVDLKWEPPKNDGGRPIQRY 14730
Cdd:COG3401     498 GGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVS 552
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
22668-22749 1.94e-33

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 127.71  E-value: 1.94e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22668 TFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNV 22747
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22748 IV 22749
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
21297-21376 6.29e-33

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 126.55  E-value: 6.29e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21297 TLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKH--RANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVNV 21374
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 21375 RV 21376
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
20503-20584 2.98e-32

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 124.62  E-value: 2.98e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20503 CYLAKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSI 20582
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 20583 KV 20584
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
23463-23542 8.83e-31

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 120.39  E-value: 8.83e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23463 VINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDA--AIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTV 23540
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgrVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 23541 RV 23542
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
24546-24624 1.28e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 119.62  E-value: 1.28e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24546 IVVRAGGSARIHIPFKGRPTPEITWSKEEGEF--TDKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVK 24623
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 24624 V 24624
Cdd:cd05748      82 V 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
28878-28957 2.04e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 119.23  E-value: 2.04e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28878 THIVRAGASIRLFIAYQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFTV 28955
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 28956 KV 28957
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
21587-21667 1.48e-29

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 116.92  E-value: 1.48e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITIQ 21666
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 21667 V 21667
Cdd:cd05748      82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
13617-13962 4.16e-29

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 129.35  E-value: 4.16e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13617 EVSLAWEEPLTDGGSKIIGYVVER-RDIKRKTWVLVTDRADSCEFTVTGLQKGGVEYLFRVSARNRVGTGEPvetDSPVE 13695
Cdd:COG3401     149 GVDGANASGTTASSVAGAGVVVSPdTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP---SNEVS 225
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13696 ARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEYDGgaeITNYVIELRDKTSIRWDTAMTVRaeDLSATVTDVVEGQEYSF 13775
Cdd:COG3401     226 VTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTYYY 300
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13776 RVRAQNriGVGKPSAATPFVKVADPIERPSPPVNLSASEQTQSSVQLTWEPPLkdgGSPILGYIIERQEEGKDNWIRCNm 13855
Cdd:COG3401     301 RVTAVD--AAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIA- 374
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13856 KPVPELTYKVTGLQKGNKYLYRVSAENAAGV-SDPSEILGPLTADDASVEPTMDLSAFKDGLEVIVPNPIKILVPSTGYp 13934
Cdd:COG3401     375 ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGV- 453
                           330       340
                    ....*....|....*....|....*...
gi 1958765569 13935 rpKATWTFGDQVLEAGDRVKIKTISAYA 13962
Cdd:COG3401     454 --SAAVLADGGDTGNAVPFTTTSSTVTA 479
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
27793-27874 9.10e-29

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 114.61  E-value: 9.10e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27793 VIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGqPKSSTVSV 27872
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG-EKSATINV 80

                    ..
gi 1958765569 27873 KV 27874
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28619-28996 2.03e-28

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 127.43  E-value: 2.03e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28619 EAQSYTAIKLITGNEYQFRVSAVNKFGVGRPleSDPVVAQIQYTIPDAPGIPEPSNVTGNSITLTWTRPESDGgneIQHY 28698
Cdd:COG3401     190 TTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGY 264
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28699 ILERREKKSTRWVKVISkrpISETRFKVTGLVEGNEYEFHVMAENAAGVGpaSGISRLIKCREPVNPPSAPAVVKVTDTS 28778
Cdd:COG3401     265 RVYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGNE--SAPSNVVSVTTDLTPPAAPSGLTATAVG 339
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28779 KTTVSLEWArPVFDGGmeIIGYIIEMCKADLGDWHKVnTEPCVKTRYTVTDLQAGEEYKFRVSAINGAGK--GDSCEVTG 28856
Cdd:COG3401     340 SSSITLSWT-ASSDAD--VTGYNVYRSTSGGGTYTKI-AETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesAPSEEVSA 415
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28857 TIKAVDR---LSAPELDIDANFKQTHIVRAGASIR-LFIAYQGRPTPTAVWSKPDSNLSIraDIHTTDSFSTLTVENCNR 28932
Cdd:COG3401     416 TTASAASgesLTASVDAVPLTDVAGATAAASAASNpGVSAAVLADGGDTGNAVPFTTTSS--TVTATTTDTTTANLSVTT 493
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 28933 NDAGKYTLTVENNSGRKSITFT---VKVLDSPGPPGPITFKDVTRGSATLMWDAPLLDGGARIHHYV 28996
Cdd:COG3401     494 GSLVGGSGASSVTNSVSVIGASaaaAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
13874-14373 6.52e-28

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.89  E-value: 6.52e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13874 YLYRVSAENAAGVSDPSEILGPLTADDASVEPTMDLSAFKDGLEVIVPNPIKILVPSTGYPRPKATWTFGDQVLEAGDRV 13953
Cdd:COG3401     101 GSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAV 180
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13954 KIKTISAYAELIISPSERPDKGI-YTLTL----ENPVKSISGEIDVNVIAR-PSAPKELKFSDVTKDSVHLTWEPPDDDG 14027
Cdd:COG3401     181 ATTSLTVTSTTLVDGGGDIEPGTtYYYRVaatdTGGESAPSNEVSVTTPTTpPSAPTGLTATADTPGSVTLSWDPVTESD 260
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14028 gspLTGYVVEKRDMSRKTWTKVmDFVTDLEFTVPDLVQGKEYLFKVCARNKCGpGEPAYTDEpVNMSAPATVPDPPENVK 14107
Cdd:COG3401     261 ---ATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYYRVTAVDAAG-NESAPSNV-VSVTTDLTPPAAPSGLT 334
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14108 WRDRTANSIFLTWDPPKNDGgsrIKGYIVEKCPRGSDKWVACGEPVPDTKMEVTGLEEGKWYAYRVKALNRQGASkpSKP 14187
Cdd:COG3401     335 ATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAP 409
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14188 TEEIQAVDTQEAPEIFLD-----VKLLAGLTVKAGTKIELPATVTGK---PEPKITWTKADTLLRPDQRITIENVP--KK 14257
Cdd:COG3401     410 SEEVSATTASAASGESLTasvdaVPLTDVAGATAAASAASNPGVSAAvlaDGGDTGNAVPFTTTSSTVTATTTDTTtaNL 489
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14258 STVTITDSKRSDTGTYIIEAVNVCGRATAVVeVNVLDKPGPPAAFDITDVTNESCLLTWNPPRDDGGSKITNYvverkat 14337
Cdd:COG3401     490 SVTTGSLVGGSGASSVTNSVSVIGASAAAAV-GGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSV------- 561
                           490       500       510
                    ....*....|....*....|....*....|....*.
gi 1958765569 14338 dSDVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAEN 14373
Cdd:COG3401     562 -SGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVH 596
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29967-30046 6.74e-28

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 111.91  E-value: 6.74e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29967 TVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLAN--RAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLV 30044
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 30045 KV 30046
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27520-27928 9.72e-28

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.11  E-value: 9.72e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27520 TSRVVWSMVAENLEECIITTTKIIKGNEYIFRVRAVNKYGIGEPleSEPVVAKNSFVTPGPPSIPEVTKITKNSMTVVWN 27599
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27600 RPTVDGgseINGYFLEKRDKKSLAWLKVlkETIRDTRQKVTGLTENSDYQYRVCAVNAAGMGpfSEPSDFYKAADPIDPP 27679
Cdd:COG3401     255 PVTESD---ATGYRVYRSNSGDGPFTKV--ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE--SAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27680 GPPAKIRIADSTKSSITLGWSKPvydGGSDVTGYVVEMRQGEEEEWTIVSTkgEARTTEYVVSNLKPGVNYYFQVSAVNC 27759
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAE--TVTTTSYTDTGLTPGTTYYYKVTAVDA 402
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27760 AGQGEPitMTEPVQAKDILEEPEIDLDvalrTSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSiqNTDSSS 27839
Cdd:COG3401     403 AGNESA--PSEEVSATTASAASGESLT----ASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAV--PFTTTS 474
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27840 LLVIPQVTRNDTGKYILTIENGVGQPKSSTVSVKVLDTPAACQKLQVKHVSLGTVTLLWDPPlidggSPIINYVIEKRDA 27919
Cdd:COG3401     475 STVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPV-----TVGASTGDVLITD 549

                    ....*....
gi 1958765569 27920 TKRTWSIVS 27928
Cdd:COG3401     550 LVSLTTSAS 558
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
24832-24913 1.10e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 111.53  E-value: 1.10e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24832 TYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSV 24911
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 24912 IV 24913
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30301-30640 1.25e-27

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.11  E-value: 1.25e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30301 THTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKVVILDKPGPPIGPIKIDEVDATSVTISWEPP-ELDGGAPLSGY 30379
Cdd:COG3401      90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGtTASSVAGAGVV 169
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30380 VVEQRDAHRPGWLPVSESVTRPTFKFT-RLTEGNEYVFRVAATNRFGIGSYlqSEVIECRSSISIPGPPETLQIFDISRD 30458
Cdd:COG3401     170 VSPDTSATAAVATTSLTVTSTTLVDGGgDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPG 247
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30459 GMTLTWYPPEDDGgsqVTGYIIERKEVRADRWVRVNKVpvTMTRYRSTGLIEGLEYEHRVTAINARGTgkPSRPSKP-TV 30537
Cdd:COG3401     248 SVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVvSV 320
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30538 AMDPIaPPGKPQNPRVTDTTRTSVSLAWSVPEDEGgskVTGYLIEMQKVDQREWTKCNTTPTKIrEYTLTHLPQGAEYRF 30617
Cdd:COG3401     321 TTDLT-PPAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTT-SYTDTGLTPGTTYYY 395
                           330       340
                    ....*....|....*....|....
gi 1958765569 30618 RVLACNAGGP-GEPAEVPGTVKVT 30640
Cdd:COG3401     396 KVTAVDAAGNeSAPSEEVSATTAS 419
I-set pfam07679
Immunoglobulin I-set domain;
7107-7196 1.49e-27

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 111.20  E-value: 1.49e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVG 7186
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7187 KDMCSAQLSV 7196
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
20532-21039 1.70e-27

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 124.34  E-value: 1.70e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20532 EDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKVVGKPGIPTGPIKFDEVTAEAMTLKWGP 20611
Cdd:COG3401      91 ATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVV 170
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20612 PKDDGGSEITNYVLEKRDSVNNKWVTcasavqkttfrvTRLHEGIEYTFRVSAENKygVGEGLKSEPIVAKHPFDVPDAP 20691
Cdd:COG3401     171 SPDTSATAAVATTSLTVTSTTLVDGG------------GDIEPGTTYYYRVAATDT--GGESAPSNEVSVTTPTTPPSAP 236
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20692 PPPNIVDVRHDSVSLTWTDPKKTGgspITGYHIEFKERNSLLWKRANKTpiRMKDFKVTGLTEGLEYEFRVMAINLAGVg 20771
Cdd:COG3401     237 TGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGN- 310
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20772 kPSLPSEPVVALDPIDPPGKPEVISVTR---NSVTLIWTEPKYDGghkLTGYIVEKRDLPSKSWMKANHVnVPDCAFTVT 20848
Cdd:COG3401     311 -ESAPSNVVSVTTDLTPPAAPSGLTATAvgsSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAET-VTTTSYTDT 385
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20849 DLVEGGKYEFRIRAKNTAGAISAPSE----STGTIICKDEYEAPTIVLDPTIKDGLTVKAGDSIVLSAISILGKPLPKSS 20924
Cdd:COG3401     386 GLTPGTTYYYKVTAVDAAGNESAPSEevsaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20925 WSKAGKDIRPSDIAQITSTPTSSMLTVKYAT--RKDAGEYTITATNPFGTKEEhVKVSVLDVPGPPGPIEISNVSAEKAT 21002
Cdd:COG3401     466 NAVPFTTTSSTVTATTTDTTTANLSVTTGSLvgGSGASSVTNSVSVIGASAAA-AVGGAPDGTPNVTGASPVTVGASTGD 544
                           490       500       510
                    ....*....|....*....|....*....|....*..
gi 1958765569 21003 LTWTPPLEDGGSPIKAYVLEKRETSRLLWTVVSEDIQ 21039
Cdd:COG3401     545 VLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSL 581
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
17045-17124 2.04e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 110.76  E-value: 2.04e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17045 RIVVHAGGVIRIIAYVSGKPPPTVTWNMNERAL--PQEATIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIV 17122
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 17123 DV 17124
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25356-25768 2.58e-27

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 123.96  E-value: 2.58e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25356 TSRLSWTQVSTEVQALNYKVTKLLPGNEYIFRVMAVNKYGVGEPleSEPVIACNPYKLPGPPSTPEASAITKDSMVLTWT 25435
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25436 rPVDDGGAeiEGYILEKRDKEGIRWTKCNkkTLTDLRFRVTGLTEGHSYEFRVAAENAAgvGEPSEPSVFYRACDALYPP 25515
Cdd:COG3401     255 -PVTESDA--TGYRVYRSNSGDGPFTKVA--TVTTTSYTDTGLTNGTTYYYRVTAVDAA--GNESAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25516 GPPSNPKVTDTSRSSVSLAWNKPiydGGAPVRGYVIELKEAAADEWTTCTppSGLQGKQFTVTKLKENTEYNFRICAFNT 25595
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ETVTTTSYTDTGLTPGTTYYYKVTAVDA 402
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25596 EGVGEPATIPGSVVAQermEAPEIELDADLRKVVTLRASATLRLFVTIKGRPEPEVKWEKAEGILTERAQIEVTSSYTML 25675
Cdd:COG3401     403 AGNESAPSEEVSATTA---SAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA 479
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25676 VIDNVTRFDSGRYNLTLENNSGSKTAFVNVRVLDSPSAPVNLTVREvkKDSVTLSWEPPLIDGGAKVTNYIVEKRETTRK 25755
Cdd:COG3401     480 TTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPD--GTPNVTGASPVTVGASTGDVLITDLVSLTTSA 557
                           410
                    ....*....|...
gi 1958765569 25756 AYATITNNCTKTT 25768
Cdd:COG3401     558 SSSVSGAGLGSGN 570
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26707-26786 2.60e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 110.37  E-value: 2.60e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26707 TLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDL--RTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTFVV 26784
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 26785 KV 26786
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26437-26819 6.68e-27

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 122.80  E-value: 6.68e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26437 TSRLAWTICEAELRTTSCKVTKLLKGNEYIFRVTGVNKYGVGEPleSVAVKALDPFTTPSPPTSLEITSVTKDSMTLCWS 26516
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26517 RPEtdgGSDISGYIIERREKNSLRWMRVNKkpVYDLRVKSTGLREGCEYEYRVFAENAAGLslPSDTSPLVRAEDPVFLP 26596
Cdd:COG3401     255 PVT---ESDATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26597 SPPSKPKIVDSGKTTITIGWVKPLfdgGAPITGYTVEYKKSEETDWKVAIQSFRGTEYTMSGLTTGAEYVFRVRSLNKVG 26676
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26677 -ASDPSDITDPQVAkereeePAFDVDSEMRKTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRTSLT 26755
Cdd:COG3401     405 nESAPSEEVSATTA------SAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT 478
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 26756 IENANRNDSGKYTLTIQNVLSAASMTFVVKVLDSPGPPANITVREVTKETAVLSWDVPENDGGA 26819
Cdd:COG3401     479 ATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAST 542
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26997-27078 1.07e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 108.45  E-value: 1.07e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26997 TVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTFINI 27076
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 27077 IV 27078
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
8989-9078 1.69e-26

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 108.50  E-value: 1.69e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVG 9068
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  9069 KDSCTAQLNI 9078
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8797-8886 2.09e-26

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 108.11  E-value: 2.09e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVG 8876
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8877 EVSSSTFLTV 8886
Cdd:pfam07679    81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3199-3289 3.64e-26

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20951:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 94  Bit Score: 107.51  E-value: 3.64e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLL---STGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKN 3275
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  3276 DYGVATTSASLSVE 3289
Cdd:cd20951      81 IHGEASSSASVVVE 94
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
16331-16420 4.86e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.91  E-value: 4.86e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16331 CLICKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKamkdgihdIPEDAQLETAENSSVIVIPECTRAHSGKYSITAKNKAG 16410
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLK--------ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG 72
                            90
                    ....*....|
gi 1958765569 16411 QKTANCRVKV 16420
Cdd:cd05748      73 EKSATINVKV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
19128-19207 6.13e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.52  E-value: 6.13e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVR-KGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVK 19206
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19207 V 19207
Cdd:cd05748      82 V 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
22381-22460 6.89e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.13  E-value: 6.89e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22381 VVTIRACCTLRLFVPIKGRPAPEVKWAREHGESLD--KASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFVNV 22458
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22459 RV 22460
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
7294-7382 7.92e-26

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 106.57  E-value: 7.92e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVG 7373
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  7374 SDTCACTVK 7382
Cdd:pfam07679    81 EAEASAELT 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22109-22355 9.09e-26

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 118.95  E-value: 9.09e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22109 TSRLAWTNVATEVQVTKLKVTKLLKGNEYIFRVMAVNKYGVGEPleSEPVLAVDPYGPPDPPKNPEVTTITKDSMVVCWg 22188
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW- 253
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22189 hpDSDGGSEIINYIVERRDKAGQRWVKCNkkALTDLRFKVSGLTEGHEYEFRIMAENAAGV-SAPSATSPFYKacdSVFK 22267
Cdd:COG3401     254 --DPVTESDATGYRVYRSNSGDGPFTKVA--TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTT---DLTP 326
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22268 PGPPGNPRVLDTSRSSISIAWNKPiydGGSEITGYMVEIALPEEDEWQVVTPPagLKATSYTITNLIENQEYKIRIYAMN 22347
Cdd:COG3401     327 PAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET--VTTTSYTDTGLTPGTTYYYKVTAVD 401

                    ....*...
gi 1958765569 22348 SEGLGEPA 22355
Cdd:COG3401     402 AAGNESAP 409
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
30658-30736 1.58e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 105.36  E-value: 1.58e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30658 VFVRQGGVIRLTIPIKGKPFPICKWTKEGQDV--SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVK 30735
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 30736 V 30736
Cdd:cd05748      82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
21651-21963 2.12e-25

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.80  E-value: 2.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21651 TAKNTVGEVGDVITIQVHDIPGPPTGPIKFDEVSSDFVTFSWEPPENDGGVPISNYVVEMR--QTDSTTWVELATTVIRT 21728
Cdd:COG3401     113 SSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDtsATAAVATTSLTVTSTTL 192
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21729 TYKATRLTTGVEYQFRVKAQNryGVGPGITSASVVANYPFKVPGPPGTPQVTAVTKDSMTISWHEPLSDGgspILGYHIE 21808
Cdd:COG3401     193 VDGGGDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVY 267
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21809 RKERNGILWQTVSKalVPGNIFKSTGLTDGIAYEFRVIAENMAGKskPSKPSEPTFALDPIDPPGKPVPLNITRHT---V 21885
Cdd:COG3401     268 RSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGsssI 343
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 21886 ALKWAKPEYTGgfkITSYVVEKRDLPNGRWLKANfSNILENEFTVSGLTEDAAYEFRVIAKNAAGAISPPSEPSDAIT 21963
Cdd:COG3401     344 TLSWTASSDAD---VTGYNVYRSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATT 417
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29708-30085 2.89e-25

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.41  E-value: 2.89e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29708 TLSYVVTRLIKNNEYTFRVRAVNKYGLGVPieSEPIVARNSFTIPSQPGIPEGVGAGKEHIIIQWTKPESDGgneISNYL 29787
Cdd:COG3401     191 TLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYR 265
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29788 VDKREKKSLRWTRVNKdyvVYDTRLKVTSLMEGCDYQFRVTAVNSAGNsePSEASNFISCREPSYTPGPPSAPRVVDTTK 29867
Cdd:COG3401     266 VYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGS 340
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29868 SSISLAWTKPMydgGTDIIGYVLEMQEKDTDQWCRVHTntTIRNNEFTVPDLKMGQKYSFRVAAVNAKGmsDYSETTAEI 29947
Cdd:COG3401     341 SSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAE--TVTTTSYTDTGLTPGTTYYYKVTAVDAAG--NESAPSEEV 413
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29948 EpVERLEIPDLELADDLKKTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDKVNRYDAGKY 30027
Cdd:COG3401     414 S-ATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVT 492
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 30028 TIEAENQSGKKSATVLVKVYDTPGPCPSVNVKEVSRDSVTITWEIPTIDGGAPVNNYI 30085
Cdd:COG3401     493 TGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDL 550
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
23064-23145 3.08e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 104.59  E-value: 3.08e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23064 TVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNV 23143
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 23144 KV 23145
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
27393-27474 6.51e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 103.44  E-value: 6.51e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27393 VVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRV 27472
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 27473 QI 27474
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
30259-30340 6.64e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 103.44  E-value: 6.64e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30259 TIHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKV 30338
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 30339 VI 30340
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22729-23136 8.55e-25

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 8.55e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22729 HYTVKLTNSAGEATETLNVIVLDK---PGPPTGpVKMDEVTADSVTLSWEPPKydgGSSINNYIVEKRDTSTTAWQIVsA 22805
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVTTPttpPSAPTG-LTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKV-A 280
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22806 TVARTTIKASRLKTGCEYQFRIAAENRYG-KSTYlnSEPVIAQYPFKVPGPPGTPFVTLASKDSMEVQWhEPVSDGGsrV 22884
Cdd:COG3401     281 TVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP--SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--V 355
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22885 IGYHLERKERNSILWVKLNKTpIPQTKFKTTGLEEGIEYEFRVSAENIVGIGkpSKPSECYAAH--DPCDPPGRPEAIIV 22962
Cdd:COG3401     356 TGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATtaSAASGESLTASVDA 432
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22963 TRNSVTLQWKKPTYDGGSKITGYVVEKKELPDGRWmkasfTNIIDTQFEVTGLIEDHRYEFRVIARNAAGVFSEPSESTG 23042
Cdd:COG3401     433 VPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA-----VPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23043 AITARDEVEPPrISMDPKYKDTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVD 23122
Cdd:COG3401     508 SVSVIGASAAA-AVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTS 586
                           410
                    ....*....|....
gi 1958765569 23123 SGNYILKAKNVAGE 23136
Cdd:COG3401     587 TNTNDVAGVHGGTL 600
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17444-17715 1.00e-24

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 1.00e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17444 SWKPPLDDGGSEITNYIIEKKELGKDIWMPVTSASAKTTCKV---------PKLLEGKDYIFRIHAENLYGISDPlvSDS 17514
Cdd:COG3401     146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVtsttlvdggGDIEPGTTYYYRVAATDTGGESAP--SNE 223
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17515 MKARDRFRVPDAPEQPVVTEVTKDSALVTWNKPNDGGkpITNYILEKRETMSKRWVRVTKEPihpYTKYRVPDLLEGCQY 17594
Cdd:COG3401     224 VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSGDGPFTKVATVT---TTSYTDTGLTNGTTY 298
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17595 EFRVSAENEIGIgdPSPPSKPVFARDPIAKPSPPINPEAIDTTCNSVDLTWQPPrhdGGSKILGYIVEYQKVGDEEWRRA 17674
Cdd:COG3401     299 YYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKI 373
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 17675 NHTPEscpETKYKVTGLRDGQTYKFRVLAVNEAG-ESDPAHV 17715
Cdd:COG3401     374 AETVT---TTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEE 412
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24787-25210 1.03e-24

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 1.03e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24787 LSSGQEYQFRVKAYNEKGKSDPRVLGVPVIAKDLTIQPSFKLPFNTYSVQAGeDLKIEIPVIGRPRPKISWVKDGEPLRQ 24866
Cdd:COG3401       6 LTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLV-AAGLSSGGGLGTGGRAGTTSGVAAVAV 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24867 TTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVIVLEKPGPPVGPVKFDEVSADFVVISWEPPAYTGG 24946
Cdd:COG3401      85 AAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVA 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24947 C-QISNYIVEKRDTTTTNWQMVSATVArTTIKVSKLKTGTEYQFRIFAENRYGKSTPldSKPVVVQYPFKEPGPPGTPFV 25025
Cdd:COG3401     165 GaGVVVSPDTSATAAVATTSLTVTSTT-LVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTA 241
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25026 TSVSKDQMLVQWhEPVNDGGskVIGYHLEQKEKNSILWVKLNKIpiQDTKFKTTGLDEGLEYEFRVSAENIVGI-GKPSK 25104
Cdd:COG3401     242 TADTPGSVTLSW-DPVTESD--ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSN 316
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25105 VSECYVARDPCDPPGRPEAIIITRNSVTLKWKKPTydgGSKITGYIVEKKDLPDGRWMKASFTnVVETEFTVTGLVEDQR 25184
Cdd:COG3401     317 VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTT 392
                           410       420
                    ....*....|....*....|....*.
gi 1958765569 25185 YEFRVIARNAADNFSEPSESSGAITA 25210
Cdd:COG3401     393 YYYKVTAVDAAGNESAPSEEVSATTA 418
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26310-26391 1.84e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 102.28  E-value: 1.84e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26310 VIVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNC 26389
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 26390 KV 26391
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
25915-25996 4.74e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 101.13  E-value: 4.74e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25915 TFNVKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITV 25994
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 25995 IV 25996
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
6915-6996 5.54e-24

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 101.18  E-value: 5.54e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIG 6994
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ..
gi 1958765569  6995 TA 6996
Cdd:pfam07679    81 EA 82
I-set pfam07679
Immunoglobulin I-set domain;
900-989 1.04e-23

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 100.41  E-value: 1.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAG 979
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569   980 TVSTSCYLAV 989
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26998-27452 1.20e-23

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 112.40  E-value: 1.20e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26998 VYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGT---TKTFI 27074
Cdd:COG3401     146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGEsapSNEVS 225
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27075 NIIVLDRPGPPTGpVAISDITEESVTLKWEPPKydgGSHVTNYIVLKRETSTAVWTEVsATVARTMIKVMKLTTGEEYQF 27154
Cdd:COG3401     226 VTTPTTPPSAPTG-LTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYY 300
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27155 RIKAENRFGI-SDhiDSACVVVKLPYTTPGPPSTPWVSNVTRESITVGWhEPVSNGGsaVIGYHLEMKDRNSILWQKANK 27233
Cdd:COG3401     301 RVTAVDAAGNeSA--PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAE 375
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27234 MIiRTTHFKVTTISAGLIYEFRVYAENAAGIGkpSHSSEPVLAIDAcePPRNVRITDISKNSVNLSWQQPAFDGGSKITG 27313
Cdd:COG3401     376 TV-TTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTA--SAASGESLTASVDAVPLTDVAGATAAASAASN 450
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27314 YIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAVGSVSNpSEVVGPITCIDSYGGPVIDLPLEYTEV 27393
Cdd:COG3401     451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGA-SSVTNSVSVIGASAAAAVGGAPDGTPN 529
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 27394 VKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNS 27452
Cdd:COG3401     530 VTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTN 588
I-set pfam07679
Immunoglobulin I-set domain;
5697-5787 1.37e-23

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 100.02  E-value: 1.37e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDA 5776
Cdd:pfam07679     1 PKFTQKPKDVEV-QEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  5777 GTASCSIELKV 5787
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19211-19297 1.70e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 99.88  E-value: 1.70e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19211 PGPVSDLKVSDVTKTSCHVSWAPPENDGGsPVTHYIVEKREAERKTWSTV-TPEVKKTSFNVTNLVPGNEYFFRVTAVNE 19289
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 19290 YGPGVPTD 19297
Cdd:cd00063      80 GGESPPSE 87
I-set pfam07679
Immunoglobulin I-set domain;
8048-8137 1.92e-23

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 99.64  E-value: 1.92e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAG 8127
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8128 KDSCSAQLGV 8137
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
3305-3391 2.10e-23

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 99.64  E-value: 2.10e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3305 PAIVTPLQDAVTSEGRPARFQCQVSGT-DLKVSWYCRDKKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAVG 3383
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*...
gi 1958765569  3384 QVSSTATL 3391
Cdd:pfam07679    81 EAEASAEL 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29169-29249 2.55e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.82  E-value: 2.55e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29169 ITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLKETDRMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITVV 29248
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 29249 V 29249
Cdd:cd05748      82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18046-18507 3.62e-23

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.86  E-value: 3.62e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18046 IRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLTVLDVPGPPTGPINi 18125
Cdd:COG3401      80 AAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGT- 158
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18126 ldvtpeymTISWQPPKDDGGSPVINYIVEKQDTrkgtwgVVSAGSSKLKLKVPHLQKGCEYVFRVKAENKMGVGPPLDSI 18205
Cdd:COG3401     159 --------TASSVAGAGVVVSPDTSATAAVATT------SLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEV 224
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18206 PTVAKHkfSPPSPPGKPVVTDITENAATVSWTLPKSDGgspITGYYVERREIT-GKWVRVNKTpiADLKFRVTGLYEGNT 18284
Cdd:COG3401     225 SVTTPT--TPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGdGPFTKVATV--TTTSYTDTGLTNGTT 297
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18285 YEFRVFAENLAGlsNPSPSSDPIKACRPIKPPGPPINPKLKDKTKESADLVWTKPLSdggSPILGYVVECQKPGTTQWDR 18364
Cdd:COG3401     298 YYYRVTAVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD---ADVTGYNVYRSTSGGGTYTK 372
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18365 INkdELIRQCAFRVPGLIEGNEYRFRIRAANIVGEgEPRELAESVIAKDILHPPEVELDVTCRDVITVRVGQTIRILARv 18444
Cdd:COG3401     373 IA--ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAA- 448
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 18445 kgrpEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:COG3401     449 ----SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
I-set pfam07679
Immunoglobulin I-set domain;
3461-3550 3.65e-23

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 98.87  E-value: 3.65e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYG 3540
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  3541 RAVCSAHLKV 3550
Cdd:pfam07679    81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
31549-31630 4.14e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.43  E-value: 4.14e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31549 VHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFGIDQKTVEL 31628
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKN-AKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 31629 DV 31630
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16015-16314 4.75e-23

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.48  E-value: 4.75e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16015 NLAVTDIKAESCYLTWDAPLDNGGSEITHYIIDKRDASRKKSEWEEVTNTAVerrygiwkLIPNGQYEFRVRAVNKYGTS 16094
Cdd:COG3401     147 LYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGD--------IEPGTTYYYRVAATDTGGES 218
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16095 DEckSDKVVIQDPYRLPGPPGKPKVLERTKGSMLVSWTPPLDNGgspITGYWLEKREEGGAYWSRVSRapitkvgLKGVE 16174
Cdd:COG3401     219 AP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT-------VTTTS 286
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16175 FSVPRLIEGVKYQFRAMAINAAGIgpPSEPSDPAVAGDPIYPPGPPSCPEVKDKTKSSISLAWKPPAkdgGSPIKGYIVE 16254
Cdd:COG3401     287 YTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVY 361
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 16255 MQEEGTTDWKKVNEpdkLLTACECVVPNLKELRKYRFRVKAVNEAG-ESEPSDTTGEIPAT 16314
Cdd:COG3401     362 RSTSGGGTYTKIAE---TVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTAS 419
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
20214-20295 6.36e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.05  E-value: 6.36e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20214 TLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIVV 20293
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 20294 KV 20295
Cdd:cd05748      81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24331-24421 8.54e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 97.95  E-value: 8.54e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24331 PGPPKSLEVTNIAKDSMTVCWNRPDSDGGsEIIGYIVEKRDRSGIRWIKCNKRRITDLRLRVTGLTEDHEYEFRVSAENA 24410
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 24411 AGVGEPSPATV 24421
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15415-15507 9.41e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 97.95  E-value: 9.41e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15415 PDAPDKPIVDDVTSNSMVVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKALLSSLKTKVDGLLEGLTYVFRVCAENAA 15494
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|...
gi 1958765569 15495 GPGKFSPPSDPKT 15507
Cdd:cd00063      81 GESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
6541-6629 9.75e-23

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.71  E-value: 9.75e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6541 VIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGK 6620
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  6621 SSCTAVVDV 6629
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7856-7945 1.21e-22

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.33  E-value: 1.21e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVG 7935
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7936 AVASSAVLVI 7945
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
4949-5038 1.40e-22

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.33  E-value: 1.40e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVG 5028
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5029 SKDSRGALIV 5038
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25868-26388 2.16e-22

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 108.55  E-value: 2.16e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25868 SGLTAGEEYVFRVAAVNEKGRSDPRQLGVPVVAKDIEIKPSVELPFNTFNVKANDQL--KIDIPFKGRPQATVAWKKDGQ 25945
Cdd:COG3401      11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLgtGGRAGTTSGVAAVAVAAAPPT 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25946 VLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIVLDrpgPPGPIRIDEVSCDNVSISWTPPEY 26025
Cdd:COG3401      91 ATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYAL---GAGLYGVDGANASGTTASSVAGAG 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26026 DGGCQISNYIVEKRETTSTTWQVVsqavarTSIKIVRLTTGSEYQFRVCAENRYGKSSYSESSAVVaeYPFSPPGPPgTP 26105
Cdd:COG3401     168 VVVSPDTSATAAVATTSLTVTSTT------LVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVT--TPTTPPSAP-TG 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26106 KVVHATKSTMV-VSWQvPVNDGGsqVIGYHLEYKERSSILWSKANKVliADTQMKVSGLDEGLLYEYRVYAENIAGIGkc 26184
Cdd:COG3401     239 LTATADTPGSVtLSWD-PVTESD--ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNE-- 311
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26185 SKACEPVPARDPCDPPGQPE---VTNITRKSVSLKWSKPrydGGAKITGYIVERRELPDGRWLKCNFTnVQETYFEVTEL 26261
Cdd:COG3401     312 SAPSNVVSVTTDLTPPAAPSgltATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGL 387
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26262 TEDQRYEFRVFARNAADSVSEPSE----STGPITVKDDVEAPRIMMDvkfrdvivVKAGEVLKINADIAGRPLPVISWAK 26337
Cdd:COG3401     388 TPGTTYYYKVTAVDAAGNESAPSEevsaTTASAASGESLTASVDAVP--------LTDVAGATAAASAASNPGVSAAVLA 459
                           490       500       510       520       530
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 26338 DGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVN 26388
Cdd:COG3401     460 DGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
I-set pfam07679
Immunoglobulin I-set domain;
33698-33787 3.04e-22

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 96.17  E-value: 3.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRG 33777
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 33778 QCSATASLTV 33787
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7577-7666 3.59e-22

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 96.17  E-value: 3.59e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAG 7656
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7657 QDESSALLTV 7666
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
20882-21397 5.33e-22

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 107.40  E-value: 5.33e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20882 KDEYEAPTIVLDPTIKDGLTVKAGDSIVLSAISILGKPLPkssWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGE 20961
Cdd:COG3401      34 KTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRA---GTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTG 110
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20962 YTITATNPFGTKEEHVKVSVLDVPGPP--------GPIEISNVSAEKATLTWTPPLEDGGSPIKAYVLEKRETSRLLWTV 21033
Cdd:COG3401     111 LTSSDEVPSPAVGTATTATAVAGGAATagtyalgaGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTST 190
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21034 VSEDiqacrhVVTKLIQGNEYLFRVSAVNhyGKGEPVQSEPVKMVDRFGPPGPPGKPEISNVTKNTATVSWkRPIDDGGs 21113
Cdd:COG3401     191 TLVD------GGGDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW-DPVTESD- 260
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21114 eITGYHVERREKKGLRWVRATKTPVSDLRckVTGLQEGNTYEFRVSAENRAGIgpPSDASNPVLMKDVAYPPGPPSNAHV 21193
Cdd:COG3401     261 -ATGYRVYRSNSGDGPFTKVATVTTTSYT--DTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTA 335
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21194 TDTTKKSASLAWGKPHydgGLEITGYVVEHQKVGDDAWIKdtTGTALRITQFVVPDLQTKEKYNFRISAVNDAGVgEPAV 21273
Cdd:COG3401     336 TAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTK--IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAP 409
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21274 IPNVEIVEKETAPDFELDAElrrTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKHRANIENTESFTLLIIPECNRYD 21353
Cdd:COG3401     410 SEEVSATTASAASGESLTAS---VDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTT 486
                           490       500       510       520
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 21354 TGKFVMTIENPAGkkSGFVNVRVLDTPGPVLNLRPTDITKDSVT 21397
Cdd:COG3401     487 ANLSVTTGSLVGG--SGASSVTNSVSVIGASAAAAVGGAPDGTP 528
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29569-29649 5.35e-22

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 95.35  E-value: 5.35e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29569 VTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMVK 29648
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 29649 V 29649
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16829-16926 5.63e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 95.64  E-value: 5.63e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16829 PGAPDKPTVSSVTRNSMTVNWEEPEYDGGsPVTGYWLEMKDTTSKRWKRVNRDPIKAMtlgvSYKVTGLIEGSDYQFRVY 16908
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSET----SYTLTGLKPGTEYEFRVR 75
                            90
                    ....*....|....*...
gi 1958765569 16909 AINAAGVGPASLPSDPVT 16926
Cdd:cd00063      76 AVNGGGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
31053-31132 9.87e-22

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.63  E-value: 9.87e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31053 DVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29242-29649 1.15e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 106.24  E-value: 1.15e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29242 TFTITVVVIGRPGPVTGPIEVSSVSAESCVLSWSEPKDDGGTEITNYIVEKRESGTTAWQLINSSVKRTQIKVTHLT--K 29319
Cdd:COG3401     122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDieP 201
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29320 YKEYCFRVSSENRFGVSKPLESVPIVAehPFVPPSAPTRPEVYYVSANAMSIRWEEPYHDGgskIVGYWVEKKERNTILW 29399
Cdd:COG3401     202 GTTYYYRVAATDTGGESAPSNEVSVTT--PTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPF 276
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29400 VKENKVPclECNYKVTGLVEGLEYQFRTYALNAAGV-SKASEASRPIMAQNPVDPPGRPEVTDVTRSTVSLVWSAPMydg 29478
Cdd:COG3401     277 TKVATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS--- 351
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29479 GSKVVGYIIERkpvSEVGDGRWLKCNyTIVSDNFFTVTALSEGDTYEFRVLAKNAAGIISKGSEstgPVTCRDEYAPPKA 29558
Cdd:COG3401     352 DADVTGYNVYR---STSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSE---EVSATTASAASGE 424
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29559 ELDARLQGDLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNAS 29638
Cdd:COG3401     425 SLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASS 504
                           410
                    ....*....|.
gi 1958765569 29639 GTKSVSVMVKV 29649
Cdd:COG3401     505 VTNSVSVIGAS 515
I-set pfam07679
Immunoglobulin I-set domain;
33416-33505 1.26e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.63  E-value: 1.26e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAG 33495
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 33496 SVSSSCKLTI 33505
Cdd:pfam07679    81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
19420-19500 1.32e-21

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 94.19  E-value: 1.32e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19420 ITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKIKVT 19499
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19500 V 19500
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31337-31430 1.39e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.49  E-value: 1.39e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31337 PSVPGKPTITAVTKDSCVVAWKPPASDGGaKIRNYYLEKREKKQNKWIAVTTEEIRETVFSVQNLIEGLEYEFRVKCENL 31416
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 31417 GGESEWSETSEPVT 31430
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
4292-4381 1.43e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 1.43e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYG 4371
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4372 SVSCTATLTV 4381
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5511-5600 1.62e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 1.62e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAG 5590
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5591 HSQCSGHLTV 5600
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30785-31145 1.76e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 105.47  E-value: 1.76e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30785 AAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFGISKPlkseEPVIPKTPLNPPEPPSNPPEVLDVTKSSVSLSWSR 30864
Cdd:COG3401     180 VATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP----SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDP 255
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30865 PKDDGgsrVTGYYIERKETSTDKWVRHNKTqiTTTMYTVTGLVPDAEYQFRIIAQNDVGlsETSPASEPVVCKDPFDKPS 30944
Cdd:COG3401     256 VTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLTPPA 328
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30945 QPGELEILSISKDSVILQWEKPEcdgGKEILGYWVEYRQSGDSAWKKSNKErIKDRQFTIGGLLEATEYEFRVFAENETG 31024
Cdd:COG3401     329 APSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31025 L-SRPRRTAMSVKTKLTSGEAPGVRKemADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLT 31103
Cdd:COG3401     405 NeSAPSEEVSATTASAASGESLTASV--DAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT 482
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 31104 VMTEEQEDEGVYTCVATNEVGEVETSSKLLLQAAPQFHPGYP 31145
Cdd:COG3401     483 DTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAP 524
I-set pfam07679
Immunoglobulin I-set domain;
8235-8325 2.35e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.86  E-value: 2.35e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVG 8314
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|.
gi 1958765569  8315 SDTCvgSVTLK 8325
Cdd:pfam07679    81 EAEA--SAELT 89
I-set pfam07679
Immunoglobulin I-set domain;
7200-7290 2.56e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.48  E-value: 2.56e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDtSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGV 7279
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  7280 GHASCSTALKV 7290
Cdd:pfam07679    80 GEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8893-8981 3.63e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.09  E-value: 3.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPIG 8972
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  8973 SASSSAKLI 8981
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16424-16516 4.02e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 93.33  E-value: 4.02e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16424 PGPPKDLKVSDITRGSCRLSWKMPDDDGGDrIKGYVIEKKTIDGKAWTKVNPNCGS-TAFVVPDLISEQQYFFRVRAENR 16502
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 16503 FGIGPPAETIQRTT 16516
Cdd:cd00063      80 GGESPPSESVTVTT 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
23751-23830 4.38e-21

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 92.65  E-value: 4.38e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23751 YSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIEII 23830
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20299-20390 4.56e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.56e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20299 PGPPVNVTVKEISKDSAYITWDPPIiDGGSPIINYVVEKRDAERKSWSTVTTECPK-TSFRVSNLEEGKSYFFRVFAENE 20377
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 20378 YGIGDPGETRDAV 20390
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28119-28450 4.77e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 104.31  E-value: 4.77e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28119 SEYVRFSKTENKITLSIKNVKKENGGKYTVIL----DNAVCRNSFPITIITLG-PPSKPKGpIRFDEIKADSAIMSWDIP 28193
Cdd:COG3401     178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVaatdTGGESAPSNEVSVTTPTtPPSAPTG-LTATADTPGSVTLSWDPV 256
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28194 EDDGggeITCYSIEKREASQTNWKMVcSSVARTTFKVSNLVKDSEYQFRVRAENRYGV-SEPlvSNVIVAKHQFRIPGPP 28272
Cdd:COG3401     257 TESD---ATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAP--SNVVSVTTDLTPPAAP 330
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28273 GKPVIYNVTSDGMSLTWDAPvydGGSEVTGFHVEKKERNSILWQRVNTSpISGREYRATGLIEGLDYQFRVYAENSAGLS 28352
Cdd:COG3401     331 SGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNE 406
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28353 SPSDPSKFTLAVSPVDPPGTPDYIDVTRETITLKWNPPLRDGGSKIVAYSIEKRQGSDRWVrcnFTDVSECQYTVSGLSP 28432
Cdd:COG3401     407 SAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA---VPFTTTSSTVTATTTD 483
                           330
                    ....*....|....*...
gi 1958765569 28433 GDRYEFRIIARNAVGTIS 28450
Cdd:COG3401     484 TTTANLSVTTGSLVGGSG 501
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20000-20092 4.78e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.78e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20000 PGRCDPPVISNITKDHMTVSWKAPADDGGsPITGYLVEKRETQAVNWTKVNRKPVIERTLKATGLQEGTEYEFRVTAINK 20079
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 20080 AGPGKPSDASKAV 20092
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
8611-8700 5.26e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 5.26e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAG 8690
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8691 RASCTTQLFV 8700
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5978-6066 5.63e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 5.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5978 QIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGS 6057
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  6058 SSCDAYLRV 6066
Cdd:pfam07679    82 AEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16371-16766 6.88e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.54  E-value: 6.88e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16371 HDIPEDAQLETAENSSVIVIPECTRAHSGKYSITAKNKAGQKTANCRVKVM---DAPGPPKDLKVSDITRGSCRLSWkmp 16447
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTATADTPGSVTLSW--- 253
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16448 DDDGGDRIKGYVIEKKTIDGKAWTKVNPNcGSTAFVVPDLISEQQYFFRVRAENRFGI-GPPAETIQRTTArdpIYPPDL 16526
Cdd:COG3401     254 DPVTESDATGYRVYRSNSGDGPFTKVATV-TTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTD---LTPPAA 329
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16527 PIKLKIGLITKNTVHLSWKPPKndgGSPVTHYIVECLAWDPTGKKKEAwrqcnrRDVEELEFTVEDLVEGGEYEFRVKAV 16606
Cdd:COG3401     330 PSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIA------ETVTTTSYTDTGLTPGTTYYYKVTAV 400
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16607 NEAGV-SKPSATVGPVTVKDQTCPPSIELKEFMEVEEGTDVNIVAKIKGVPFPTLTW--FKAPPKKPDSKEPVVYDTHVN 16683
Cdd:COG3401     401 DAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVlaDGGDTGNAVPFTTTSSTVTAT 480
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16684 KQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTASKEMRLNVLGRPGPPVGPIKFESISADQMTLSWLPPKDDGGSKITN 16763
Cdd:COG3401     481 TTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560

                    ...
gi 1958765569 16764 YVI 16766
Cdd:COG3401     561 VSG 563
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20101-20189 7.06e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 7.06e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20101 PGPPAFPKVYDTTRSSVSLSWgKPAFDGGSPIIGYLVEVKRADSDHWVRCNlPEKLQKTRFEVTGLMENTEYQFRVYAVN 20180
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*....
gi 1958765569 20181 KIGYSDPSD 20189
Cdd:cd00063      79 GGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23249-23338 7.27e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 7.27e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23249 PDAPKAPEVTAVTKDSMIVVWERPASDGGsEILGYVLEKRDKEGIRWTRCHKRLIGELRLRVTGLLENHNYEFRVSAENA 23328
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 23329 AGLSEPSPPS 23338
Cdd:cd00063      80 GGESPPSESV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
23844-24121 7.63e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.54  E-value: 7.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23844 FDEVSAESITLSWNPPLYTGGCQITNYIVQKRDTTTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENRYGQSFAleS 23923
Cdd:COG3401     144 GAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--S 221
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23924 EPIVAQYPYKEPGPPGTPFVTAVSKDSMVVQWHEPINNGgspVIGYHLERKERNSILWTKVNKTIihDTQFKALNLEEGI 24003
Cdd:COG3401     222 NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGT 296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24004 EYEFRVYAENivGVGKASKNS-ECYVARDPcDPPGTPEAIIVKR---NEITLQWTkPVYDGGsmITGYIVEKRDLPEGRW 24079
Cdd:COG3401     297 TYYYRVTAVD--AAGNESAPSnVVSVTTDL-TPPAAPSGLTATAvgsSSITLSWT-ASSDAD--VTGYNVYRSTSGGGTY 370
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 24080 MKASFTnVIETQFTVSGLTEDQRYEFRVIAKNAAGAISKPSD 24121
Cdd:COG3401     371 TKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSE 411
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
32201-32293 1.20e-20

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20951:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 94  Bit Score: 91.71  E-value: 1.20e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:cd20951      81 IHGEASSSASVVV 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15807-15899 1.21e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 91.79  E-value: 1.21e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15807 PTSPERLTYTERTKSTITLDWKEPRSDGGsPIQGYIIEKRRHDKPDFERVNKRLCPTTSFLVDNLDEHQMYEFRVKAVND 15886
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 15887 IGESEPSLPLNVV 15899
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
4760-4849 1.90e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.16  E-value: 1.90e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4760 PTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEAG 4839
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4840 SQTSVGELIV 4849
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
9182-9271 1.99e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.16  E-value: 1.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9182 PVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAG 9261
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  9262 SDTSKCKVTI 9271
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
6353-6438 2.31e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.78  E-value: 2.31e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6353 PVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVG 6432
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*.
gi 1958765569  6433 SDTCIC 6438
Cdd:pfam07679    81 EAEASA 86
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14696-14787 2.95e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.63  E-value: 2.95e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14696 PGPPYALTVVDVTKRHVDLKWEPPKNDGGrPIQRYIIEKKEKLGTRWVKAGKTSGPDCNFRVTDVIEGTEVQFQVRAENE 14775
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 14776 AGVGHPSEPTEI 14787
Cdd:cd00063      80 GGESPPSESVTV 91
I-set pfam07679
Immunoglobulin I-set domain;
8424-8511 3.03e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.39  E-value: 3.03e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8424 IVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKD 8503
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*...
gi 1958765569  8504 SCTVSIQV 8511
Cdd:pfam07679    83 EASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
4387-4476 3.21e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.39  E-value: 3.21e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4467 ADICQAELTI 4476
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17229-17322 3.62e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.63  E-value: 3.62e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17229 PERPEDLEVKEVTKNTVTLTWNPPKYDGGsEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNI 17308
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 17309 VGQGKPSFCTKPIT 17322
Cdd:cd00063      80 GGESPPSESVTVTT 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1417-1507 3.98e-20

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05744:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 91  Bit Score: 90.25  E-value: 3.98e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:cd05744      81 GENSFNAELVV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31634-31725 3.99e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 3.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31634 PDPPRGVKVSDVSRDSVNLTWTEPASDGGsKVTNYIVEKCATTAERWLRV--GQARETRYTVVNLFGKTSYQFRVIAENK 31711
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 31712 FGLSKPSEPSEPTV 31725
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
4573-4663 4.60e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.01  E-value: 4.60e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4573 PSFVKKVDPSYLMlPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDA 4652
Cdd:pfam07679     1 PKFTQKPKDVEVQ-EGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  4653 GSDSCSTEVVI 4663
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24273-24538 9.77e-20

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.08  E-value: 9.77e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24273 TSRLAWTVVASEVVTNSLKVTKLLEGNEYIFRIMAVNKYGVGEPleSAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWN 24352
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24353 RPDSDGgseIIGYIVEKRDRSGIRWIKCNKrrITDLRLRVTGLTEDHEYEFRVSAENAAGV-GEPS-PATVYYKacdpVF 24430
Cdd:COG3401     255 PVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSnVVSVTTD----LT 325
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24431 KPGPPTNVHIVDTTKNSITLAWGKPiydGGSDILGYVVEICKADEEEWQIVTpqTGLRVTRFEISKLIEHQEYKIRVCAL 24510
Cdd:COG3401     326 PPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ETVTTTSYTDTGLTPGTTYYYKVTAV 400
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 24511 NKVGLGEAASVPGTVKPEDKLEAPELDL 24538
Cdd:COG3401     401 DAAGNESAPSEEVSATTASAASGESLTA 428
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21380-21469 1.01e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.01e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21380 PGPVLNLRPTDITKDSVTLHWDLPLiDGGSRITNYIVEKREATRKSYSTVTTKCHK-CTYKVTGLTEGCEYFFRVMAENE 21458
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 21459 YGIGEPTETTE 21469
Cdd:cd00063      80 GGESPPSESVT 90
I-set pfam07679
Immunoglobulin I-set domain;
6636-6725 1.08e-19

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.85  E-value: 1.08e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6636 PSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAG 6715
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6716 SDECRALLTV 6725
Cdd:pfam07679    81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
28480-28560 1.15e-19

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 88.42  E-value: 1.15e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIE--RRMNMEITDVlgSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEIT 28557
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKetGRVQIETTAS--STSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    ...
gi 1958765569 28558 VKV 28560
Cdd:cd05748      80 VKV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15097-15184 1.56e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.56e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15097 DVEVHNPTAKAMTITWKPPLYDGGsKIMGYIIEKLAKGEDRWKRCNEHLVPVLTYTAKGLEEGKEYQFRVRAENAAGIGE 15176
Cdd:cd00063       6 NLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84

                    ....*...
gi 1958765569 15177 PSRATPPT 15184
Cdd:cd00063      85 PSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26887-26970 1.57e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.57e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26887 PSPPEKLGVTSVSKDSVSLSWLKPEHDGGsRILHYVVEALEKGQKNWVKCAV--VKTTHHVVSGLREGHEYFFRVFAENQ 26964
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 26965 AGLSDP 26970
Cdd:cd00063      80 GGESPP 85
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
14908-14988 1.57e-19

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 88.03  E-value: 1.57e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14908 IVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASINVK 14987
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 14988 V 14988
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18908-19001 1.59e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.59e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18908 PGRPDPPEVTKVSKEEMTVVWNAPEYDGGKsITGYYLEKKEKHAVRWVPVNKSAIPERRLKVQNLLPGHEYQFRVKAENE 18987
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 18988 VGIGEPSLPSRPVV 19001
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14797-14888 1.62e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.62e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14797 PSPPLDLHVTDAGRKHIAIAWKPPEKNGGsPIIGYHVEMCPVGTEKWMRVNSRPIKDLKFKVeEGVVPDKEYVLRVRAVN 14876
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTL-TGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|..
gi 1958765569 14877 AVGVSDPSEISE 14888
Cdd:cd00063      79 GGGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24725-24808 2.25e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 2.25e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24725 PSPPGKVTLTDVSQTSASLMWEKPEHDGGsRILGYVVEMQPKGTEKWSVV--AESKVCSAVVSGLSSGQEYQFRVKAYNE 24802
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 24803 KGKSDP 24808
Cdd:cd00063      80 GGESPP 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25808-25891 2.32e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 2.32e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25808 PLPPGRVTLVDVTRNTATIKWEKPESDGGsKITGYVVEMQTKGSEKWSTCT--QVKTLEATISGLTAGEEYVFRVAAVNE 25885
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 25886 KGRSDP 25891
Cdd:cd00063      80 GGESPP 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18854-19394 2.37e-19

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.92  E-value: 2.37e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18854 VWSTYSANVLTPGATVTRLIEGNEYIFRVRAENKIGTGPPTESKPVIAKTkYDRPGRPDPPEVTKVSKEEMTVVWNAPEY 18933
Cdd:COG3401      88 PPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAAT-AGTYALGAGLYGVDGANASGTTASSVAGA 166
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18934 DGGKSITGYYLEKKEKHAVRWVPVNKSAIPERrlkvqnLLPGHEYQFRVKAENEVGIgepSLPSRPVVAKDPIEPPGPPT 19013
Cdd:COG3401     167 GVVVSPDTSATAAVATTSLTVTSTTLVDGGGD------IEPGTTYYYRVAATDTGGE---SAPSNEVSVTTPTTPPSAPT 237
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19014 NFKVVDTTKNSITLAWgKPVYDGGApiIGYVVEmRpkiaDASPDEGWKRCNAAAQLvrmEFTVTSLDENQEYEFRVCAQN 19093
Cdd:COG3401     238 GLTATADTPGSVTLSW-DPVTESDA--TGYRVY-R----SNSGDGPFTKVATVTTT---SYTDTGLTNGTTYYYRVTAVD 306
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19094 QVGIgrpaelkeairpkeileppeidldasmrklvvvragcpirlfaivRGRPAPKVTwrkvgidnvvrkgqvdlvdtma 19173
Cdd:COG3401     307 AAGN---------------------------------------------ESAPSNVVS---------------------- 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19174 flvipnstrddsgkysltlVNPAGEKavfvnvkvldtPGPVSDLKVSDVTKTSCHVSWAPPEndgGSPVTHYIVEKREAE 19253
Cdd:COG3401     320 -------------------VTTDLTP-----------PAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSG 366
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19254 RKTWSTVTPEVKKTSFNVTNLVPGNEYFFRVTAVNEYGP-GVPTDVPKPVLASDPLSEPDPPRKVEVTEMTKNSATLAWL 19332
Cdd:COG3401     367 GGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAAS 446
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 19333 PPLRDGGAKIDGYIISYREEDQP--ADRWTEYSVVKDLSLIITGLKEGKKYKFRVAARNAVGVS 19394
Cdd:COG3401     447 AASNPGVSAAVLADGGDTGNAVPftTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
I-set pfam07679
Immunoglobulin I-set domain;
7482-7570 2.53e-19

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.08  E-value: 2.53e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7482 RIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGK 7561
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  7562 SSCTVSVHV 7570
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8518-8607 2.58e-19

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 2.58e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAG 8597
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8598 SDECSAPLTV 8607
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17105-17508 2.89e-19

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.54  E-value: 2.89e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17105 YSLLAKNEGGERKKTIIVDVLDVPGPVGIP--FLSDNLTNDSCKLTWFSPEDDGgspITNYVIQKREADRRAWTPVTyTV 17182
Cdd:COG3401     207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVA-TV 282
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17183 TRQNATVQGLIQGKSYFFRIAAENSIG-MGPFVETpnALVIRDpITVPERPEDLEVKEVTKNTVTLTWNPPKydgGSEII 17261
Cdd:COG3401     283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNV--VSVTTD-LTPPAAPSGLTATAVGSSSITLSWTASS---DADVT 356
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17262 NYVLESRLIGTEKFHKVTnDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQGkpSFCTKPITCKDELAPPTLDLDfRDKLT 17341
Cdd:COG3401     357 GYNVYRSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASGESLT-ASVDA 432
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17342 VRVGEAFALTGRYSGkPKPKVDWFKDEADVlEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFCQVNVV 17421
Cdd:COG3401     433 VPLTDVAGATAAASA-ASNPGVSAAVLADG-GDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17422 DRPGPPVGPVVFDeVTKEYMVISWKPPLDDGGSEITNYIIEKKELGKDIWMPVTSASAKTTCKVPKLLEGKDYIFRIHAE 17501
Cdd:COG3401     511 VIGASAAAAVGGA-PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589

                    ....*..
gi 1958765569 17502 NLYGISD 17508
Cdd:COG3401     590 NDVAGVH 596
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
25228-25310 3.29e-19

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 87.26  E-value: 3.29e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25228 VIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAaRMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPIT 25307
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETG-RVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    ...
gi 1958765569 25308 VKV 25310
Cdd:cd05748      80 VKV 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
19817-19897 3.33e-19

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 87.26  E-value: 3.33e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19897 V 19897
Cdd:cd05748      82 V 82
I-set pfam07679
Immunoglobulin I-set domain;
1801-1889 3.73e-19

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 3.73e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDG-IHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGgTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  1880 VTEHKVKLEI 1889
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5137-5225 3.84e-19

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 3.84e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5137 FTEKLEPsQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGS 5216
Cdd:pfam07679     3 FTQKPKD-VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  5217 DHCTSIVIV 5225
Cdd:pfam07679    82 AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22561-22644 4.67e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 4.67e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22561 PLPPGKITLMDVTRNSVSLSWEKPEHDGGsRILGYIVEMQSKGSDKWATCAT--VKVTEATITGLIQGEEYSFRVSAQNE 22638
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 22639 KGISDP 22644
Cdd:cd00063      80 GGESPP 85
I-set pfam07679
Immunoglobulin I-set domain;
6259-6349 4.75e-19

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 4.75e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPA 6338
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  6339 GSTSCSTKVIV 6349
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22464-22553 5.68e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.68e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22464 PGPPQNLKIKEVTKTSVTLTWEPPLLDGGsKIKNYIVEKRESTRKAYSTVATNCHK-TSWKIDQLQEGCSYYFRVLAENE 22542
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 22543 YGIGLPAETAE 22553
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26790-26881 5.90e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.90e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26790 PGPPANITVREVTKETAVLSWDVPENDGGaPVKNYHIEKREASKKAWVSV-TNNCSRLSYKVTNLQEGAVYYFRVSGENE 26868
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 26869 FGVGVPAETKEGV 26881
Cdd:cd00063      80 GGESPPSESVTVT 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
24146-24227 6.84e-19

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 86.49  E-value: 6.84e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24146 TIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNV 24225
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 24226 KV 24227
Cdd:cd05748      81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23643-23734 1.01e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.40  E-value: 1.01e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23643 PQPPGKITVDDVTRNSVSLSWTKPEHDGGsKIIQYIVEMQAKNTDKWSEC--ARVKSLEAVITSLTQGEEYLFRVIAVNE 23720
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 23721 KGRSDPRSLAVPIT 23734
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16729-16821 1.05e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.40  E-value: 1.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16729 PGPPVGpIKFESISADQMTLSWLPPKDDGGsKITNYVIEKREANRKTWVRVSSEP-KECMYTIPKLLEGHEYVFRIMAQN 16807
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 16808 KYGIGEPLDSEPET 16821
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19604-19697 1.26e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.01  E-value: 1.26e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19604 PSEPKNARVTKVNKDCIFVAWDRPDSDGGsPITGYLIERKERNSLLWVKANDTIVRSTEYPCAGLVEGLEYSFRIYALNK 19683
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 19684 AGSSPPSKPTEYVT 19697
Cdd:cd00063      80 GGESPPSESVTVTT 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
21982-22063 1.35e-18

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 85.72  E-value: 1.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21982 TITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNV 22061
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22062 KV 22063
Cdd:cd05748      81 KV 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
17741-17818 1.52e-18

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 85.33  E-value: 1.52e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17741 HIKVGDTLRLSAIIKGVPFPKVTWKKEDRE--APTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd05748       3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPlkETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
23089-23628 2.11e-18

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.84  E-value: 2.11e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23089 WVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNVKVLDRPGPPEGPVA-ISGVTAEKCM 23167
Cdd:COG3401      74 GTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYAlGAGLYGVDGA 153
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23168 LAWKPPLQDGGSDIINYIVERRETSRLVWTLVDANVQTLSCKVTKLLEGNEYIFRIMAVNKYGVGEPleSEPLIAKNPFV 23247
Cdd:COG3401     154 NASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTT 231
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23248 VPDAPKAPEVTAVTKDSMIVVWERPASDGgseILGYVLEKRDKEGIRWTRchkrlIGEL---RLRVTGLLENHNYEFRVS 23324
Cdd:COG3401     232 PPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTK-----VATVtttSYTDTGLTNGTTYYYRVT 303
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23325 AENAAGlsEPSPPSAYQKACDPIYKPGPPNNPKVMDVTRSSVFLSWTKPiydGGCEIQGYIVEKCDVSVGEWTMCTppTG 23404
Cdd:COG3401     304 AVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ET 376
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23405 INKTNLEVEKLLEKHEYNFRICAINKAGVGEhaDVPGPVMVEEKLEAPDIDLDLELRKVINIRAGGSlrlFVPIKGRPTP 23484
Cdd:COG3401     377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNES--APSEEVSATTASAASGESLTASVDAVPLTDVAGA---TAAASAASNP 451
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23485 EVKWGKVDGEIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTleNSSGTKSAFVTVRVLDTPSPPVNLKVTEITKDSVSI 23564
Cdd:COG3401     452 GVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTT--GSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPN 529
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 23565 TW-EPPLLDGGSKIKNYIVEKREATRKSYAAVVTNCHKNSWKIDQLQEGcSYYFRVTAENEYGIG 23628
Cdd:COG3401     530 VTgASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLG-GSLLTTTSTNTNDVA 593
I-set pfam07679
Immunoglobulin I-set domain;
32306-32396 2.13e-18

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.39  E-value: 2.13e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGlDYYALHIRDTLPEDTGYYRVTATNTA 32385
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569 32386 GSTSCQAHLQV 32396
Cdd:pfam07679    80 GEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5791-5879 2.35e-18

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.00  E-value: 2.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5791 PIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANEGG 5870
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  5871 SCACTARVA 5879
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30147-30240 2.35e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 85.24  E-value: 2.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30147 PLVPTKLEVVDVTKSTVTLAWEKPLYDGGsRLTGYVLEACKAGTERWMKVVTLKPTVLDHTVISLNEGEQYLFRVRAQNE 30226
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 30227 KGVSEPREIVTPVT 30240
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
1038-1127 3.08e-18

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.00  E-value: 3.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKqtGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEG--GTYTLTISNVQPDDSGKYTCVATNS 78
                            90
                    ....*....|
gi 1958765569  1118 HGETSASASL 1127
Cdd:pfam07679    79 AGEAEASAEL 88
I-set pfam07679
Immunoglobulin I-set domain;
8328-8418 4.21e-18

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 84.62  E-value: 4.21e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8328 PQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDkGEIVRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKNDA 8407
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  8408 GVQECYATLSV 8418
Cdd:pfam07679    80 GEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5042-5131 4.55e-18

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 84.23  E-value: 4.55e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5042 PSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVAG 5121
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5122 SVECSANLFV 5131
Cdd:pfam07679    81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
32886-32975 5.24e-18

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20951:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 94  Bit Score: 84.39  E-value: 5.24e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32886 PRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESS---KIHYTNTSGVLTLEILDCQTEDSGTYRAVCTN 32962
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 32963 YKGEASDYATLDV 32975
Cdd:cd20951      81 IHGEASSSASVVV 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
19450-19935 5.32e-18

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 94.30  E-value: 5.32e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19450 DVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKIKVTVMDAPGPPQPPFDISEIDADACSLSWHIPL 19529
Cdd:COG3401      83 AVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASS 162
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19530 EdGGSNITNYIVEKCDVSRGDWVTALASVTKTSCrVGKLIPGQEYIFRVRAENRFGISEPltSPKMLAKFPFDVPSEPKN 19609
Cdd:COG3401     163 V-AGAGVVVSPDTSATAAVATTSLTVTSTTLVDG-GGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTG 238
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19610 ARVTKVNKDCIFVAWDRPDSDGgspITGYLIERKERNSLLWVKANDtiVRSTEYPCAGLVEGLEYSFRIYALNKAGSspP 19689
Cdd:COG3401     239 LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--E 311
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19690 SKPTEYVTARMPVDPPGKPEVVDVT---KNSASLIWARPKhdgGSKIIGYFVEACKLPGDKWVRCNTTPHQIpleEYTAT 19766
Cdd:COG3401     312 SAPSNVVSVTTDLTPPAAPSGLTATavgSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTT---SYTDT 385
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19767 GLEENAQYQFRAIAKTAVNISqpSEPSDPVTILAENVPP--RIELSVEMKSLLTVKAGTNVCLDATVFGKPMPTVSWKKD 19844
Cdd:COG3401     386 GLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASgeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGD 463
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19845 S---TPIKQTEGVKMAMK-RNLCTLELFSVNRKDSGDYTITAENSS---GSKSATIKLKVLDKPGPPASVKINKMYADRA 19917
Cdd:COG3401     464 TgnaVPFTTTSSTVTATTtDTTTANLSVTTGSLVGGSGASSVTNSVsviGASAAAAVGGAPDGTPNVTGASPVTVGASTG 543
                           490
                    ....*....|....*...
gi 1958765569 19918 MLSWEPPLEDGGSEITNY 19935
Cdd:COG3401     544 DVLITDLVSLTTSASSSV 561
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21477-21568 7.70e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 83.70  E-value: 7.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21477 PLPPDSLNIMDITKNTVSLAWPKPRHDGGsKITGYVIEAQRKGSDQWTHIST--VKGLECVVRNLTEGEEYTFQVMAVNS 21554
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 21555 AGRSAPRESRPVIV 21568
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
4862-4942 1.20e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.08  E-value: 1.20e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4862 IQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFT 4941
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569  4942 V 4942
Cdd:pfam07679    90 V 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1249-1337 1.51e-17

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05893:

Pssm-ID: 472250  Cd Length: 92  Bit Score: 82.84  E-value: 1.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIR-RGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05893       3 FEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQG 82
                            90
                    ....*....|
gi 1958765569  1328 NAICSGKLYV 1337
Cdd:cd05893      83 RISCTGRLMV 92
I-set pfam07679
Immunoglobulin I-set domain;
33892-33984 1.52e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 82.69  E-value: 1.52e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSqeqQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGN 33971
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS---SDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 33972 EFGSDSATVNINI 33984
Cdd:pfam07679    78 SAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29058-29141 1.58e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 1.58e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29058 PAPPRRLDVVDTSKSSAVLAWLKPEHDGGsRITSYLLEMRQKGSDFW--VEAGHTKQLTFTVERLVENTEYEFRVKAKND 29135
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 29136 AGYSEP 29141
Cdd:cd00063      80 GGESPP 85
I-set pfam07679
Immunoglobulin I-set domain;
4480-4569 2.10e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 82.31  E-value: 2.10e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAG 4559
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4560 SSSSSATVAV 4569
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17922-18011 2.29e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.54  E-value: 2.29e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17922 PGPPKDLHHVDVDKTEVSLVWNKPDRDGGsPITGYLVEYQEEGAKDWIKFKT--VKNLECVVTGLQQGKTYRFRVKAENI 17999
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 18000 IGLGLPDTTIPI 18011
Cdd:cd00063      80 GGESPPSESVTV 91
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15640-16002 2.61e-17

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 92.37  E-value: 2.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15640 VTGRPVPTKVWTIEEGELDKERVVIENVGTKSELIIKNALRKDHG---RYVITATNSCGSKFAAARVEVF---DVPGPVL 15713
Cdd:COG3401     158 TTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGttyYYRVAATDTGGESAPSNEVSVTtptTPPSAPT 237
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15714 DLKPVVTNRKMCLLNWSDPADDGgseITGFIIERKDAKMHTWRQPIETERSKCDITGLIEGQEYKFRVIAKNKFGcgppV 15793
Cdd:COG3401     238 GLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAG----N 310
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15794 EIGP--ILAVDP-LGPPTSPERLTYTERTKSTITLDWkEPRSDGGspIQGYIIEKRRHDKPDFERVNKrLCPTTSFLVDN 15870
Cdd:COG3401     311 ESAPsnVVSVTTdLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTG 386
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15871 LDEHQMYEFRVKAVNDIG-ESEPSLPlnVVIQDDEVPPTIKLRLAVRGDTIKVKAGEPVNI----PADVTGLPMPKIEWS 15945
Cdd:COG3401     387 LTPGTTYYYKVTAVDAAGnESAPSEE--VSATTASAASGESLTASVDAVPLTDVAGATAAAsaasNPGVSAAVLADGGDT 464
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 15946 KNEKVIEKPTDALNITKEEVSRSEAKTElSIPKAVREDKGTYTITASNRLGSVFRNV 16002
Cdd:COG3401     465 GNAVPFTTTSSTVTATTTDTTTANLSVT-TGSLVGGSGASSVTNSVSVIGASAAAAV 520
I-set pfam07679
Immunoglobulin I-set domain;
6729-6818 2.89e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 2.89e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6729 PSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNNAG 6808
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6809 QASCTTRLFV 6818
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5884-5973 2.95e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 2.95e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESG 5963
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5964 VERCYAFLLV 5973
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7952-8040 3.76e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.53  E-value: 3.76e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLG 8031
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  8032 TASSSAKLI 8040
Cdd:pfam07679    81 EAEASAELT 89
I-set pfam07679
Immunoglobulin I-set domain;
5229-5317 5.13e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.15  E-value: 5.13e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEVG 5308
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  5309 SSTCSARVT 5317
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29653-29744 5.34e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.39  E-value: 5.34e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29653 PGPCGKLTVSRVTEEKCTLAWSLPQEDGGaEITHYIVERRETSRLNWVIVEAECLT-LSYVVTRLIKNNEYTFRVRAVNK 29731
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 29732 YGLGVPIESEPIV 29744
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
7011-7099 6.54e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.15  E-value: 6.54e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLG 7090
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  7091 TASSTARLT 7099
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19901-19992 6.61e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 6.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19901 PGPPASVKINKMYADRAMLSWEPPlEDGGSEITNYIVDKRETSRPNWAQVSAT-VPITSCTVEKLIEGHEYQFRICAENK 19979
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 19980 YGVGDPIFTEPVI 19992
Cdd:cd00063      80 GGESPPSESVTVT 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
31440-31532 6.77e-17

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20951:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 94  Bit Score: 81.31  E-value: 6.77e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEI--IADGLKYRVQEfKGGYHQLIIASVTDDDATVYQVRAT 31517
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKIES-EYGVHVLHIRRVTVEDSAVYSAVAK 79
                            90
                    ....*....|....*
gi 1958765569 31518 NQGGSVSGTASLEVE 31532
Cdd:cd20951      80 NIHGEASSSASVVVE 94
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17822-17909 7.73e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 7.73e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17822 PGPPRDLEVSEIRKDSCYLTWKEPLDDGGSvVTNYVVERKDVATAQWSPLSTT-SKKKSHMAKHLNEGNQYLFRVAAENQ 17900
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*....
gi 1958765569 17901 YGRGPFVET 17909
Cdd:cd00063      80 GGESPPSES 88
I-set pfam07679
Immunoglobulin I-set domain;
6073-6162 1.14e-16

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 80.38  E-value: 1.14e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAG 6152
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6153 DNACSGILTV 6162
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18613-18706 1.16e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.62  E-value: 1.16e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18613 PGEPENLHIADKGKTFVYLKWRRPDYDGGsPNLSYHVERRLKGSADWERVHKGSIKETHYMVDKCVENQIYEFRVQTKNE 18692
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 18693 GGESDWVRTEEVVV 18706
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
9292-9380 1.47e-16

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.99  E-value: 1.47e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGE 9371
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDG-QPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  9372 IESNVNLQV 9380
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7387-7477 1.75e-16

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.99  E-value: 1.75e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7387 PRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDkGEVIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKNDA 7466
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  7467 GMRECSALLTV 7477
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14992-15078 1.86e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 1.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14992 PGPCKDIKASDITKSSCKLTWEPPEFDGGsPILHYVLERREAGRRTYIPVMSGE-NKLSWTVKDLIPNGEYFFRVKAVNK 15070
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 15071 IGGGEYIE 15078
Cdd:cd00063      80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15314-15405 3.96e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 3.96e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15314 PGPPINFVFEDIRKDSVLCKWEPPLDDGGsEIINYTLEKKDKtkPDSEWIVITSTLRN-CKYSVTKLIEGKEYLFRVRAE 15392
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREK--GSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|...
gi 1958765569 15393 NRFGPGPPCVSKP 15405
Cdd:cd00063      78 NGGGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15521-15607 4.12e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 4.12e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15521 RVADTSSTTIELEWEPPAfNGGGEIMGYFVDKQLVGTNEWSRCTEKMVKVRQFTVKEIREGADYKLRVSAVNAAGEGPPG 15600
Cdd:cd00063       8 RVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86

                    ....*..
gi 1958765569 15601 ETEPVTV 15607
Cdd:cd00063      87 ESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28961-29045 4.82e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.69  E-value: 4.82e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28961 PGPPGPITFKDVTRGSATLMWDAPLLDGGaRIHHYVIEKREASRRSWQVVSEK-CTRQILKVSDLTEGVPYYFRVSAENE 29039
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 29040 YGVGEP 29045
Cdd:cd00063      80 GGESPP 85
I-set pfam07679
Immunoglobulin I-set domain;
6446-6536 4.86e-16

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 78.45  E-value: 4.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKeKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDG 6525
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK-DGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  6526 GVRENMASLTV 6536
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20396-20484 6.33e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.31  E-value: 6.33e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20396 PGPVVDLKVLAVTKSSCTIGWKKPRSDGGsRITGYVVDF-LTEENKWQRVMKSLSLQYST--KDLKEGKEYTFRVSAENE 20472
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYrEKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 20473 NGEGTPSEIMVV 20484
Cdd:cd00063      80 GGESPPSESVTV 91
I-set pfam07679
Immunoglobulin I-set domain;
9671-9757 6.70e-16

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 78.07  E-value: 6.70e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9671 QFTKRIQNIVVSEHQSATFECEVSFD-DAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARlEPRG 9749
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT-NSAG 80

                    ....*...
gi 1958765569  9750 EARSTAEL 9757
Cdd:pfam07679    81 EAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24628-24719 1.11e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.54  E-value: 1.11e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24628 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGaKVKNYVIDKRESTRKAYANVSSKCSK-TSFKVENLTEGAIYYFRVMAENE 24706
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 24707 FGVGVPAETSDAV 24719
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
3019-3102 1.81e-15

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.91  E-value: 1.81e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3019 EFRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVA----GG 3093
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  3094 NMSTANLFV 3102
Cdd:pfam07679    82 AEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18809-18891 3.23e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.11  E-value: 3.23e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18809 PGPVRNLKIADVSSDRCTIRWDPPEDDGG-CEIQNYILEKCEsKRMVWSTYSANVLTPGATVTRLIEGNEYIFRVRAENK 18887
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  18888 IGTG 18891
Cdd:smart00060    80 AGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31235-31328 4.06e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.00  E-value: 4.06e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31235 PDKPTGpIVIEALLKNSVVISWKAPADDGGSwITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQN 31314
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 31315 TFGISEPLEVASVV 31328
Cdd:cd00063      79 GGGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
6824-6909 4.75e-15

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 4.75e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6824 FVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAGRD 6903
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*.
gi 1958765569  6904 SCDALV 6909
Cdd:pfam07679    83 EASAEL 88
I-set pfam07679
Immunoglobulin I-set domain;
6166-6255 4.84e-15

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 4.84e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6166 PSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTNDVG 6245
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6246 SDSCTTMLLV 6255
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8706-8790 5.82e-15

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.37  E-value: 5.82e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8706 FVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKD 8785
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*
gi 1958765569  8786 SCSAQ 8790
Cdd:pfam07679    83 EASAE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18514-18604 7.21e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 75.23  E-value: 7.21e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18514 PGPCQNLKVSNVTKENCTISWENPLDNGGsEITNFIVEYRKPNQKGWSIVASDVTKR---LIKaNLLANNEYYFRVCAEN 18590
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSEtsyTLT-GLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 18591 KVGVGPTIETKTPI 18604
Cdd:cd00063      79 GGGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
3577-3667 1.04e-14

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 1.04e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIiHNPDGSGTFIVNDPQRGDSGLYICKAENLW 3656
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV-TYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  3657 GTSTCTAELLV 3667
Cdd:pfam07679    80 GEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
4667-4753 1.35e-14

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 1.35e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4667 PSFIKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEVG 4746
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*..
gi 1958765569  4747 KCGCVAT 4753
Cdd:pfam07679    81 EAEASAE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30050-30141 1.50e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.46  E-value: 1.50e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30050 PGPCPSVNVKEVSRDSVTITWEIPTIDGGaPVNNYIIEKREAAMRAFKTVTTKCSKTL-YRISGLVEGTMYYFRVLPENI 30128
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETsYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 30129 YGIGEPCETSDAV 30141
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16940-17025 3.33e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 73.30  E-value: 3.33e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16940 KVTDWTKSSVDLEWSPPlKDGGSKITGYIVEYKEEGKEEWEKGKDKEVRGTKLVVTGLKEGAFYKFRVRAVNIAGVGEPG 17019
Cdd:cd00063       8 RVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86

                    ....*.
gi 1958765569 17020 EVTDII 17025
Cdd:cd00063      87 ESVTVT 92
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
27811-28075 3.97e-14

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 81.97  E-value: 3.97e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27811 PPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKY---ILTIENGVGQPKSSTVSVKVLDT-PAACQKLQV 27886
Cdd:COG3401     162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYyyrVAATDTGGESAPSNEVSVTTPTTpPSAPTGLTA 241
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27887 KHVSLGTVTLLWDPPlidGGSPIINYVIEKRDATKRTWSIVShKCSGTSFKVMDLSEKTPFFFRVLAENEIGI-GEPCET 27965
Cdd:COG3401     242 TADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVA-TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNV 317
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27966 TEPVKAAEVPAPIRDLSMKDSTKTSVVLSWTKPDfdgGSIITDYLVERKGKGEQAWSH-AGISKTCEIEIGQLKEQSVLE 28044
Cdd:COG3401     318 VSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKiAETVTTTSYTDTGLTPGTTYY 394
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 28045 FRVSARNEKG----QSDPVTIGPLTVKELVITPEV 28075
Cdd:COG3401     395 YKVTAVDAAGnesaPSEEVSATTASAASGESLTAS 429
I-set pfam07679
Immunoglobulin I-set domain;
9085-9175 4.46e-14

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 73.06  E-value: 4.46e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLSeTIEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATNDA 9164
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  9165 GSALCTSSIVI 9175
Cdd:pfam07679    80 GEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8141-8218 5.21e-14

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.68  E-value: 5.21e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8141 PRFIKKLdQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:pfam07679     1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2756-2839 8.81e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 72.29  E-value: 8.81e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2756 KIIKKPKDVTALENATVAFEVSVSHDTVP-VKWFHKNVEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVV----GQ 2830
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2831 LECKAKLFV 2839
Cdd:pfam07679    82 AEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
31154-31229 9.91e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 71.85  E-value: 9.91e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31154 VGSTLRLHVMYIGRPVPAMTWYHGQKLLQNSESITIENTEHYTHLVMKNVQRKtHAGKYKVQLSNVFGTVDAILDV 31229
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRS-DSGKYTLTLKNSAGEKSATINV 80
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12983-13047 1.57e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 71.38  E-value: 1.57e-13
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  12983 NLEVSEGDTIKLVCEVS-KPGAEVTWYK-GDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCR 13047
Cdd:smart00410     3 SVTVKEGESVTLSCEASgSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCA 69
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9581-9663 2.36e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 70.75  E-value: 2.36e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9581 PAWERHLQDVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTCK----HE 9655
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVatnsAG 80

                    ....*...
gi 1958765569  9656 DLETSAEL 9663
Cdd:pfam07679    81 EAEASAEL 88
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
13521-13598 5.56e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 69.54  E-value: 5.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13521 LVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTK---TVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKAEGFINLQ 13597
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgrvQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 13598 V 13598
Cdd:cd05748      82 V 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5322-5411 5.83e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 5.83e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5322 PSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAG 5401
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5402 IQRCSALLSV 5411
Cdd:pfam07679    81 EAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30743-30823 8.69e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 8.69e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30743 PEGPLEYDDIQTRSVRVSWRPPADDGG-ADILGYILERREVpKAAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFG 30821
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81

                     ..
gi 1958765569  30822 IS 30823
Cdd:smart00060    82 EG 83
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7670-7759 1.02e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 69.21  E-value: 1.02e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7670 PSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTNDAG 7749
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7750 SASCTTHLFV 7759
Cdd:pfam07679    81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12175-12258 1.39e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 68.82  E-value: 1.39e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12175 PYFTVKLHDKTGVEKDEIILKCEVSKDVP--VKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC----DCG 12248
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSAG 80
                            90
                    ....*....|
gi 1958765569 12249 TDTTKANVTV 12258
Cdd:pfam07679    81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1682-1754 1.90e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 68.44  E-value: 1.90e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  1682 FECRLTpiGDPTMVVEWLHDGKPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:pfam07679    20 FTCTVT--GTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5604-5693 1.93e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 68.44  E-value: 1.93e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5604 PYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSV-WKDDTSTiLELFSAKAADSGTYICQLSNDV 5682
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVtYEGGTYT-LTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  5683 GTTSSKATIFV 5693
Cdd:pfam07679    80 GEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7765-7852 2.67e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 2.67e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7765 FVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEAGQD 7844
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*...
gi 1958765569  7845 ICEALVSV 7852
Cdd:pfam07679    83 EASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4199-4286 3.03e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 67.67  E-value: 3.03e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4199 PTILKPLVDTISEKGDTVHLTSSISNAK--EVNWYFKGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNG 4276
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4277 KAMTSAKLTV 4286
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28571-28656 3.24e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 3.24e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28571 IRFTNITGEKMTLWWEAPLNDGcAPVTHYIIEKRETSRLAWALIE-DHCEAQSYTAIKLITGNEYQFRVSAVNKFGVGRP 28649
Cdd:cd00063       7 LRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85

                    ....*..
gi 1958765569 28650 LESDPVV 28656
Cdd:cd00063      86 SESVTVT 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1516-1607 3.61e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 67.67  E-value: 3.61e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKN-SDIIVPHKYpRIRIEGtkGEAALKIDSTISQDSAWYTATAIN 1594
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDgQPLRSSDRF-KVTYEG--GTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569  1595 KAGRDTTRCKVNI 1607
Cdd:pfam07679    78 SAGEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
11628-11719 3.83e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 3.83e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11628 KFVKEIKDIVLTEaesvGSSAIFECLVSPSTAIT-TWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRL 11706
Cdd:pfam07679     2 KFTQKPKDVEVQE----GESARFTCTVTGTPDPEvSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 11707 GNKEKTSTAKLIV 11719
Cdd:pfam07679    78 SAGEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
13065-13148 3.83e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 3.83e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13065 EFISKPQNLEILEGEKAEFVCTIS-KESFEVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVV----MVGA 13139
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSAGE 81

                    ....*....
gi 1958765569 13140 ARAAAHLTV 13148
Cdd:pfam07679    82 AEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12087-12170 5.38e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 5.38e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12087 KFISPLEDQTVKEGQTATFVCELS-HEKMHVVWFKNDVKLHTTRTVLMSSEGKTYKLEIRETTLDDISQIKAQVKN---- 12161
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsage 81

                    ....*....
gi 1958765569 12162 LSSTANLKV 12170
Cdd:pfam07679    82 AEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5423-5504 5.65e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 5.65e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5423 SIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKASI 5502
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569  5503 NV 5504
Cdd:pfam07679    89 TV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2843-2926 2.13e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 65.36  E-value: 2.13e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2843 HITKTMRNIEVPETKAASFECEVSHFNVPS-MWLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVC----GN 2917
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEvSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2918 DQVSATLTV 2926
Cdd:pfam07679    82 AEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2407-2490 3.08e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 64.97  E-value: 3.08e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2407 VITPLKDVNVIEGTKAVLECKVS---VPDVTsvkWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYKL----MV 2479
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTgtpDPEVS---WFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSA 79
                            90
                    ....*....|.
gi 1958765569  2480 GRVETSCNLSV 2490
Cdd:pfam07679    80 GEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12711-12782 7.05e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 7.05e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12711 LRPLKDVTVTAGETATFDCELS-YEDIPVEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAK 12782
Cdd:pfam07679     4 TQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT 76
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12798-12881 1.24e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20951:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 94  Bit Score: 63.21  E-value: 1.24e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12798 EFTKPLEDQTVEEEATAVLECEVSRE-NAKVKWFKNGTEI---LKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAKD- 12872
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNi 81
                            90
                    ....*....|..
gi 1958765569 12873 ---FKTSCNLNV 12881
Cdd:cd20951      82 hgeASSSASVVV 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33230-33319 1.41e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.41e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33230 PKITQSLK-AEASR-DIAKLTCAVESSALcaKEVAWYKDGKKLKENGHFQFHYSaDGTYELKIHNLSESDCGEYVCEVSG 33307
Cdd:pfam07679     1 PKFTQKPKdVEVQEgESARFTCTVTGTPD--PEVSWFKDGQPLRSSDRFKVTYE-GGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|..
gi 1958765569 33308 EGGTSKTSFQFT 33319
Cdd:pfam07679    78 SAGEAEASAELT 89
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12354-12428 1.44e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.44e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12354 FITPLSDVKVFEKDEAKFECEVSREPK-TFRWLKGTQEIAGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAEDK 12428
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
PspC_subgroup_2 super family cl41463
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11121-11427 1.65e-10

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


The actual alignment was detected with superfamily member NF033839:

Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 70.18  E-value: 1.65e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11121 PEVPKEvvPEKKVAVPKKPEVPPAKVPEVPKKPVVEEKPVIEEKPaipvaeKVESPPTEVYEEPE----EVAAQEEEPAP 11196
Cdd:NF033839    281 QDTPKE--PGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKP------QLEKPKPEVKPQPEkpkpEVKPQLETPKP 352
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11197 VVEEEeyeappppapeipvpqvPEEPKKVV---PEKKypvikkpeppppkvpEVSKKPAPMKKVPVVKKPEPPEAEVPEV 11273
Cdd:NF033839    353 EVKPQ-----------------PEKPKPEVkpqPEKP---------------KPEVKPQPETPKPEVKPQPEKPKPEVKP 400
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11274 PKKLAPVKKEPVPVTKKPEVLPEkvPEAPKkitPEKRESapvpeepeappapveeiPEETIYEEKATITIGRKETPPvee 11353
Cdd:NF033839    401 QPEKPKPEVKPQPEKPKPEVKPQ--PEKPK---PEVKPQ-----------------PEKPKPEVKPQPEKPKPEVKP--- 455
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 11354 reierfiQPEEPGMEPQPE-ETPVQEPEPEKKVIEKPKLKPRPPIRAPSPPKEDVKEKIFQLKAVSKKKVPEKPE 11427
Cdd:NF033839    456 -------QPETPKPEVKPQpEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNKPK 523
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
13336-13419 2.23e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 2.23e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13336 EFVEHLEDQTVTEFDDAVFSCQLS-REKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVEDR--- 13411
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*....
gi 1958765569 13412 -KSRARLFV 13419
Cdd:pfam07679    82 aEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12442-12525 2.53e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 2.53e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12442 KFLTPLKDVTAKERENAVFTVELSHDNIP-VSWFKNDQRLHTSKRVSMHDEGKTHSITFKDLSIDDTSQIRVEAMGI--- 12517
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*....
gi 1958765569 12518 -SSEAKLTV 12525
Cdd:pfam07679    82 aEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2136-2222 3.49e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 3.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2136 FTQELQDVVAKEKDTmATFECETS-EPFVKVKWYKDGIEVHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSCVlVEDE-- 2212
Cdd:pfam07679     3 FTQKPKDVEVQEGES-ARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV-ATNSag 80
                            90
                    ....*....|
gi 1958765569  2213 NIKTTAKLIV 2222
Cdd:pfam07679    81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2931-3013 4.24e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 61.50  E-value: 4.24e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2931 ITSMLKDINAEEKDTITFEVTVnyEG---ISYKWLKNGVEIKSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVA----G 3003
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTV--TGtpdPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaG 80
                            90
                    ....*....|
gi 1958765569  3004 KATSTATLYV 3013
Cdd:pfam07679    81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12530-12614 4.99e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20972:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 91  Bit Score: 61.44  E-value: 4.99e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12530 PYFTGKLQDYTGVEKDEVVLQCEISKADAP-VKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC----DCG 12604
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPvVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSClatnSVG 81
                            90
                    ....*....|
gi 1958765569 12605 TDQTSGKLDI 12614
Cdd:cd20972      82 SDTTSAEIFV 91
PTZ00121 super family cl31754
MAEBL; Provisional
10032-10560 1.83e-09

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 1.83e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10032 RRMEEEKV--QVTKVPEVSKKIVPQKPSRTPVQEEII----EVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKK 10105
Cdd:PTZ00121   1218 RKAEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIrkfeEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10106 TvtEEKIHVAVSKKIEPPPKVPEPPKKPVPEEVVPVPIPKKVEPPAVKVPEAPKKPVPEEKKPVPIPKKEPAA------- 10178
Cdd:PTZ00121   1298 A--EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekkkee 1375
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10179 PPKVPEAPKKPAPEEKTAVPVAKKKEAPPPKVTEVQKKVVTEEKITIIPQREESPPPAvpEIPKKKVPEEKRP--VPRKE 10256
Cdd:PTZ00121   1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKAdeAKKKA 1453
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10257 EVPPPKAPPKKPVPEEVVPVPIPKKAPP--RAEVSKKTVVEEKKFAAEERLSMAVPQRVELMRHEEEEWTYSEEEEqvsv 10334
Cdd:PTZ00121   1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---- 1529
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10335 svyreEERDEEEAEITEYEVLEEPEEYVVEEKLHVISKRVEVEPAKVPEKHEKKIIPRPKVPAKIEEPPPTKVPEPPKKm 10414
Cdd:PTZ00121   1530 -----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE- 1603
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10415 vPEKKVPAPPPKKVPPAKAPEEPKKPVPERRVPAEVVEIEEPPPTKvTEKHMKITQEEKVLVAVTKKEEPPRARVPEEPK 10494
Cdd:PTZ00121   1604 -EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 10495 KVVPEEKFPKLKPRREEEPPAKVTEVRKRAVKEEKVSIEVPKREprPTKEVTVTEEKKwsytREEE 10560
Cdd:PTZ00121   1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE--EENKIKAEEAKK----EAEE 1741
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2582-2664 2.16e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 59.58  E-value: 2.16e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2582 ISKPLTDQTVAESQEAVFECEV-ANPESEGEWLKDGKHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYTYKVATS---- 2656
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVtGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSagea 82

                    ....*...
gi 1958765569  2657 KTSAKLKV 2664
Cdd:pfam07679    83 EASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12887-12958 2.22e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20951:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 94  Bit Score: 59.74  E-value: 2.22e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12887 EFLRPLTDLQVKEKETARFECEIS-KENVKVQWFKDGAEI---KKGKKYDIISKGAVRILVINKCLLNDEAEYSCE 12958
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAV 77
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
13153-13241 4.11e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 58.81  E-value: 4.11e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13153 RIVVPLKDTKVKEQQEAVFNCEVntEGA---KAKWFRNDEAIFDSSKYIILQKDLVYTLRIRDARLDDQANFSVSLTNHR 13229
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTV--TGTpdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|..
gi 1958765569 13230 GEnVKSAANLIV 13241
Cdd:pfam07679    80 GE-AEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2494-2577 4.81e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 58.81  E-value: 4.81e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2494 KIIRGLRDLTCTETQNVVFEVELS-HSGIDVVWNFKGQEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGEYAFYA----GE 2568
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2569 NTTSGKLTV 2577
Cdd:pfam07679    82 AEASAELTV 90
PTZ00121 super family cl31754
MAEBL; Provisional
32984-33612 6.31e-09

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.93  E-value: 6.31e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32984 ASQRRDEEVPKSVFPELTKTEAYAISSFKRTSEMEAASSVRevKSQMTETRESLSSYEHHVSAEMKSAASEEKSLEEkat 33063
Cdd:PTZ00121   1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR--KAEEVRKAEELRKAEDARKAEAARKAEEERKAEE--- 1216
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33064 VRKIKTTLAARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTA-KYKSTFEISSVQASDEGN 33142
Cdd:PTZ00121   1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKKKADEAK 1296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33143 YSVVVENTD---GKQEAQFTLTVQKAKAVEKAVTSPPRVKSPEPRVKSPETVKSPKRVKSPELVASHPKAVSPTETKPTE 33219
Cdd:PTZ00121   1297 KAEEKKKADeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33220 KGQqlpVPAPPKitqslKAEASRDIAKLTCAVESSALCAKEVAWYKDGKKLKEnghfqfhysadgtyELKihnlsesdcg 33299
Cdd:PTZ00121   1377 KKK---ADAAKK-----KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD--------------EAK---------- 1424
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33300 eyvceVSGEGGTSKTSFQFTGQSFKSIHEQVSSTTETKKSVQKTAESAEAKKATQKTAESAEAKKATQKTAESAEAKKPA 33379
Cdd:PTZ00121   1425 -----KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33380 QKTAESAEAKKPAQKTAEPTEAKKQEPIAPESVSSKpvivtglrdttvsSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQS 33459
Cdd:PTZ00121   1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK-------------ADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33460 SKYKLSNDKEEFIL---EILKtetsdgglyscTVANSAGSVSSSCKLTIKAVKDTEAQKVSTQKTSEVTAKKKESVQQEI 33536
Cdd:PTZ00121   1567 EEAKKAEEDKNMALrkaEEAK-----------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
                           570       580       590       600       610       620       630
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33537 SQKVLTSEEikmsEVKSHETLAIKEEASKVLIAEEVKKSAAASLEKSIVHEEVTKTSQASEEVKTHAEIKALSTQM 33612
Cdd:PTZ00121   1636 EQLKKKEAE----EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
13247-13330 1.12e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 57.65  E-value: 1.12e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13247 RIIEPLKDIETMEKKSVTFWCKVN---RLNVTlkWTKNGEEVAFDNRISYRIDKYKHSLIIKDCGFPDEGEYIVTA---- 13319
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtpDPEVS--WFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsa 79
                            90
                    ....*....|.
gi 1958765569 13320 GQDKSVAELLI 13330
Cdd:pfam07679    80 GEAEASAELTV 90
PspC_subgroup_2 super family cl41463
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10808-11022 2.28e-08

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


The actual alignment was detected with superfamily member NF033839:

Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 63.25  E-value: 2.28e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10808 PPAKVPEIPKKPEEKVSVPVPKKEKAPPAKVPEvPKKPVPEEKAPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKkv 10887
Cdd:NF033839    292 PSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQ-LEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQ-- 368
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10888 eaPPAKAPEVPPKEVTPEKKVPvvppkkpeapppkvpeppkevvpekkvsmvppKRPEAPPAKV---PEASK-EVVPE-- 10961
Cdd:NF033839    369 --PEKPKPEVKPQPETPKPEVK--------------------------------PQPEKPKPEVkpqPEKPKpEVKPQpe 414
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10962 -KKVSVAPKKKPEAPAVK-VPEAPKKVV---PEKKVPVAAPkKPEAPAAEV---PEVPKAAV-PQKKIPE 11022
Cdd:NF033839    415 kPKPEVKPQPEKPKPEVKpQPEKPKPEVkpqPEKPKPEVKP-QPETPKPEVkpqPEKPKPEVkPQPEKPK 483
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
28080-28152 8.32e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.88  E-value: 8.32e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 28080 IPGAQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDN 28152
Cdd:pfam13927     6 VSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9498-9578 1.66e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 54.19  E-value: 1.66e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9498 IENQTVLKDNDAIFEIDIkINYPEIKLSWYKGTEKLEPSNKYEITINGDRHTLRVRNCQLKDQGNYRLVC----GPHIAS 9573
Cdd:pfam07679     7 PKDVEVQEGESARFTCTV-TGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGEAEAS 85

                    ....*
gi 1958765569  9574 AKLTV 9578
Cdd:pfam07679    86 AELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2228-2312 1.74e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 54.19  E-value: 1.74e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2228 EFVKELQDIEVPESYSGELECIIS--PEnIEGKWYHNDVELKSNGKYSITSRRGRQNLTVKDVTKEDQGEYCFVV--DGK 2303
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtPD-PEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnSAG 80

                    ....*....
gi 1958765569  2304 KTTCKLKMK 2312
Cdd:pfam07679    81 EAEASAELT 89
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33612-33689 2.18e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 53.80  E-value: 2.18e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33612 MNITSGQRVTLKANIAGATD--VKWVLNGTELSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCIGKTSQGVVKCQFDLT 33689
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
THB super family cl39704
Tri-helix bundle domain; This domain can be found in the myosin-binding motif (m-domain) ...
9414-9444 5.31e-07

Tri-helix bundle domain; This domain can be found in the myosin-binding motif (m-domain) region present in myosin-binding protein C (MyBP-C). MyBP-C is a sarcomeric assembly protein necessary for the regulation of sarcomere structure and function. The MyBP-C family of proteins consists mainly of modules with immunoglobulin (Ig) or fibronectin folds. This domain exhibits a three-helix bundle fold and there is a known actin-binding motif, LK(R/K)XK positioned in the third helix (alpha3), similar to that found in villin and related proteins.


The actual alignment was detected with superfamily member pfam18362:

Pssm-ID: 465725  Cd Length: 34  Bit Score: 51.20  E-value: 5.31e-07
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1958765569  9414 DIMELLKNVDPKEYEKYARMYGITDFRGLLQ 9444
Cdd:pfam18362     1 DVWEILSNAPPKDYEKIAFQYGITDLRGMLK 31
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2668-2752 8.72e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 52.26  E-value: 8.72e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2668 KIKKTLRNLTVTETQDAIFSVELT-HPDVKgVQWIKNGVVLDSNDKYEISVKGTLYSLKIKNCAMADESVYGFK----LG 2742
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPE-VSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVatnsAG 80
                            90
                    ....*....|
gi 1958765569  2743 RLGASARLHV 2752
Cdd:pfam07679    81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12264-12347 1.23e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12264 KVEKPLYGVEVFVGETARFEIELS---EPDVhgQWKLKGEPLTASPDCEIIEDGKKHVLVLYNCQLDMTGEVSFQAAN-- 12338
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtpDPEV--SWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsa 79
                            90
                    ....*....|.
gi 1958765569 12339 --AKSAANLKV 12347
Cdd:pfam07679    80 geAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12000-12082 1.29e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12000 FAVPLKDVTVPEKRQARFECVLT--REANVIWSKGPDIIKASDKFDIIADGKKHILVINDSQFDDEGVYT--AEVEGKKT 12075
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTgtPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTcvATNSAGEA 82

                    ....*..
gi 1958765569 12076 SAQLFVT 12082
Cdd:pfam07679    83 EASAELT 89
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2317-2388 1.67e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05744:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 91  Bit Score: 51.34  E-value: 1.67e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2317 AILQGLSDQKVCEGDIVQLEVKVS-LENVEGVWMKDGQEVQHSDRVHIVIDKQ-SHMLLIEDMTKEDAGNYSFT 2388
Cdd:cd05744       2 HFLQAPGDLEVQEGRLCRFDCKVSgLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCI 75
Titin_Z pfam09042
Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like ...
463-505 2.48e-06

Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. This interaction is essential for sarcomere assembly.


:

Pssm-ID: 462662  Cd Length: 43  Bit Score: 49.50  E-value: 2.48e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958765569   463 QKQMRKEAEKTAVTKVVVAADKAKEQELRLRTREEIITKQEQT 505
Cdd:pfam09042     1 QEKVREEDEKTAVSTVVVAVDKAKVLEPVSKSEEEIAAEQEQE 43
PspC_subgroup_2 super family cl41463
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11286-11617 2.77e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


The actual alignment was detected with superfamily member NF033839:

Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 56.32  E-value: 2.77e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11286 PVTKKPEVLPEKVPEAPKKITPEKRESAPVPEEPEAPPAPVEEIPEETIYEEKATITIGRKETPPVEEREIERFIQPEEP 11365
Cdd:NF033839    172 PTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNV 251
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11366 GMEPQPEETPVQEPEPEKKVIEKPKL-----KPRPPI-RAPSPPKEDVKekifqlkavSKKKVPEKPEVVEKVEPTPLKV 11439
Cdd:NF033839    252 NTKVEIENTVHKIFADMDAVVTKFKKgltqdTPKEPGnKKPSAPKPGMQ---------PSPQPEKKEVKPEPETPKPEVK 322
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11440 PTAEKKVrkllPEPKPQPKEEvvlKSVLRKRPEEEEPKVEPKKVEKVKKPEEPPPPPKAVEVEAPPEPKPKERKVPEPTK 11519
Cdd:NF033839    323 PQLEKPK----PEVKPQPEKP---KPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPK 395
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11520 vPEIKPAIPLPGPEPKPKPEPevktmKAPPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKPK-GPIKGVAKKTPSP-IE 11597
Cdd:NF033839    396 -PEVKPQPEKPKPEVKPQPEK-----PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvKPQPETPKPEVKPqPE 469
                           330       340
                    ....*....|....*....|
gi 1958765569 11598 AERKKLRPGSGGEKPPDEAP 11617
Cdd:NF033839    470 KPKPEVKPQPEKPKPDNSKP 489
PTZ00121 super family cl31754
MAEBL; Provisional
433-679 7.75e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 7.75e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   433 DMARVREPVISAVEQTAQRTTTTAVHVQPAQKQMRKEAEKTAVTKVVVAADKAKEQ---------ELRLRTREEIITKQE 503
Cdd:PTZ00121   1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieevmklyEEEKKMKAEEAKKAE 1616
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   504 QTHIAHEQIRKETEkafVPKVVISATKAKEQETRITGEITTKQEQKRITQETITK----ETRKTVVPKVIVATPKIKEQD 579
Cdd:PTZ00121   1617 EAKIKAEELKKAEE---EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEA 1693
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   580 VVSRSREAitTKRDQVQITQEKKRKETE----TTALSTIAVATTKAKEQETVLRSREAMTTRQEHIQVTHGKVGVGKKAE 655
Cdd:PTZ00121   1694 LKKEAEEA--KKAEELKKKEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
                           250       260
                    ....*....|....*....|....
gi 1958765569   656 AVATVVAAVDQARVREPREPRHVE 679
Cdd:PTZ00121   1772 EIRKEKEAVIEEELDEEDEKRRME 1795
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
11732-11802 1.66e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.66e-05
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  11732 EEVTVVKGQPLYLSCELNKERD--VVWRKDGKIVVEKPGRIVPGVIGLMRALTINDADDTDAGTYTVTVENAN 11802
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPpeVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS 74
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
15203-15310 1.74e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 48.35  E-value: 1.74e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15203 VKRGDEIALDATISGSPYPTITWIKDENVIVPeeikkrvappvrrkkgeaeeeepftlplTERLSINNSKQgESQLRVRD 15282
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKE----------------------------TGRVQIETTAS-STSLVIKN 54
                            90       100
                    ....*....|....*....|....*...
gi 1958765569 15283 SLRPDHGQYMIKVENDHGVAKAPCTVSV 15310
Cdd:cd05748      55 AKRSDSGKYTLTLKNSAGEKSATINVKV 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3113-3193 3.39e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20967:

Pssm-ID: 472250  Cd Length: 82  Bit Score: 47.62  E-value: 3.39e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3113 KKEVQVIEKQRAVVEFEVNEDDVDAHWYKDGIEINFQVEERHQYVVERRihRMFISEARHSDAGEYTFVAGRNRSSVTLY 3192
Cdd:cd20967       4 QPAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKR--TLTVQQASLADAGEYQCVAGGEKCSFELF 81

                    .
gi 1958765569  3193 V 3193
Cdd:cd20967      82 V 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
13425-13507 7.12e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 46.87  E-value: 7.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13425 EIIRPPQDILEAPGADVIFLAELNKDKV-EVQWLRNNMIVVQGDKHQMMSEGKIHRLQICDIKPRDQGEYRFIAKDK--- 13500
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*...
gi 1958765569 13501 -EARAKLE 13507
Cdd:pfam07679    82 aEASAELT 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
11825-11889 2.75e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.19  E-value: 2.75e-04
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  11825 RDQHVKPKGTAVFTCHI-AKDTPNIKWFKGYDEiPLEPNDKTEILKEGNHLILKVKNAMPEDIDEY 11889
Cdd:smart00410     2 PSVTVKEGESVTLSCEAsGSPPPEVTWYKQGGK-LLAESGRFSVSRSGSTSTLTISNVTPEDSGTY 66
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12620-12703 4.88e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 44.56  E-value: 4.88e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12620 KLVRPLYSVEVMETETARFETEISED-DIHANWKLKGEALLQTPECEIKEEGKIHVLILHNCRLDQTGGVDFQAAN---- 12694
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsage 81

                    ....*....
gi 1958765569 12695 VKSSAHLRV 12703
Cdd:pfam07679    82 AEASAELTV 90
 
Name Accession Description Interval E-value
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
31762-32038 1.41e-175

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 543.30  E-value: 1.41e-175
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14104       1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14104      81 VDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLKPGDKFRLQYT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKE 32001
Cdd:cd14104     161 SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKE 240
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1958765569 32002 RKSRMTASEALKHPWLKQRMDRVSTKVIRTLRHRRYY 32038
Cdd:cd14104     241 RKSRMTAQEALNHPWLKQGMETVSSKDIKTTRHRRYY 277
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
31763-32017 7.41e-76

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 256.30  E-value: 7.41e-76
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:smart00220     1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRerILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                             90       100       110       120       130       140       150       160
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31841 GLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLLF 31920
Cdd:smart00220    81 GGDLFDLLKKRGR-LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD--EDGHVKLADFGLARQLDPGEKLTTFV 157
                            170       180       190       200       210       220       230       240
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31921 TAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETN-QQMIENIMNAEYTFDEEaFQEISLEAMDFIDRLLV 31999
Cdd:smart00220   158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPP-EWDISPEAKDLIRKLLV 236
                            250
                     ....*....|....*...
gi 1958765569  32000 KERKSRMTASEALKHPWL 32017
Cdd:smart00220   237 KDPEKRLTAEEALQHPFF 254
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
32081-32170 6.69e-56

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 192.56  E-value: 6.69e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32081 PVSGQIMHAIGEEGGYVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYG 32160
Cdd:cd20927       1 PVSGQIMHAVGEEGGHVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYG 80
                            90
                    ....*....|
gi 1958765569 32161 EDSSYAELFV 32170
Cdd:cd20927      81 EDSSYAELFV 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
33070-33161 2.33e-53

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 185.25  E-value: 2.33e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33070 TLAARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVEN 33149
Cdd:cd05747       1 TLPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVEN 80
                            90
                    ....*....|..
gi 1958765569 33150 TDGKQEAQFTLT 33161
Cdd:cd05747      81 SEGKQEAQFTLT 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6-98 1.99e-48

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 171.00  E-value: 1.99e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNG 85
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569    86 SGQATSTAELLVT 98
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
103-193 3.04e-45

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 161.98  E-value: 3.04e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   103 PPNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSV 182
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569   183 GRATSTADLLV 193
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
18713-18806 8.54e-42

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 152.12  E-value: 8.54e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18713 PVLDLKLSGVLtVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATN 18792
Cdd:cd20974       1 PVFTQPLQSVV-VLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569 18793 PAGSFVAYATVNVL 18806
Cdd:cd20974      80 GSGQATSTAELLVL 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2038-2129 1.81e-39

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 145.64  E-value: 1.81e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERS--DRIYWYWPEDNVCELVIRDVTAEDSASIMVKAIN 2115
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSsiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  2116 IAGETSSHAFLLVQ 2129
Cdd:cd20951      81 IHGEASSSASVVVE 94
Pkinase pfam00069
Protein kinase domain;
31763-32017 6.24e-39

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 148.93  E-value: 6.24e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV---KGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:pfam00069     1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKekiKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSaFELNEREVVSYVRQVCEALEflhsqnighfdirpeniiYQTRKNSIIkiiefgqarqlkpGDnfrll 31919
Cdd:pfam00069    81 EGGSLFDLLSEK-GAFSEREAKFIMKQILEGLE------------------SGSSLTTFV-------------GT----- 123
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 ftaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEaFQEISLEAMDFIDRLLV 31999
Cdd:pfam00069   124 ---PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLK 199
                           250
                    ....*....|....*...
gi 1958765569 32000 KERKSRMTASEALKHPWL 32017
Cdd:pfam00069   200 KDPSKRLTATQALQHPWF 217
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
14277-14730 9.48e-34

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 143.99  E-value: 9.48e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14277 AVNVCGRATAVVEVNVLDKPGPPAAFdITDVTNESCLLTWNPPRDDGGSKITNYVVERKATDSDVWHKLSSTVKDTNfka 14356
Cdd:COG3401     121 AVGTATTATAVAGGAATAGTYALGAG-LYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGG--- 196
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14357 TKLTPNKEYIFRVAAENmyGVGEPVQATPIIAKYQFDPPGPPTRLEPSDITKDAVTLTWcepDDDGGSPITGYWVERLDP 14436
Cdd:COG3401     197 GDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW---DPVTESDATGYRVYRSNS 271
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14437 DTDKWVRCNKmpVKDTTYRVKGLTNKKKYRFRVLAENLAGpgKPSRSTEPILIKDPIDPPWPPGKPTVKDIGKTSLVLNW 14516
Cdd:COG3401     272 GDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW 347
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14517 TKPEhdgGAKIESYVIEMLKTGTDDWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKAG-ESEPSEPSDPvlcrEKLYP 14595
Cdd:COG3401     348 TASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSA----TTASA 420
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14596 PSPPRWLEVINITKNTADLKWTVPEKDGGSPITNYIVEKRDVRRKGWQTVDTTVKDtkcTVTPLTEGSLYVFRVAAENAI 14675
Cdd:COG3401     421 ASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSST---VTATTTDTTTANLSVTTGSLV 497
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 14676 GQSDYTEIGDSVLAKDTFTTPGPPYALTVVDVTKRHVDLKWEPPKNDGGRPIQRY 14730
Cdd:COG3401     498 GGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVS 552
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
22668-22749 1.94e-33

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 127.71  E-value: 1.94e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22668 TFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNV 22747
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22748 IV 22749
Cdd:cd05748      81 KV 82
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
31756-32013 2.10e-33

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 140.53  E-value: 2.10e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31756 TKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV----LVKKEISILNIARHRNILYLHESFESMEE 31831
Cdd:COG0515       2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPeareRFRREARALARLNHPNIVRVYDVGEEDGR 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqtRKNSIIKIIEFGQARQLK 31911
Cdd:COG0515      82 PYLVMEYVEGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL--TPDGRVKLIDFGIARALG 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFR---LLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISL 31988
Cdd:COG0515     159 GATLTQtgtVVGT-PGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPP 237
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31989 EAMDFIDRLLVKERKSR-MTASEALK 32013
Cdd:COG0515     238 ALDAIVLRALAKDPEERyQSAAELAA 263
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
21297-21376 6.29e-33

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 126.55  E-value: 6.29e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21297 TLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKH--RANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVNV 21374
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 21375 RV 21376
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
20503-20584 2.98e-32

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 124.62  E-value: 2.98e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20503 CYLAKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSI 20582
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 20583 KV 20584
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
23463-23542 8.83e-31

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 120.39  E-value: 8.83e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23463 VINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDA--AIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTV 23540
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgrVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 23541 RV 23542
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
24546-24624 1.28e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 119.62  E-value: 1.28e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24546 IVVRAGGSARIHIPFKGRPTPEITWSKEEGEF--TDKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVK 24623
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 24624 V 24624
Cdd:cd05748      82 V 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
28878-28957 2.04e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 119.23  E-value: 2.04e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28878 THIVRAGASIRLFIAYQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFTV 28955
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 28956 KV 28957
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
21587-21667 1.48e-29

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 116.92  E-value: 1.48e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITIQ 21666
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 21667 V 21667
Cdd:cd05748      82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
13617-13962 4.16e-29

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 129.35  E-value: 4.16e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13617 EVSLAWEEPLTDGGSKIIGYVVER-RDIKRKTWVLVTDRADSCEFTVTGLQKGGVEYLFRVSARNRVGTGEPvetDSPVE 13695
Cdd:COG3401     149 GVDGANASGTTASSVAGAGVVVSPdTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP---SNEVS 225
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13696 ARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEYDGgaeITNYVIELRDKTSIRWDTAMTVRaeDLSATVTDVVEGQEYSF 13775
Cdd:COG3401     226 VTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTYYY 300
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13776 RVRAQNriGVGKPSAATPFVKVADPIERPSPPVNLSASEQTQSSVQLTWEPPLkdgGSPILGYIIERQEEGKDNWIRCNm 13855
Cdd:COG3401     301 RVTAVD--AAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIA- 374
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13856 KPVPELTYKVTGLQKGNKYLYRVSAENAAGV-SDPSEILGPLTADDASVEPTMDLSAFKDGLEVIVPNPIKILVPSTGYp 13934
Cdd:COG3401     375 ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGV- 453
                           330       340
                    ....*....|....*....|....*...
gi 1958765569 13935 rpKATWTFGDQVLEAGDRVKIKTISAYA 13962
Cdd:COG3401     454 --SAAVLADGGDTGNAVPFTTTSSTVTA 479
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
27793-27874 9.10e-29

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 114.61  E-value: 9.10e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27793 VIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGqPKSSTVSV 27872
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG-EKSATINV 80

                    ..
gi 1958765569 27873 KV 27874
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28619-28996 2.03e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 127.43  E-value: 2.03e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28619 EAQSYTAIKLITGNEYQFRVSAVNKFGVGRPleSDPVVAQIQYTIPDAPGIPEPSNVTGNSITLTWTRPESDGgneIQHY 28698
Cdd:COG3401     190 TTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGY 264
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28699 ILERREKKSTRWVKVISkrpISETRFKVTGLVEGNEYEFHVMAENAAGVGpaSGISRLIKCREPVNPPSAPAVVKVTDTS 28778
Cdd:COG3401     265 RVYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGNE--SAPSNVVSVTTDLTPPAAPSGLTATAVG 339
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28779 KTTVSLEWArPVFDGGmeIIGYIIEMCKADLGDWHKVnTEPCVKTRYTVTDLQAGEEYKFRVSAINGAGK--GDSCEVTG 28856
Cdd:COG3401     340 SSSITLSWT-ASSDAD--VTGYNVYRSTSGGGTYTKI-AETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesAPSEEVSA 415
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28857 TIKAVDR---LSAPELDIDANFKQTHIVRAGASIR-LFIAYQGRPTPTAVWSKPDSNLSIraDIHTTDSFSTLTVENCNR 28932
Cdd:COG3401     416 TTASAASgesLTASVDAVPLTDVAGATAAASAASNpGVSAAVLADGGDTGNAVPFTTTSS--TVTATTTDTTTANLSVTT 493
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 28933 NDAGKYTLTVENNSGRKSITFT---VKVLDSPGPPGPITFKDVTRGSATLMWDAPLLDGGARIHHYV 28996
Cdd:COG3401     494 GSLVGGSGASSVTNSVSVIGASaaaAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
13874-14373 6.52e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.89  E-value: 6.52e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13874 YLYRVSAENAAGVSDPSEILGPLTADDASVEPTMDLSAFKDGLEVIVPNPIKILVPSTGYPRPKATWTFGDQVLEAGDRV 13953
Cdd:COG3401     101 GSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAV 180
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13954 KIKTISAYAELIISPSERPDKGI-YTLTL----ENPVKSISGEIDVNVIAR-PSAPKELKFSDVTKDSVHLTWEPPDDDG 14027
Cdd:COG3401     181 ATTSLTVTSTTLVDGGGDIEPGTtYYYRVaatdTGGESAPSNEVSVTTPTTpPSAPTGLTATADTPGSVTLSWDPVTESD 260
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14028 gspLTGYVVEKRDMSRKTWTKVmDFVTDLEFTVPDLVQGKEYLFKVCARNKCGpGEPAYTDEpVNMSAPATVPDPPENVK 14107
Cdd:COG3401     261 ---ATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYYRVTAVDAAG-NESAPSNV-VSVTTDLTPPAAPSGLT 334
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14108 WRDRTANSIFLTWDPPKNDGgsrIKGYIVEKCPRGSDKWVACGEPVPDTKMEVTGLEEGKWYAYRVKALNRQGASkpSKP 14187
Cdd:COG3401     335 ATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAP 409
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14188 TEEIQAVDTQEAPEIFLD-----VKLLAGLTVKAGTKIELPATVTGK---PEPKITWTKADTLLRPDQRITIENVP--KK 14257
Cdd:COG3401     410 SEEVSATTASAASGESLTasvdaVPLTDVAGATAAASAASNPGVSAAvlaDGGDTGNAVPFTTTSSTVTATTTDTTtaNL 489
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14258 STVTITDSKRSDTGTYIIEAVNVCGRATAVVeVNVLDKPGPPAAFDITDVTNESCLLTWNPPRDDGGSKITNYvverkat 14337
Cdd:COG3401     490 SVTTGSLVGGSGASSVTNSVSVIGASAAAAV-GGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSV------- 561
                           490       500       510
                    ....*....|....*....|....*....|....*.
gi 1958765569 14338 dSDVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAEN 14373
Cdd:COG3401     562 -SGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVH 596
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29967-30046 6.74e-28

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 111.91  E-value: 6.74e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29967 TVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLAN--RAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLV 30044
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 30045 KV 30046
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27520-27928 9.72e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.11  E-value: 9.72e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27520 TSRVVWSMVAENLEECIITTTKIIKGNEYIFRVRAVNKYGIGEPleSEPVVAKNSFVTPGPPSIPEVTKITKNSMTVVWN 27599
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27600 RPTVDGgseINGYFLEKRDKKSLAWLKVlkETIRDTRQKVTGLTENSDYQYRVCAVNAAGMGpfSEPSDFYKAADPIDPP 27679
Cdd:COG3401     255 PVTESD---ATGYRVYRSNSGDGPFTKV--ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE--SAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27680 GPPAKIRIADSTKSSITLGWSKPvydGGSDVTGYVVEMRQGEEEEWTIVSTkgEARTTEYVVSNLKPGVNYYFQVSAVNC 27759
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAE--TVTTTSYTDTGLTPGTTYYYKVTAVDA 402
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27760 AGQGEPitMTEPVQAKDILEEPEIDLDvalrTSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSiqNTDSSS 27839
Cdd:COG3401     403 AGNESA--PSEEVSATTASAASGESLT----ASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAV--PFTTTS 474
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27840 LLVIPQVTRNDTGKYILTIENGVGQPKSSTVSVKVLDTPAACQKLQVKHVSLGTVTLLWDPPlidggSPIINYVIEKRDA 27919
Cdd:COG3401     475 STVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPV-----TVGASTGDVLITD 549

                    ....*....
gi 1958765569 27920 TKRTWSIVS 27928
Cdd:COG3401     550 LVSLTTSAS 558
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
24832-24913 1.10e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 111.53  E-value: 1.10e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24832 TYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSV 24911
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 24912 IV 24913
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30301-30640 1.25e-27

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.11  E-value: 1.25e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30301 THTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKVVILDKPGPPIGPIKIDEVDATSVTISWEPP-ELDGGAPLSGY 30379
Cdd:COG3401      90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGtTASSVAGAGVV 169
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30380 VVEQRDAHRPGWLPVSESVTRPTFKFT-RLTEGNEYVFRVAATNRFGIGSYlqSEVIECRSSISIPGPPETLQIFDISRD 30458
Cdd:COG3401     170 VSPDTSATAAVATTSLTVTSTTLVDGGgDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPG 247
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30459 GMTLTWYPPEDDGgsqVTGYIIERKEVRADRWVRVNKVpvTMTRYRSTGLIEGLEYEHRVTAINARGTgkPSRPSKP-TV 30537
Cdd:COG3401     248 SVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVvSV 320
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30538 AMDPIaPPGKPQNPRVTDTTRTSVSLAWSVPEDEGgskVTGYLIEMQKVDQREWTKCNTTPTKIrEYTLTHLPQGAEYRF 30617
Cdd:COG3401     321 TTDLT-PPAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTT-SYTDTGLTPGTTYYY 395
                           330       340
                    ....*....|....*....|....
gi 1958765569 30618 RVLACNAGGP-GEPAEVPGTVKVT 30640
Cdd:COG3401     396 KVTAVDAAGNeSAPSEEVSATTAS 419
I-set pfam07679
Immunoglobulin I-set domain;
7107-7196 1.49e-27

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 111.20  E-value: 1.49e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVG 7186
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7187 KDMCSAQLSV 7196
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
20532-21039 1.70e-27

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 124.34  E-value: 1.70e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20532 EDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKVVGKPGIPTGPIKFDEVTAEAMTLKWGP 20611
Cdd:COG3401      91 ATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVV 170
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20612 PKDDGGSEITNYVLEKRDSVNNKWVTcasavqkttfrvTRLHEGIEYTFRVSAENKygVGEGLKSEPIVAKHPFDVPDAP 20691
Cdd:COG3401     171 SPDTSATAAVATTSLTVTSTTLVDGG------------GDIEPGTTYYYRVAATDT--GGESAPSNEVSVTTPTTPPSAP 236
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20692 PPPNIVDVRHDSVSLTWTDPKKTGgspITGYHIEFKERNSLLWKRANKTpiRMKDFKVTGLTEGLEYEFRVMAINLAGVg 20771
Cdd:COG3401     237 TGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGN- 310
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20772 kPSLPSEPVVALDPIDPPGKPEVISVTR---NSVTLIWTEPKYDGghkLTGYIVEKRDLPSKSWMKANHVnVPDCAFTVT 20848
Cdd:COG3401     311 -ESAPSNVVSVTTDLTPPAAPSGLTATAvgsSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAET-VTTTSYTDT 385
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20849 DLVEGGKYEFRIRAKNTAGAISAPSE----STGTIICKDEYEAPTIVLDPTIKDGLTVKAGDSIVLSAISILGKPLPKSS 20924
Cdd:COG3401     386 GLTPGTTYYYKVTAVDAAGNESAPSEevsaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20925 WSKAGKDIRPSDIAQITSTPTSSMLTVKYAT--RKDAGEYTITATNPFGTKEEhVKVSVLDVPGPPGPIEISNVSAEKAT 21002
Cdd:COG3401     466 NAVPFTTTSSTVTATTTDTTTANLSVTTGSLvgGSGASSVTNSVSVIGASAAA-AVGGAPDGTPNVTGASPVTVGASTGD 544
                           490       500       510
                    ....*....|....*....|....*....|....*..
gi 1958765569 21003 LTWTPPLEDGGSPIKAYVLEKRETSRLLWTVVSEDIQ 21039
Cdd:COG3401     545 VLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSL 581
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
17045-17124 2.04e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 110.76  E-value: 2.04e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17045 RIVVHAGGVIRIIAYVSGKPPPTVTWNMNERAL--PQEATIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIV 17122
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 17123 DV 17124
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25356-25768 2.58e-27

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 123.96  E-value: 2.58e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25356 TSRLSWTQVSTEVQALNYKVTKLLPGNEYIFRVMAVNKYGVGEPleSEPVIACNPYKLPGPPSTPEASAITKDSMVLTWT 25435
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25436 rPVDDGGAeiEGYILEKRDKEGIRWTKCNkkTLTDLRFRVTGLTEGHSYEFRVAAENAAgvGEPSEPSVFYRACDALYPP 25515
Cdd:COG3401     255 -PVTESDA--TGYRVYRSNSGDGPFTKVA--TVTTTSYTDTGLTNGTTYYYRVTAVDAA--GNESAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25516 GPPSNPKVTDTSRSSVSLAWNKPiydGGAPVRGYVIELKEAAADEWTTCTppSGLQGKQFTVTKLKENTEYNFRICAFNT 25595
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ETVTTTSYTDTGLTPGTTYYYKVTAVDA 402
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25596 EGVGEPATIPGSVVAQermEAPEIELDADLRKVVTLRASATLRLFVTIKGRPEPEVKWEKAEGILTERAQIEVTSSYTML 25675
Cdd:COG3401     403 AGNESAPSEEVSATTA---SAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA 479
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25676 VIDNVTRFDSGRYNLTLENNSGSKTAFVNVRVLDSPSAPVNLTVREvkKDSVTLSWEPPLIDGGAKVTNYIVEKRETTRK 25755
Cdd:COG3401     480 TTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPD--GTPNVTGASPVTVGASTGDVLITDLVSLTTSA 557
                           410
                    ....*....|...
gi 1958765569 25756 AYATITNNCTKTT 25768
Cdd:COG3401     558 SSSVSGAGLGSGN 570
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26707-26786 2.60e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 110.37  E-value: 2.60e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26707 TLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDL--RTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTFVV 26784
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 26785 KV 26786
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26437-26819 6.68e-27

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 122.80  E-value: 6.68e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26437 TSRLAWTICEAELRTTSCKVTKLLKGNEYIFRVTGVNKYGVGEPleSVAVKALDPFTTPSPPTSLEITSVTKDSMTLCWS 26516
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26517 RPEtdgGSDISGYIIERREKNSLRWMRVNKkpVYDLRVKSTGLREGCEYEYRVFAENAAGLslPSDTSPLVRAEDPVFLP 26596
Cdd:COG3401     255 PVT---ESDATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26597 SPPSKPKIVDSGKTTITIGWVKPLfdgGAPITGYTVEYKKSEETDWKVAIQSFRGTEYTMSGLTTGAEYVFRVRSLNKVG 26676
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26677 -ASDPSDITDPQVAkereeePAFDVDSEMRKTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRTSLT 26755
Cdd:COG3401     405 nESAPSEEVSATTA------SAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT 478
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 26756 IENANRNDSGKYTLTIQNVLSAASMTFVVKVLDSPGPPANITVREVTKETAVLSWDVPENDGGA 26819
Cdd:COG3401     479 ATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAST 542
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26997-27078 1.07e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 108.45  E-value: 1.07e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26997 TVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTFINI 27076
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 27077 IV 27078
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
8989-9078 1.69e-26

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 108.50  E-value: 1.69e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVG 9068
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  9069 KDSCTAQLNI 9078
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8797-8886 2.09e-26

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 108.11  E-value: 2.09e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVG 8876
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8877 EVSSSTFLTV 8886
Cdd:pfam07679    81 EAEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3199-3289 3.64e-26

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 107.51  E-value: 3.64e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLL---STGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKN 3275
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  3276 DYGVATTSASLSVE 3289
Cdd:cd20951      81 IHGEASSSASVVVE 94
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
16331-16420 4.86e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.91  E-value: 4.86e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16331 CLICKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKamkdgihdIPEDAQLETAENSSVIVIPECTRAHSGKYSITAKNKAG 16410
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLK--------ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG 72
                            90
                    ....*....|
gi 1958765569 16411 QKTANCRVKV 16420
Cdd:cd05748      73 EKSATINVKV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
25628-25707 5.68e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.52  E-value: 5.68e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25628 VVTLRASATLRLFVTIKGRPEPEVKWEKAEGIL--TERAQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVNV 25705
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 25706 RV 25707
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
19128-19207 6.13e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.52  E-value: 6.13e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVR-KGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVK 19206
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19207 V 19207
Cdd:cd05748      82 V 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
22381-22460 6.89e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.13  E-value: 6.89e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22381 VVTIRACCTLRLFVPIKGRPAPEVKWAREHGESLD--KASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFVNV 22458
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22459 RV 22460
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
7294-7382 7.92e-26

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 106.57  E-value: 7.92e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVG 7373
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  7374 SDTCACTVK 7382
Cdd:pfam07679    81 EAEASAELT 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22109-22355 9.09e-26

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 118.95  E-value: 9.09e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22109 TSRLAWTNVATEVQVTKLKVTKLLKGNEYIFRVMAVNKYGVGEPleSEPVLAVDPYGPPDPPKNPEVTTITKDSMVVCWg 22188
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW- 253
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22189 hpDSDGGSEIINYIVERRDKAGQRWVKCNkkALTDLRFKVSGLTEGHEYEFRIMAENAAGV-SAPSATSPFYKacdSVFK 22267
Cdd:COG3401     254 --DPVTESDATGYRVYRSNSGDGPFTKVA--TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTT---DLTP 326
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22268 PGPPGNPRVLDTSRSSISIAWNKPiydGGSEITGYMVEIALPEEDEWQVVTPPagLKATSYTITNLIENQEYKIRIYAMN 22347
Cdd:COG3401     327 PAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET--VTTTSYTDTGLTPGTTYYYKVTAVD 401

                    ....*...
gi 1958765569 22348 SEGLGEPA 22355
Cdd:COG3401     402 AAGNESAP 409
I-set pfam07679
Immunoglobulin I-set domain;
6-97 1.26e-25

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 105.80  E-value: 1.26e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTStlPGVQISFSDGRARLMIPAVTKANSGRYSLRATNG 85
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS--DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                            90
                    ....*....|..
gi 1958765569    86 SGQATSTAELLV 97
Cdd:pfam07679    79 AGEAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
30658-30736 1.58e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 105.36  E-value: 1.58e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30658 VFVRQGGVIRLTIPIKGKPFPICKWTKEGQDV--SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVK 30735
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 30736 V 30736
Cdd:cd05748      82 V 82
I-set pfam07679
Immunoglobulin I-set domain;
33074-33162 1.63e-25

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 105.42  E-value: 1.63e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33074 RILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGK 33153
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569 33154 QEAQFTLTV 33162
Cdd:pfam07679    82 AEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
21651-21963 2.12e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.80  E-value: 2.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21651 TAKNTVGEVGDVITIQVHDIPGPPTGPIKFDEVSSDFVTFSWEPPENDGGVPISNYVVEMR--QTDSTTWVELATTVIRT 21728
Cdd:COG3401     113 SSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDtsATAAVATTSLTVTSTTL 192
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21729 TYKATRLTTGVEYQFRVKAQNryGVGPGITSASVVANYPFKVPGPPGTPQVTAVTKDSMTISWHEPLSDGgspILGYHIE 21808
Cdd:COG3401     193 VDGGGDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVY 267
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21809 RKERNGILWQTVSKalVPGNIFKSTGLTDGIAYEFRVIAENMAGKskPSKPSEPTFALDPIDPPGKPVPLNITRHT---V 21885
Cdd:COG3401     268 RSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGsssI 343
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 21886 ALKWAKPEYTGgfkITSYVVEKRDLPNGRWLKANfSNILENEFTVSGLTEDAAYEFRVIAKNAAGAISPPSEPSDAIT 21963
Cdd:COG3401     344 TLSWTASSDAD---VTGYNVYRSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATT 417
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29708-30085 2.89e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.41  E-value: 2.89e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29708 TLSYVVTRLIKNNEYTFRVRAVNKYGLGVPieSEPIVARNSFTIPSQPGIPEGVGAGKEHIIIQWTKPESDGgneISNYL 29787
Cdd:COG3401     191 TLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYR 265
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29788 VDKREKKSLRWTRVNKdyvVYDTRLKVTSLMEGCDYQFRVTAVNSAGNsePSEASNFISCREPSYTPGPPSAPRVVDTTK 29867
Cdd:COG3401     266 VYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGS 340
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29868 SSISLAWTKPMydgGTDIIGYVLEMQEKDTDQWCRVHTntTIRNNEFTVPDLKMGQKYSFRVAAVNAKGmsDYSETTAEI 29947
Cdd:COG3401     341 SSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAE--TVTTTSYTDTGLTPGTTYYYKVTAVDAAG--NESAPSEEV 413
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29948 EpVERLEIPDLELADDLKKTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDKVNRYDAGKY 30027
Cdd:COG3401     414 S-ATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVT 492
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 30028 TIEAENQSGKKSATVLVKVYDTPGPCPSVNVKEVSRDSVTITWEIPTIDGGAPVNNYI 30085
Cdd:COG3401     493 TGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDL 550
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
23064-23145 3.08e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 104.59  E-value: 3.08e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23064 TVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNV 23143
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 23144 KV 23145
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
27393-27474 6.51e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 103.44  E-value: 6.51e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27393 VVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRV 27472
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 27473 QI 27474
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
30259-30340 6.64e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 103.44  E-value: 6.64e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30259 TIHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKV 30338
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 30339 VI 30340
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22729-23136 8.55e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 8.55e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22729 HYTVKLTNSAGEATETLNVIVLDK---PGPPTGpVKMDEVTADSVTLSWEPPKydgGSSINNYIVEKRDTSTTAWQIVsA 22805
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVTTPttpPSAPTG-LTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKV-A 280
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22806 TVARTTIKASRLKTGCEYQFRIAAENRYG-KSTYlnSEPVIAQYPFKVPGPPGTPFVTLASKDSMEVQWhEPVSDGGsrV 22884
Cdd:COG3401     281 TVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP--SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--V 355
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22885 IGYHLERKERNSILWVKLNKTpIPQTKFKTTGLEEGIEYEFRVSAENIVGIGkpSKPSECYAAH--DPCDPPGRPEAIIV 22962
Cdd:COG3401     356 TGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATtaSAASGESLTASVDA 432
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22963 TRNSVTLQWKKPTYDGGSKITGYVVEKKELPDGRWmkasfTNIIDTQFEVTGLIEDHRYEFRVIARNAAGVFSEPSESTG 23042
Cdd:COG3401     433 VPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA-----VPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23043 AITARDEVEPPrISMDPKYKDTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVD 23122
Cdd:COG3401     508 SVSVIGASAAA-AVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTS 586
                           410
                    ....*....|....
gi 1958765569 23123 SGNYILKAKNVAGE 23136
Cdd:COG3401     587 TNTNDVAGVHGGTL 600
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17444-17715 1.00e-24

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 1.00e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17444 SWKPPLDDGGSEITNYIIEKKELGKDIWMPVTSASAKTTCKV---------PKLLEGKDYIFRIHAENLYGISDPlvSDS 17514
Cdd:COG3401     146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVtsttlvdggGDIEPGTTYYYRVAATDTGGESAP--SNE 223
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17515 MKARDRFRVPDAPEQPVVTEVTKDSALVTWNKPNDGGkpITNYILEKRETMSKRWVRVTKEPihpYTKYRVPDLLEGCQY 17594
Cdd:COG3401     224 VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSGDGPFTKVATVT---TTSYTDTGLTNGTTY 298
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17595 EFRVSAENEIGIgdPSPPSKPVFARDPIAKPSPPINPEAIDTTCNSVDLTWQPPrhdGGSKILGYIVEYQKVGDEEWRRA 17674
Cdd:COG3401     299 YYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKI 373
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 17675 NHTPEscpETKYKVTGLRDGQTYKFRVLAVNEAG-ESDPAHV 17715
Cdd:COG3401     374 AETVT---TTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEE 412
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24787-25210 1.03e-24

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 1.03e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24787 LSSGQEYQFRVKAYNEKGKSDPRVLGVPVIAKDLTIQPSFKLPFNTYSVQAGeDLKIEIPVIGRPRPKISWVKDGEPLRQ 24866
Cdd:COG3401       6 LTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLV-AAGLSSGGGLGTGGRAGTTSGVAAVAV 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24867 TTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVIVLEKPGPPVGPVKFDEVSADFVVISWEPPAYTGG 24946
Cdd:COG3401      85 AAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVA 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24947 C-QISNYIVEKRDTTTTNWQMVSATVArTTIKVSKLKTGTEYQFRIFAENRYGKSTPldSKPVVVQYPFKEPGPPGTPFV 25025
Cdd:COG3401     165 GaGVVVSPDTSATAAVATTSLTVTSTT-LVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTA 241
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25026 TSVSKDQMLVQWhEPVNDGGskVIGYHLEQKEKNSILWVKLNKIpiQDTKFKTTGLDEGLEYEFRVSAENIVGI-GKPSK 25104
Cdd:COG3401     242 TADTPGSVTLSW-DPVTESD--ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSN 316
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25105 VSECYVARDPCDPPGRPEAIIITRNSVTLKWKKPTydgGSKITGYIVEKKDLPDGRWMKASFTnVVETEFTVTGLVEDQR 25184
Cdd:COG3401     317 VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTT 392
                           410       420
                    ....*....|....*....|....*.
gi 1958765569 25185 YEFRVIARNAADNFSEPSESSGAITA 25210
Cdd:COG3401     393 YYYKVTAVDAAGNESAPSEEVSATTA 418
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26310-26391 1.84e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 102.28  E-value: 1.84e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26310 VIVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNC 26389
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 26390 KV 26391
Cdd:cd05748      81 KV 82
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
31780-32018 1.91e-24

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 108.79  E-value: 1.91e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31780 CVETSSKKTFMAKFVKV-----KGTDQVLVKKEISILN-----------IARHRNILYLHESFESMEELVMIFEFISGLD 31843
Cdd:PHA03390     16 CEIVKKLKLIDGKFGKVsvlkhKPTQKLFVQKIIKAKNfnaiepmvhqlMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGD 95
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSIIKIIEFGQARQLKpgdnfrllftAP 31923
Cdd:PHA03390     96 LFDLLKKEGK-LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY-DRAKDRIYLCDYGLCKIIG----------TP 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31924 -------EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFlAETNQQMIE-NIMNAEYTFDEEAFQEISLEAMDFID 31995
Cdd:PHA03390    164 scydgtlDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPF-KEDEDEELDlESLLKRQQKKLPFIKNVSKNANDFVQ 242
                           250       260
                    ....*....|....*....|....
gi 1958765569 31996 RLLVKERKSRMTA-SEALKHPWLK 32018
Cdd:PHA03390    243 SMLKYNINYRLTNyNEIIKHPFLK 266
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
25915-25996 4.74e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 101.13  E-value: 4.74e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25915 TFNVKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITV 25994
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 25995 IV 25996
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
6915-6996 5.54e-24

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 101.18  E-value: 5.54e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIG 6994
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ..
gi 1958765569  6995 TA 6996
Cdd:pfam07679    81 EA 82
I-set pfam07679
Immunoglobulin I-set domain;
900-989 1.04e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 100.41  E-value: 1.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAG 979
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569   980 TVSTSCYLAV 989
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26998-27452 1.20e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 112.40  E-value: 1.20e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26998 VYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGT---TKTFI 27074
Cdd:COG3401     146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGEsapSNEVS 225
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27075 NIIVLDRPGPPTGpVAISDITEESVTLKWEPPKydgGSHVTNYIVLKRETSTAVWTEVsATVARTMIKVMKLTTGEEYQF 27154
Cdd:COG3401     226 VTTPTTPPSAPTG-LTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYY 300
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27155 RIKAENRFGI-SDhiDSACVVVKLPYTTPGPPSTPWVSNVTRESITVGWhEPVSNGGsaVIGYHLEMKDRNSILWQKANK 27233
Cdd:COG3401     301 RVTAVDAAGNeSA--PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAE 375
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27234 MIiRTTHFKVTTISAGLIYEFRVYAENAAGIGkpSHSSEPVLAIDAcePPRNVRITDISKNSVNLSWQQPAFDGGSKITG 27313
Cdd:COG3401     376 TV-TTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTA--SAASGESLTASVDAVPLTDVAGATAAASAASN 450
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27314 YIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAVGSVSNpSEVVGPITCIDSYGGPVIDLPLEYTEV 27393
Cdd:COG3401     451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGA-SSVTNSVSVIGASAAAAVGGAPDGTPN 529
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 27394 VKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNS 27452
Cdd:COG3401     530 VTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTN 588
I-set pfam07679
Immunoglobulin I-set domain;
5697-5787 1.37e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 100.02  E-value: 1.37e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDA 5776
Cdd:pfam07679     1 PKFTQKPKDVEV-QEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  5777 GTASCSIELKV 5787
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19211-19297 1.70e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 99.88  E-value: 1.70e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19211 PGPVSDLKVSDVTKTSCHVSWAPPENDGGsPVTHYIVEKREAERKTWSTV-TPEVKKTSFNVTNLVPGNEYFFRVTAVNE 19289
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 19290 YGPGVPTD 19297
Cdd:cd00063      80 GGESPPSE 87
I-set pfam07679
Immunoglobulin I-set domain;
8048-8137 1.92e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 99.64  E-value: 1.92e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAG 8127
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8128 KDSCSAQLGV 8137
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
3305-3391 2.10e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 99.64  E-value: 2.10e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3305 PAIVTPLQDAVTSEGRPARFQCQVSGT-DLKVSWYCRDKKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAVG 3383
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*...
gi 1958765569  3384 QVSSTATL 3391
Cdd:pfam07679    81 EAEASAEL 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29169-29249 2.55e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.82  E-value: 2.55e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29169 ITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLKETDRMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITVV 29248
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 29249 V 29249
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22167-22259 3.42e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 99.11  E-value: 3.42e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22167 PDPPKNPEVTTITKDSMVVCWGHPDSDGGsEIINYIVERRDKAGQRWVKCNKKALTDLRFKVSGLTEGHEYEFRIMAENA 22246
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 22247 AGVSAPSATSPFY 22259
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18046-18507 3.62e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.86  E-value: 3.62e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18046 IRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLTVLDVPGPPTGPINi 18125
Cdd:COG3401      80 AAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGT- 158
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18126 ldvtpeymTISWQPPKDDGGSPVINYIVEKQDTrkgtwgVVSAGSSKLKLKVPHLQKGCEYVFRVKAENKMGVGPPLDSI 18205
Cdd:COG3401     159 --------TASSVAGAGVVVSPDTSATAAVATT------SLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEV 224
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18206 PTVAKHkfSPPSPPGKPVVTDITENAATVSWTLPKSDGgspITGYYVERREIT-GKWVRVNKTpiADLKFRVTGLYEGNT 18284
Cdd:COG3401     225 SVTTPT--TPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGdGPFTKVATV--TTTSYTDTGLTNGTT 297
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18285 YEFRVFAENLAGlsNPSPSSDPIKACRPIKPPGPPINPKLKDKTKESADLVWTKPLSdggSPILGYVVECQKPGTTQWDR 18364
Cdd:COG3401     298 YYYRVTAVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD---ADVTGYNVYRSTSGGGTYTK 372
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18365 INkdELIRQCAFRVPGLIEGNEYRFRIRAANIVGEgEPRELAESVIAKDILHPPEVELDVTCRDVITVRVGQTIRILARv 18444
Cdd:COG3401     373 IA--ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAA- 448
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 18445 kgrpEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:COG3401     449 ----SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
I-set pfam07679
Immunoglobulin I-set domain;
3461-3550 3.65e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 98.87  E-value: 3.65e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYG 3540
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  3541 RAVCSAHLKV 3550
Cdd:pfam07679    81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
31549-31630 4.14e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.43  E-value: 4.14e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31549 VHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFGIDQKTVEL 31628
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKN-AKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 31629 DV 31630
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
104-193 4.48e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 98.48  E-value: 4.48e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVG 183
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569   184 RATSTADLLV 193
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16015-16314 4.75e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.48  E-value: 4.75e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16015 NLAVTDIKAESCYLTWDAPLDNGGSEITHYIIDKRDASRKKSEWEEVTNTAVerrygiwkLIPNGQYEFRVRAVNKYGTS 16094
Cdd:COG3401     147 LYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGD--------IEPGTTYYYRVAATDTGGES 218
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16095 DEckSDKVVIQDPYRLPGPPGKPKVLERTKGSMLVSWTPPLDNGgspITGYWLEKREEGGAYWSRVSRapitkvgLKGVE 16174
Cdd:COG3401     219 AP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT-------VTTTS 286
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16175 FSVPRLIEGVKYQFRAMAINAAGIgpPSEPSDPAVAGDPIYPPGPPSCPEVKDKTKSSISLAWKPPAkdgGSPIKGYIVE 16254
Cdd:COG3401     287 YTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVY 361
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 16255 MQEEGTTDWKKVNEpdkLLTACECVVPNLKELRKYRFRVKAVNEAG-ESEPSDTTGEIPAT 16314
Cdd:COG3401     362 RSTSGGGTYTKIAE---TVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTAS 419
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
20214-20295 6.36e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.05  E-value: 6.36e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20214 TLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIVV 20293
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 20294 KV 20295
Cdd:cd05748      81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
13804-13891 8.46e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 97.95  E-value: 8.46e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13804 PSPPVNLSASEQTQSSVQLTWEPPlKDGGSPILGYIIERQEEGKDNWIRCNMKPVPELTYKVTGLQKGNKYLYRVSAENA 13883
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 13884 AGVSDPSE 13891
Cdd:cd00063      80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24331-24421 8.54e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 97.95  E-value: 8.54e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24331 PGPPKSLEVTNIAKDSMTVCWNRPDSDGGsEIIGYIVEKRDRSGIRWIKCNKRRITDLRLRVTGLTEDHEYEFRVSAENA 24410
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 24411 AGVGEPSPATV 24421
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15415-15507 9.41e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 97.95  E-value: 9.41e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15415 PDAPDKPIVDDVTSNSMVVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKALLSSLKTKVDGLLEGLTYVFRVCAENAA 15494
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|...
gi 1958765569 15495 GPGKFSPPSDPKT 15507
Cdd:cd00063      81 GESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
6541-6629 9.75e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.71  E-value: 9.75e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6541 VIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGK 6620
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  6621 SSCTAVVDV 6629
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7856-7945 1.21e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.33  E-value: 1.21e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVG 7935
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7936 AVASSAVLVI 7945
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
4949-5038 1.40e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.33  E-value: 1.40e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVG 5028
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5029 SKDSRGALIV 5038
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25868-26388 2.16e-22

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 108.55  E-value: 2.16e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25868 SGLTAGEEYVFRVAAVNEKGRSDPRQLGVPVVAKDIEIKPSVELPFNTFNVKANDQL--KIDIPFKGRPQATVAWKKDGQ 25945
Cdd:COG3401      11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLgtGGRAGTTSGVAAVAVAAAPPT 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25946 VLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIVLDrpgPPGPIRIDEVSCDNVSISWTPPEY 26025
Cdd:COG3401      91 ATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYAL---GAGLYGVDGANASGTTASSVAGAG 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26026 DGGCQISNYIVEKRETTSTTWQVVsqavarTSIKIVRLTTGSEYQFRVCAENRYGKSSYSESSAVVaeYPFSPPGPPgTP 26105
Cdd:COG3401     168 VVVSPDTSATAAVATTSLTVTSTT------LVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVT--TPTTPPSAP-TG 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26106 KVVHATKSTMV-VSWQvPVNDGGsqVIGYHLEYKERSSILWSKANKVliADTQMKVSGLDEGLLYEYRVYAENIAGIGkc 26184
Cdd:COG3401     239 LTATADTPGSVtLSWD-PVTESD--ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNE-- 311
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26185 SKACEPVPARDPCDPPGQPE---VTNITRKSVSLKWSKPrydGGAKITGYIVERRELPDGRWLKCNFTnVQETYFEVTEL 26261
Cdd:COG3401     312 SAPSNVVSVTTDLTPPAAPSgltATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGL 387
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26262 TEDQRYEFRVFARNAADSVSEPSE----STGPITVKDDVEAPRIMMDvkfrdvivVKAGEVLKINADIAGRPLPVISWAK 26337
Cdd:COG3401     388 TPGTTYYYKVTAVDAAGNESAPSEevsaTTASAASGESLTASVDAVP--------LTDVAGATAAASAASNPGVSAAVLA 459
                           490       500       510       520       530
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 26338 DGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVN 26388
Cdd:COG3401     460 DGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
I-set pfam07679
Immunoglobulin I-set domain;
33698-33787 3.04e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 96.17  E-value: 3.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRG 33777
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 33778 QCSATASLTV 33787
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7577-7666 3.59e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 96.17  E-value: 3.59e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAG 7656
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7657 QDESSALLTV 7666
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17524-17613 5.01e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 95.64  E-value: 5.01e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17524 PDAPEQPVVTEVTKDSALVTWNKPNDGGKPITNYILEKRETMSKRWVRVTKEPIhPYTKYRVPDLLEGCQYEFRVSAENE 17603
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 17604 IGIGDPSPPS 17613
Cdd:cd00063      80 GGESPPSESV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
20882-21397 5.33e-22

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 107.40  E-value: 5.33e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20882 KDEYEAPTIVLDPTIKDGLTVKAGDSIVLSAISILGKPLPkssWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGE 20961
Cdd:COG3401      34 KTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRA---GTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTG 110
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20962 YTITATNPFGTKEEHVKVSVLDVPGPP--------GPIEISNVSAEKATLTWTPPLEDGGSPIKAYVLEKRETSRLLWTV 21033
Cdd:COG3401     111 LTSSDEVPSPAVGTATTATAVAGGAATagtyalgaGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTST 190
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21034 VSEDiqacrhVVTKLIQGNEYLFRVSAVNhyGKGEPVQSEPVKMVDRFGPPGPPGKPEISNVTKNTATVSWkRPIDDGGs 21113
Cdd:COG3401     191 TLVD------GGGDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW-DPVTESD- 260
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21114 eITGYHVERREKKGLRWVRATKTPVSDLRckVTGLQEGNTYEFRVSAENRAGIgpPSDASNPVLMKDVAYPPGPPSNAHV 21193
Cdd:COG3401     261 -ATGYRVYRSNSGDGPFTKVATVTTTSYT--DTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTA 335
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21194 TDTTKKSASLAWGKPHydgGLEITGYVVEHQKVGDDAWIKdtTGTALRITQFVVPDLQTKEKYNFRISAVNDAGVgEPAV 21273
Cdd:COG3401     336 TAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTK--IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAP 409
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21274 IPNVEIVEKETAPDFELDAElrrTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKHRANIENTESFTLLIIPECNRYD 21353
Cdd:COG3401     410 SEEVSATTASAASGESLTAS---VDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTT 486
                           490       500       510       520
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 21354 TGKFVMTIENPAGkkSGFVNVRVLDTPGPVLNLRPTDITKDSVT 21397
Cdd:COG3401     487 ANLSVTTGSLVGG--SGASSVTNSVSVIGASAAAAVGGAPDGTP 528
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29569-29649 5.35e-22

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 95.35  E-value: 5.35e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29569 VTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMVK 29648
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 29649 V 29649
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16829-16926 5.63e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 95.64  E-value: 5.63e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16829 PGAPDKPTVSSVTRNSMTVNWEEPEYDGGsPVTGYWLEMKDTTSKRWKRVNRDPIKAMtlgvSYKVTGLIEGSDYQFRVY 16908
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSET----SYTLTGLKPGTEYEFRVR 75
                            90
                    ....*....|....*...
gi 1958765569 16909 AINAAGVGPASLPSDPVT 16926
Cdd:cd00063      76 AVNGGGESPPSESVTVTT 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
899-989 8.44e-22

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 94.96  E-value: 8.44e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd20972      81 GSDTTSAEIFV 91
I-set pfam07679
Immunoglobulin I-set domain;
31053-31132 9.87e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.63  E-value: 9.87e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31053 DVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29242-29649 1.15e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 106.24  E-value: 1.15e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29242 TFTITVVVIGRPGPVTGPIEVSSVSAESCVLSWSEPKDDGGTEITNYIVEKRESGTTAWQLINSSVKRTQIKVTHLT--K 29319
Cdd:COG3401     122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDieP 201
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29320 YKEYCFRVSSENRFGVSKPLESVPIVAehPFVPPSAPTRPEVYYVSANAMSIRWEEPYHDGgskIVGYWVEKKERNTILW 29399
Cdd:COG3401     202 GTTYYYRVAATDTGGESAPSNEVSVTT--PTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPF 276
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29400 VKENKVPclECNYKVTGLVEGLEYQFRTYALNAAGV-SKASEASRPIMAQNPVDPPGRPEVTDVTRSTVSLVWSAPMydg 29478
Cdd:COG3401     277 TKVATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS--- 351
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29479 GSKVVGYIIERkpvSEVGDGRWLKCNyTIVSDNFFTVTALSEGDTYEFRVLAKNAAGIISKGSEstgPVTCRDEYAPPKA 29558
Cdd:COG3401     352 DADVTGYNVYR---STSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSE---EVSATTASAASGE 424
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29559 ELDARLQGDLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNAS 29638
Cdd:COG3401     425 SLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASS 504
                           410
                    ....*....|.
gi 1958765569 29639 GTKSVSVMVKV 29649
Cdd:COG3401     505 VTNSVSVIGAS 515
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27281-27374 1.21e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.49  E-value: 1.21e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27281 EPPRNVRITDISKNSVNLSWQQPAFDGGsKITGYIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAV 27360
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 27361 GsVSNPSEVVGPIT 27374
Cdd:cd00063      81 G-ESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19211-19293 1.23e-21

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 94.22  E-value: 1.23e-21
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19211 PGPVSDLKVSDVTKTSCHVSWAPPENDGG-SPVTHYIVEKREaERKTWSTVTPEVKKTSFNVTNLVPGNEYFFRVTAVNE 19289
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  19290 YGPG 19293
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
33416-33505 1.26e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.63  E-value: 1.26e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAG 33495
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 33496 SVSSSCKLTI 33505
Cdd:pfam07679    81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
19420-19500 1.32e-21

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 94.19  E-value: 1.32e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19420 ITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKIKVT 19499
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19500 V 19500
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31337-31430 1.39e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.49  E-value: 1.39e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31337 PSVPGKPTITAVTKDSCVVAWKPPASDGGaKIRNYYLEKREKKQNKWIAVTTEEIRETVFSVQNLIEGLEYEFRVKCENL 31416
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 31417 GGESEWSETSEPVT 31430
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
4292-4381 1.43e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 1.43e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYG 4371
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4372 SVSCTATLTV 4381
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5511-5600 1.62e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 1.62e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAG 5590
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5591 HSQCSGHLTV 5600
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30785-31145 1.76e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 105.47  E-value: 1.76e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30785 AAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFGISKPlkseEPVIPKTPLNPPEPPSNPPEVLDVTKSSVSLSWSR 30864
Cdd:COG3401     180 VATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP----SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDP 255
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30865 PKDDGgsrVTGYYIERKETSTDKWVRHNKTqiTTTMYTVTGLVPDAEYQFRIIAQNDVGlsETSPASEPVVCKDPFDKPS 30944
Cdd:COG3401     256 VTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLTPPA 328
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30945 QPGELEILSISKDSVILQWEKPEcdgGKEILGYWVEYRQSGDSAWKKSNKErIKDRQFTIGGLLEATEYEFRVFAENETG 31024
Cdd:COG3401     329 APSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31025 L-SRPRRTAMSVKTKLTSGEAPGVRKemADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLT 31103
Cdd:COG3401     405 NeSAPSEEVSATTASAASGESLTASV--DAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT 482
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 31104 VMTEEQEDEGVYTCVATNEVGEVETSSKLLLQAAPQFHPGYP 31145
Cdd:COG3401     483 DTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAP 524
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14496-14584 1.90e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.10  E-value: 1.90e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14496 PWPPGKPTVKDIGKTSLVLNWTKPEHDGGaKIESYVIEMLKTGTDDWVRVAEGVPT-TEHLLTGLMEGQEYSFRVRAVNK 14574
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 14575 AGESEPSEPS 14584
Cdd:cd00063      80 GGESPPSESV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30545-30632 2.09e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.10  E-value: 2.09e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30545 PGKPQNPRVTDTTRTSVSLAWSVPEDEGGsKVTGYLIEMQKVDQREWTKCNTTPTKIREYTLTHLPQGAEYRFRVLACNA 30624
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 30625 GGPGEPAE 30632
Cdd:cd00063      80 GGESPPSE 87
I-set pfam07679
Immunoglobulin I-set domain;
8235-8325 2.35e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.86  E-value: 2.35e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVG 8314
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|.
gi 1958765569  8315 SDTCvgSVTLK 8325
Cdd:pfam07679    81 EAEA--SAELT 89
I-set pfam07679
Immunoglobulin I-set domain;
7200-7290 2.56e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.48  E-value: 2.56e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDtSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGV 7279
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  7280 GHASCSTALKV 7290
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28766-28855 2.67e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 93.72  E-value: 2.67e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28766 PSAPAVVKVTDTSKTTVSLEWARPVFDGGmEIIGYIIEMCKADLGDWHKVNTEPCVKTRYTVTDLQAGEEYKFRVSAING 28845
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 28846 AGKGDSCEVT 28855
Cdd:cd00063      80 GGESPPSESV 89
I-set pfam07679
Immunoglobulin I-set domain;
3199-3288 3.63e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.09  E-value: 3.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYG 3278
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  3279 VATTSASLSV 3288
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8893-8981 3.63e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.09  E-value: 3.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPIG 8972
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  8973 SASSSAKLI 8981
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16424-16516 4.02e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 93.33  E-value: 4.02e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16424 PGPPKDLKVSDITRGSCRLSWKMPDDDGGDrIKGYVIEKKTIDGKAWTKVNPNCGS-TAFVVPDLISEQQYFFRVRAENR 16502
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 16503 FGIGPPAETIQRTT 16516
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16217-16308 4.30e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.30e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16217 PGPPSCPEVKDKTKSSISLAWKPPaKDGGSPIKGYIVEMQEEGTTDWKKVNEPDklLTACECVVPNLKELRKYRFRVKAV 16296
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTP--GSETSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|..
gi 1958765569 16297 NEAGESEPSDTT 16308
Cdd:cd00063      78 NGGGESPPSESV 89
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
23751-23830 4.38e-21

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 92.65  E-value: 4.38e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23751 YSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIEII 23830
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20299-20390 4.56e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.56e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20299 PGPPVNVTVKEISKDSAYITWDPPIiDGGSPIINYVVEKRDAERKSWSTVTTECPK-TSFRVSNLEEGKSYFFRVFAENE 20377
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 20378 YGIGDPGETRDAV 20390
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22952-23045 4.74e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.74e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22952 DPPGRPEAIIVTRNSVTLQWKKPTYDGGsKITGYVVEKKELPDGRWMKASFTNIIDTQFEVTGLIEDHRYEFRVIARNAA 23031
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 23032 GVfSEPSESTGAIT 23045
Cdd:cd00063      81 GE-SPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28119-28450 4.77e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 104.31  E-value: 4.77e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28119 SEYVRFSKTENKITLSIKNVKKENGGKYTVIL----DNAVCRNSFPITIITLG-PPSKPKGpIRFDEIKADSAIMSWDIP 28193
Cdd:COG3401     178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVaatdTGGESAPSNEVSVTTPTtPPSAPTG-LTATADTPGSVTLSWDPV 256
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28194 EDDGggeITCYSIEKREASQTNWKMVcSSVARTTFKVSNLVKDSEYQFRVRAENRYGV-SEPlvSNVIVAKHQFRIPGPP 28272
Cdd:COG3401     257 TESD---ATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAP--SNVVSVTTDLTPPAAP 330
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28273 GKPVIYNVTSDGMSLTWDAPvydGGSEVTGFHVEKKERNSILWQRVNTSpISGREYRATGLIEGLDYQFRVYAENSAGLS 28352
Cdd:COG3401     331 SGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNE 406
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28353 SPSDPSKFTLAVSPVDPPGTPDYIDVTRETITLKWNPPLRDGGSKIVAYSIEKRQGSDRWVrcnFTDVSECQYTVSGLSP 28432
Cdd:COG3401     407 SAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA---VPFTTTSSTVTATTTD 483
                           330
                    ....*....|....*...
gi 1958765569 28433 GDRYEFRIIARNAVGTIS 28450
Cdd:COG3401     484 TTTANLSVTTGSLVGGSG 501
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20000-20092 4.78e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.78e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20000 PGRCDPPVISNITKDHMTVSWKAPADDGGsPITGYLVEKRETQAVNWTKVNRKPVIERTLKATGLQEGTEYEFRVTAINK 20079
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 20080 AGPGKPSDASKAV 20092
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
8611-8700 5.26e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 5.26e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAG 8690
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8691 RASCTTQLFV 8700
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5978-6066 5.63e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 5.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5978 QIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGS 6057
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  6058 SSCDAYLRV 6066
Cdd:pfam07679    82 AEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16371-16766 6.88e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.54  E-value: 6.88e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16371 HDIPEDAQLETAENSSVIVIPECTRAHSGKYSITAKNKAGQKTANCRVKVM---DAPGPPKDLKVSDITRGSCRLSWkmp 16447
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTATADTPGSVTLSW--- 253
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16448 DDDGGDRIKGYVIEKKTIDGKAWTKVNPNcGSTAFVVPDLISEQQYFFRVRAENRFGI-GPPAETIQRTTArdpIYPPDL 16526
Cdd:COG3401     254 DPVTESDATGYRVYRSNSGDGPFTKVATV-TTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTD---LTPPAA 329
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16527 PIKLKIGLITKNTVHLSWKPPKndgGSPVTHYIVECLAWDPTGKKKEAwrqcnrRDVEELEFTVEDLVEGGEYEFRVKAV 16606
Cdd:COG3401     330 PSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIA------ETVTTTSYTDTGLTPGTTYYYKVTAV 400
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16607 NEAGV-SKPSATVGPVTVKDQTCPPSIELKEFMEVEEGTDVNIVAKIKGVPFPTLTW--FKAPPKKPDSKEPVVYDTHVN 16683
Cdd:COG3401     401 DAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVlaDGGDTGNAVPFTTTSSTVTAT 480
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16684 KQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTASKEMRLNVLGRPGPPVGPIKFESISADQMTLSWLPPKDDGGSKITN 16763
Cdd:COG3401     481 TTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560

                    ...
gi 1958765569 16764 YVI 16766
Cdd:COG3401     561 VSG 563
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20101-20189 7.06e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 7.06e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20101 PGPPAFPKVYDTTRSSVSLSWgKPAFDGGSPIIGYLVEVKRADSDHWVRCNlPEKLQKTRFEVTGLMENTEYQFRVYAVN 20180
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*....
gi 1958765569 20181 KIGYSDPSD 20189
Cdd:cd00063      79 GGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23249-23338 7.27e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 7.27e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23249 PDAPKAPEVTAVTKDSMIVVWERPASDGGsEILGYVLEKRDKEGIRWTRCHKRLIGELRLRVTGLLENHNYEFRVSAENA 23328
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 23329 AGLSEPSPPS 23338
Cdd:cd00063      80 GGESPPSESV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26495-26585 7.63e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 7.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26495 PSPPTSLEITSVTKDSMTLCWSRPETDGGsDISGYIIERREKNSLRWMRVNKKPVYDLRVKSTGLREGCEYEYRVFAENA 26574
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 26575 AGLSLPSDTSP 26585
Cdd:cd00063      80 GGESPPSESVT 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
23844-24121 7.63e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.54  E-value: 7.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23844 FDEVSAESITLSWNPPLYTGGCQITNYIVQKRDTTTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENRYGQSFAleS 23923
Cdd:COG3401     144 GAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--S 221
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23924 EPIVAQYPYKEPGPPGTPFVTAVSKDSMVVQWHEPINNGgspVIGYHLERKERNSILWTKVNKTIihDTQFKALNLEEGI 24003
Cdd:COG3401     222 NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGT 296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24004 EYEFRVYAENivGVGKASKNS-ECYVARDPcDPPGTPEAIIVKR---NEITLQWTkPVYDGGsmITGYIVEKRDLPEGRW 24079
Cdd:COG3401     297 TYYYRVTAVD--AAGNESAPSnVVSVTTDL-TPPAAPSGLTATAvgsSSITLSWT-ASSDAD--VTGYNVYRSTSGGGTY 370
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 24080 MKASFTnVIETQFTVSGLTEDQRYEFRVIAKNAAGAISKPSD 24121
Cdd:COG3401     371 TKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSE 411
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18216-18307 7.86e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 7.86e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18216 PSPPGKPVVTDITENAATVSWTLPKSDGGsPITGYYVERREI-TGKWVRVNKTPIADLKFRVTGLYEGNTYEFRVFAENL 18294
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 18295 AGLSNPSPSSDPI 18307
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21091-21174 1.03e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 1.03e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21091 EISNVTKNTATVSWKRPiDDGGSEITGYHVERREKKGLRWVRATKTPVSDLRCKVTGLQEGNTYEFRVSAENRAGIGPPS 21170
Cdd:cd00063       8 RVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86

                    ....
gi 1958765569 21171 DASN 21174
Cdd:cd00063      87 ESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28269-28361 1.04e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 1.04e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28269 PGPPGKPVIYNVTSDGMSLTWDAPVYDGGsEVTGFHVEKKERNSILWQRVNTSPISGREYRATGLIEGLDYQFRVYAENS 28348
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 28349 AGLSSPSDPSKFT 28361
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25116-25209 1.15e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 91.79  E-value: 1.15e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25116 DPPGRPEAIIITRNSVTLKWKKPTYDGGsKITGYIVEKKDLPDGRWMKASFTNVVETEFTVTGLVEDQRYEFRVIARNAA 25195
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 25196 dNFSEPSESSGAIT 25209
Cdd:cd00063      81 -GESPPSESVTVTT 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
32201-32293 1.20e-20

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 91.71  E-value: 1.20e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:cd20951      81 IHGEASSSASVVV 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15807-15899 1.21e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 91.79  E-value: 1.21e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15807 PTSPERLTYTERTKSTITLDWKEPRSDGGsPIQGYIIEKRRHDKPDFERVNKRLCPTTSFLVDNLDEHQMYEFRVKAVND 15886
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 15887 IGESEPSLPLNVV 15899
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
4760-4849 1.90e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.16  E-value: 1.90e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4760 PTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEAG 4839
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4840 SQTSVGELIV 4849
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
9182-9271 1.99e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.16  E-value: 1.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9182 PVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAG 9261
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  9262 SDTSKCKVTI 9271
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
6353-6438 2.31e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.78  E-value: 2.31e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6353 PVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVG 6432
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*.
gi 1958765569  6433 SDTCIC 6438
Cdd:pfam07679    81 EAEASA 86
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14696-14787 2.95e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.63  E-value: 2.95e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14696 PGPPYALTVVDVTKRHVDLKWEPPKNDGGrPIQRYIIEKKEKLGTRWVKAGKTSGPDCNFRVTDVIEGTEVQFQVRAENE 14775
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 14776 AGVGHPSEPTEI 14787
Cdd:cd00063      80 GGESPPSESVTV 91
I-set pfam07679
Immunoglobulin I-set domain;
8424-8511 3.03e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.39  E-value: 3.03e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8424 IVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKD 8503
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*...
gi 1958765569  8504 SCTVSIQV 8511
Cdd:pfam07679    83 EASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
4387-4476 3.21e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.39  E-value: 3.21e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4467 ADICQAELTI 4476
Cdd:pfam07679    81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
14212-14292 3.45e-20

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 89.96  E-value: 3.45e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14212 LTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVN 14291
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 14292 V 14292
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16524-16622 3.58e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.63  E-value: 3.58e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16524 PDLPIKLKIGLITKNTVHLSWKPPKNDGGsPVTHYIVEClawdpTGKKKEAWRQCNRRDVEELEFTVEDLVEGGEYEFRV 16603
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEY-----REKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRV 74
                            90
                    ....*....|....*....
gi 1958765569 16604 KAVNEAGVSKPSATVGPVT 16622
Cdd:cd00063      75 RAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17229-17322 3.62e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.63  E-value: 3.62e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17229 PERPEDLEVKEVTKNTVTLTWNPPKYDGGsEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNI 17308
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 17309 VGQGKPSFCTKPIT 17322
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26198-26291 3.87e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 3.87e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26198 DPPGQPEVTNITRKSVSLKWSKPRYDGGaKITGYIVERRELPDGRWLKCNFTNVQETYFEVTELTEDQRYEFRVFARNAA 26277
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 26278 dSVSEPSESTGPIT 26291
Cdd:cd00063      81 -GESPPSESVTVTT 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1417-1507 3.98e-20

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 90.25  E-value: 3.98e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:cd05744      81 GENSFNAELVV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31634-31725 3.99e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 3.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31634 PDPPRGVKVSDVSRDSVNLTWTEPASDGGsKVTNYIVEKCATTAERWLRV--GQARETRYTVVNLFGKTSYQFRVIAENK 31711
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 31712 FGLSKPSEPSEPTV 31725
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
4573-4663 4.60e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.01  E-value: 4.60e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4573 PSFVKKVDPSYLMlPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDA 4652
Cdd:pfam07679     1 PKFTQKPKDVEVQ-EGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  4653 GSDSCSTEVVI 4663
Cdd:pfam07679    80 GEAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
20900-20981 4.94e-20

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 89.57  E-value: 4.94e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20900 LTVKAGDSIVLSaISILGKPLPKSSWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEHVKV 20979
Cdd:cd05748       2 IVVRAGESLRLD-IPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 20980 SV 20981
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
32201-32293 7.78e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 89.24  E-value: 7.78e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPgddDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS---SDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:pfam07679    78 SAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21771-21863 7.88e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.48  E-value: 7.88e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21771 PGPPGTPQVTAVTKDSMTISWHEPLSDGGsPILGYHIERKERNGILWQTVSKALVPGNIFKSTGLTDGIAYEFRVIAENM 21850
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 21851 AGKSKPSKPSEPT 21863
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24273-24538 9.77e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.08  E-value: 9.77e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24273 TSRLAWTVVASEVVTNSLKVTKLLEGNEYIFRIMAVNKYGVGEPleSAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWN 24352
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24353 RPDSDGgseIIGYIVEKRDRSGIRWIKCNKrrITDLRLRVTGLTEDHEYEFRVSAENAAGV-GEPS-PATVYYKacdpVF 24430
Cdd:COG3401     255 PVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSnVVSVTTD----LT 325
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24431 KPGPPTNVHIVDTTKNSITLAWGKPiydGGSDILGYVVEICKADEEEWQIVTpqTGLRVTRFEISKLIEHQEYKIRVCAL 24510
Cdd:COG3401     326 PPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ETVTTTSYTDTGLTPGTTYYYKVTAV 400
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 24511 NKVGLGEAASVPGTVKPEDKLEAPELDL 24538
Cdd:COG3401     401 DAAGNESAPSEEVSATTASAASGESLTA 428
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21380-21469 1.01e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.01e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21380 PGPVLNLRPTDITKDSVTLHWDLPLiDGGSRITNYIVEKREATRKSYSTVTTKCHK-CTYKVTGLTEGCEYFFRVMAENE 21458
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 21459 YGIGEPTETTE 21469
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27679-27770 1.04e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.04e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27679 PGPPAKIRIADSTKSSITLGWSKPVYDGGsDVTGYVVEMRQGEEEEWTIVSTKgEARTTEYVVSNLKPGVNYYFQVSAVN 27758
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVT-PGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|..
gi 1958765569 27759 CAGQGEPITMTE 27770
Cdd:cd00063      79 GGGESPPSESVT 90
I-set pfam07679
Immunoglobulin I-set domain;
6636-6725 1.08e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.85  E-value: 1.08e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6636 PSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAG 6715
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6716 SDECRALLTV 6725
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29854-29944 1.15e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.15e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29854 PGPPSAPRVVDTTKSSISLAWTKPMYDGGtDIIGYVLEMQEKDTDQWCRVhTNTTIRNNEFTVPDLKMGQKYSFRVAAVN 29933
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEV-EVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|.
gi 1958765569 29934 AKGMSDYSETT 29944
Cdd:cd00063      79 GGGESPPSESV 89
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
28480-28560 1.15e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 88.42  E-value: 1.15e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIE--RRMNMEITDVlgSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEIT 28557
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKetGRVQIETTAS--STSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    ...
gi 1958765569 28558 VKV 28560
Cdd:cd05748      80 VKV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30943-31028 1.16e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.16e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30943 PSQPGELEILSISKDSVILQWEKPECDGGkEILGYWVEYRQSGDSAWKKSNKERIKDRQFTIGGLLEATEYEFRVFAENE 31022
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 31023 TGLSRP 31028
Cdd:cd00063      80 GGESPP 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15097-15184 1.56e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.56e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15097 DVEVHNPTAKAMTITWKPPLYDGGsKIMGYIIEKLAKGEDRWKRCNEHLVPVLTYTAKGLEEGKEYQFRVRAENAAGIGE 15176
Cdd:cd00063       6 NLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84

                    ....*...
gi 1958765569 15177 PSRATPPT 15184
Cdd:cd00063      85 PSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26887-26970 1.57e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.57e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26887 PSPPEKLGVTSVSKDSVSLSWLKPEHDGGsRILHYVVEALEKGQKNWVKCAV--VKTTHHVVSGLREGHEYFFRVFAENQ 26964
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 26965 AGLSDP 26970
Cdd:cd00063      80 GGESPP 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
14908-14988 1.57e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 88.03  E-value: 1.57e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14908 IVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASINVK 14987
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 14988 V 14988
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18908-19001 1.59e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.59e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18908 PGRPDPPEVTKVSKEEMTVVWNAPEYDGGKsITGYYLEKKEKHAVRWVPVNKSAIPERRLKVQNLLPGHEYQFRVKAENE 18987
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 18988 VGIGEPSLPSRPVV 19001
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14797-14888 1.62e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.62e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14797 PSPPLDLHVTDAGRKHIAIAWKPPEKNGGsPIIGYHVEMCPVGTEKWMRVNSRPIKDLKFKVeEGVVPDKEYVLRVRAVN 14876
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTL-TGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|..
gi 1958765569 14877 AVGVSDPSEISE 14888
Cdd:cd00063      79 GGGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24725-24808 2.25e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 2.25e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24725 PSPPGKVTLTDVSQTSASLMWEKPEHDGGsRILGYVVEMQPKGTEKWSVV--AESKVCSAVVSGLSSGQEYQFRVKAYNE 24802
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 24803 KGKSDP 24808
Cdd:cd00063      80 GGESPP 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25808-25891 2.32e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 2.32e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25808 PLPPGRVTLVDVTRNTATIKWEKPESDGGsKITGYVVEMQTKGSEKWSTCT--QVKTLEATISGLTAGEEYVFRVAAVNE 25885
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 25886 KGRSDP 25891
Cdd:cd00063      80 GGESPP 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18854-19394 2.37e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.92  E-value: 2.37e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18854 VWSTYSANVLTPGATVTRLIEGNEYIFRVRAENKIGTGPPTESKPVIAKTkYDRPGRPDPPEVTKVSKEEMTVVWNAPEY 18933
Cdd:COG3401      88 PPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAAT-AGTYALGAGLYGVDGANASGTTASSVAGA 166
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18934 DGGKSITGYYLEKKEKHAVRWVPVNKSAIPERrlkvqnLLPGHEYQFRVKAENEVGIgepSLPSRPVVAKDPIEPPGPPT 19013
Cdd:COG3401     167 GVVVSPDTSATAAVATTSLTVTSTTLVDGGGD------IEPGTTYYYRVAATDTGGE---SAPSNEVSVTTPTTPPSAPT 237
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19014 NFKVVDTTKNSITLAWgKPVYDGGApiIGYVVEmRpkiaDASPDEGWKRCNAAAQLvrmEFTVTSLDENQEYEFRVCAQN 19093
Cdd:COG3401     238 GLTATADTPGSVTLSW-DPVTESDA--TGYRVY-R----SNSGDGPFTKVATVTTT---SYTDTGLTNGTTYYYRVTAVD 306
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19094 QVGIgrpaelkeairpkeileppeidldasmrklvvvragcpirlfaivRGRPAPKVTwrkvgidnvvrkgqvdlvdtma 19173
Cdd:COG3401     307 AAGN---------------------------------------------ESAPSNVVS---------------------- 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19174 flvipnstrddsgkysltlVNPAGEKavfvnvkvldtPGPVSDLKVSDVTKTSCHVSWAPPEndgGSPVTHYIVEKREAE 19253
Cdd:COG3401     320 -------------------VTTDLTP-----------PAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSG 366
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19254 RKTWSTVTPEVKKTSFNVTNLVPGNEYFFRVTAVNEYGP-GVPTDVPKPVLASDPLSEPDPPRKVEVTEMTKNSATLAWL 19332
Cdd:COG3401     367 GGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAAS 446
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 19333 PPLRDGGAKIDGYIISYREEDQP--ADRWTEYSVVKDLSLIITGLKEGKKYKFRVAARNAVGVS 19394
Cdd:COG3401     447 AASNPGVSAAVLADGGDTGNAVPftTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
I-set pfam07679
Immunoglobulin I-set domain;
7482-7570 2.53e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.08  E-value: 2.53e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7482 RIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGK 7561
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  7562 SSCTVSVHV 7570
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8518-8607 2.58e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 2.58e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAG 8597
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8598 SDECSAPLTV 8607
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17105-17508 2.89e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.54  E-value: 2.89e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17105 YSLLAKNEGGERKKTIIVDVLDVPGPVGIP--FLSDNLTNDSCKLTWFSPEDDGgspITNYVIQKREADRRAWTPVTyTV 17182
Cdd:COG3401     207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVA-TV 282
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17183 TRQNATVQGLIQGKSYFFRIAAENSIG-MGPFVETpnALVIRDpITVPERPEDLEVKEVTKNTVTLTWNPPKydgGSEII 17261
Cdd:COG3401     283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNV--VSVTTD-LTPPAAPSGLTATAVGSSSITLSWTASS---DADVT 356
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17262 NYVLESRLIGTEKFHKVTnDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQGkpSFCTKPITCKDELAPPTLDLDfRDKLT 17341
Cdd:COG3401     357 GYNVYRSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASGESLT-ASVDA 432
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17342 VRVGEAFALTGRYSGkPKPKVDWFKDEADVlEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFCQVNVV 17421
Cdd:COG3401     433 VPLTDVAGATAAASA-ASNPGVSAAVLADG-GDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17422 DRPGPPVGPVVFDeVTKEYMVISWKPPLDDGGSEITNYIIEKKELGKDIWMPVTSASAKTTCKVPKLLEGKDYIFRIHAE 17501
Cdd:COG3401     511 VIGASAAAAVGGA-PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589

                    ....*..
gi 1958765569 17502 NLYGISD 17508
Cdd:COG3401     590 NDVAGVH 596
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24034-24127 3.17e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.94  E-value: 3.17e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24034 DPPGTPEAIIVKRNEITLQWTKPVYDGGSmITGYIVEKRDLPEGRWMKASFTNVIETQFTVSGLTEDQRYEFRVIAKNAA 24113
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 24114 GaISKPSDSTGPIT 24127
Cdd:cd00063      81 G-ESPPSESVTVTT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
25228-25310 3.29e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 87.26  E-value: 3.29e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25228 VIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAaRMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPIT 25307
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETG-RVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    ...
gi 1958765569 25308 VKV 25310
Cdd:cd05748      80 VKV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
19817-19897 3.33e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 87.26  E-value: 3.33e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19897 V 19897
Cdd:cd05748      82 V 82
I-set pfam07679
Immunoglobulin I-set domain;
1801-1889 3.73e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 3.73e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDG-IHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGgTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  1880 VTEHKVKLEI 1889
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5137-5225 3.84e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 3.84e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5137 FTEKLEPsQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGS 5216
Cdd:pfam07679     3 FTQKPKD-VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  5217 DHCTSIVIV 5225
Cdd:pfam07679    82 AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22561-22644 4.67e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 4.67e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22561 PLPPGKITLMDVTRNSVSLSWEKPEHDGGsRILGYIVEMQSKGSDKWATCAT--VKVTEATITGLIQGEEYSFRVSAQNE 22638
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 22639 KGISDP 22644
Cdd:cd00063      80 GGESPP 85
I-set pfam07679
Immunoglobulin I-set domain;
6259-6349 4.75e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 4.75e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPA 6338
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  6339 GSTSCSTKVIV 6349
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22464-22553 5.68e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.68e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22464 PGPPQNLKIKEVTKTSVTLTWEPPLLDGGsKIKNYIVEKRESTRKAYSTVATNCHK-TSWKIDQLQEGCSYYFRVLAENE 22542
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 22543 YGIGLPAETAE 22553
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18809-18900 5.84e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.84e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18809 PGPVRNLKIADVSSDRCTIRWDPPEDDGGcEIQNYILEKCESKRMVWSTYSANVLT-PGATVTRLIEGNEYIFRVRAENK 18887
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 18888 IGTGPPTESKPVI 18900
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26790-26881 5.90e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.90e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26790 PGPPANITVREVTKETAVLSWDVPENDGGaPVKNYHIEKREASKKAWVSV-TNNCSRLSYKVTNLQEGAVYYFRVSGENE 26868
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 26869 FGVGVPAETKEGV 26881
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20299-20381 5.90e-19

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 86.51  E-value: 5.90e-19
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20299 PGPPVNVTVKEISKDSAYITWDPPIIDGG-SPIINYVVEKRDaERKSWSTVTTECPKTSFRVSNLEEGKSYFFRVFAENE 20377
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  20378 YGIG 20381
Cdd:smart00060    80 AGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
24146-24227 6.84e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 86.49  E-value: 6.84e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24146 TIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNV 24225
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 24226 KV 24227
Cdd:cd05748      81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23643-23734 1.01e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.40  E-value: 1.01e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23643 PQPPGKITVDDVTRNSVSLSWTKPEHDGGsKIIQYIVEMQAKNTDKWSEC--ARVKSLEAVITSLTQGEEYLFRVIAVNE 23720
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 23721 KGRSDPRSLAVPIT 23734
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16729-16821 1.05e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.40  E-value: 1.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16729 PGPPVGpIKFESISADQMTLSWLPPKDDGGsKITNYVIEKREANRKTWVRVSSEP-KECMYTIPKLLEGHEYVFRIMAQN 16807
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 16808 KYGIGEPLDSEPET 16821
Cdd:cd00063      79 GGGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
1417-1507 1.19e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 86.16  E-value: 1.19e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVViKEDGTQSLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVT-YEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19604-19697 1.26e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.01  E-value: 1.26e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19604 PSEPKNARVTKVNKDCIFVAWDRPDSDGGsPITGYLIERKERNSLLWVKANDTIVRSTEYPCAGLVEGLEYSFRIYALNK 19683
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 19684 AGSSPPSKPTEYVT 19697
Cdd:cd00063      80 GGESPPSESVTVTT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
21982-22063 1.35e-18

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 85.72  E-value: 1.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21982 TITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNV 22061
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22062 KV 22063
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
17741-17818 1.52e-18

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 85.33  E-value: 1.52e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17741 HIKVGDTLRLSAIIKGVPFPKVTWKKEDRE--APTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd05748       3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPlkETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
23089-23628 2.11e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.84  E-value: 2.11e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23089 WVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNVKVLDRPGPPEGPVA-ISGVTAEKCM 23167
Cdd:COG3401      74 GTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYAlGAGLYGVDGA 153
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23168 LAWKPPLQDGGSDIINYIVERRETSRLVWTLVDANVQTLSCKVTKLLEGNEYIFRIMAVNKYGVGEPleSEPLIAKNPFV 23247
Cdd:COG3401     154 NASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTT 231
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23248 VPDAPKAPEVTAVTKDSMIVVWERPASDGgseILGYVLEKRDKEGIRWTRchkrlIGEL---RLRVTGLLENHNYEFRVS 23324
Cdd:COG3401     232 PPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTK-----VATVtttSYTDTGLTNGTTYYYRVT 303
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23325 AENAAGlsEPSPPSAYQKACDPIYKPGPPNNPKVMDVTRSSVFLSWTKPiydGGCEIQGYIVEKCDVSVGEWTMCTppTG 23404
Cdd:COG3401     304 AVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ET 376
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23405 INKTNLEVEKLLEKHEYNFRICAINKAGVGEhaDVPGPVMVEEKLEAPDIDLDLELRKVINIRAGGSlrlFVPIKGRPTP 23484
Cdd:COG3401     377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNES--APSEEVSATTASAASGESLTASVDAVPLTDVAGA---TAAASAASNP 451
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23485 EVKWGKVDGEIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTleNSSGTKSAFVTVRVLDTPSPPVNLKVTEITKDSVSI 23564
Cdd:COG3401     452 GVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTT--GSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPN 529
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 23565 TW-EPPLLDGGSKIKNYIVEKREATRKSYAAVVTNCHKNSWKIDQLQEGcSYYFRVTAENEYGIG 23628
Cdd:COG3401     530 VTgASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLG-GSLLTTTSTNTNDVA 593
I-set pfam07679
Immunoglobulin I-set domain;
32306-32396 2.13e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.39  E-value: 2.13e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGlDYYALHIRDTLPEDTGYYRVTATNTA 32385
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569 32386 GSTSCQAHLQV 32396
Cdd:pfam07679    80 GEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5791-5879 2.35e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.00  E-value: 2.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5791 PIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANEGG 5870
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  5871 SCACTARVA 5879
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30147-30240 2.35e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 85.24  E-value: 2.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30147 PLVPTKLEVVDVTKSTVTLAWEKPLYDGGsRLTGYVLEACKAGTERWMKVVTLKPTVLDHTVISLNEGEQYLFRVRAQNE 30226
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 30227 KGVSEPREIVTPVT 30240
Cdd:cd00063      80 GGESPPSESVTVTT 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33079-33162 2.44e-18

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 84.86  E-value: 2.44e-18
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33079 PRSITVHEGESARFSCDTDGEPVPTVTWLR-GGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQ 33157
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  33158 FTLTV 33162
Cdd:smart00410    81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
1038-1127 3.08e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.00  E-value: 3.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKqtGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEG--GTYTLTISNVQPDDSGKYTCVATNS 78
                            90
                    ....*....|
gi 1958765569  1118 HGETSASASL 1127
Cdd:pfam07679    79 AGEAEASAEL 88
I-set pfam07679
Immunoglobulin I-set domain;
8328-8418 4.21e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 84.62  E-value: 4.21e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8328 PQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDkGEIVRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKNDA 8407
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  8408 GVQECYATLSV 8418
Cdd:pfam07679    80 GEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
22670-22749 4.46e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 84.23  E-value: 4.46e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNVIV 22749
Cdd:pfam07679    11 EVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5042-5131 4.55e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 84.23  E-value: 4.55e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5042 PSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVAG 5121
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5122 SVECSANLFV 5131
Cdd:pfam07679    81 EAEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
32886-32975 5.24e-18

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 84.39  E-value: 5.24e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32886 PRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESS---KIHYTNTSGVLTLEILDCQTEDSGTYRAVCTN 32962
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 32963 YKGEASDYATLDV 32975
Cdd:cd20951      81 IHGEASSSASVVV 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
19450-19935 5.32e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 94.30  E-value: 5.32e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19450 DVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKIKVTVMDAPGPPQPPFDISEIDADACSLSWHIPL 19529
Cdd:COG3401      83 AVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASS 162
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19530 EdGGSNITNYIVEKCDVSRGDWVTALASVTKTSCrVGKLIPGQEYIFRVRAENRFGISEPltSPKMLAKFPFDVPSEPKN 19609
Cdd:COG3401     163 V-AGAGVVVSPDTSATAAVATTSLTVTSTTLVDG-GGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTG 238
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19610 ARVTKVNKDCIFVAWDRPDSDGgspITGYLIERKERNSLLWVKANDtiVRSTEYPCAGLVEGLEYSFRIYALNKAGSspP 19689
Cdd:COG3401     239 LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--E 311
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19690 SKPTEYVTARMPVDPPGKPEVVDVT---KNSASLIWARPKhdgGSKIIGYFVEACKLPGDKWVRCNTTPHQIpleEYTAT 19766
Cdd:COG3401     312 SAPSNVVSVTTDLTPPAAPSGLTATavgSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTT---SYTDT 385
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19767 GLEENAQYQFRAIAKTAVNISqpSEPSDPVTILAENVPP--RIELSVEMKSLLTVKAGTNVCLDATVFGKPMPTVSWKKD 19844
Cdd:COG3401     386 GLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASgeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGD 463
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19845 S---TPIKQTEGVKMAMK-RNLCTLELFSVNRKDSGDYTITAENSS---GSKSATIKLKVLDKPGPPASVKINKMYADRA 19917
Cdd:COG3401     464 TgnaVPFTTTSSTVTATTtDTTTANLSVTTGSLVGGSGASSVTNSVsviGASAAAAVGGAPDGTPNVTGASPVTVGASTG 543
                           490
                    ....*....|....*...
gi 1958765569 19918 MLSWEPPLEDGGSEITNY 19935
Cdd:COG3401     544 DVLITDLVSLTTSASSSV 561
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17625-17710 7.00e-18

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 83.43  E-value: 7.00e-18
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17625 PSPPINPEAIDTTCNSVDLTWQPPRHDGGSkilGYIVEYQKVGDEEWRRANHTPESCPETKYKVTGLRDGQTYKFRVLAV 17704
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT---GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  17705 NEAGES 17710
Cdd:smart00060    78 NGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21477-21568 7.70e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 83.70  E-value: 7.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21477 PLPPDSLNIMDITKNTVSLAWPKPRHDGGsKITGYVIEAQRKGSDQWTHIST--VKGLECVVRNLTEGEEYTFQVMAVNS 21554
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 21555 AGRSAPRESRPVIV 21568
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24432-24526 9.00e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 83.70  E-value: 9.00e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24432 PGPPTNVHIVDTTKNSITLAWGKPIYDGGsDILGYVVEICKADEEEWQIVTPQTGlRVTRFEISKLIEHQEYKIRVCALN 24511
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1958765569 24512 KVGLGEaASVPGTVK 24526
Cdd:cd00063      79 GGGESP-PSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
4862-4942 1.20e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.08  E-value: 1.20e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4862 IQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFT 4941
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569  4942 V 4942
Cdd:pfam07679    90 V 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14496-14578 1.47e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 82.66  E-value: 1.47e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14496 PWPPGKPTVKDIGKTSLVLNWTKPEHDGGAKIESYVIEMLKTGTDDWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKA 14575
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  14576 GES 14578
Cdd:smart00060    81 GEG 83
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1249-1337 1.51e-17

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 82.84  E-value: 1.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIR-RGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05893       3 FEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQG 82
                            90
                    ....*....|
gi 1958765569  1328 NAICSGKLYV 1337
Cdd:cd05893      83 RISCTGRLMV 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18216-18298 1.51e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 82.66  E-value: 1.51e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18216 PSPPGKPVVTDITENAATVSWTLPKSDGG-SPITGYYVERREITGKWVRVNKTPiADLKFRVTGLYEGNTYEFRVFAENL 18294
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  18295 AGLS 18298
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
33892-33984 1.52e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 82.69  E-value: 1.52e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSqeqQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGN 33971
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS---SDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 33972 EFGSDSATVNINI 33984
Cdd:pfam07679    78 SAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29058-29141 1.58e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 1.58e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29058 PAPPRRLDVVDTSKSSAVLAWLKPEHDGGsRITSYLLEMRQKGSDFW--VEAGHTKQLTFTVERLVENTEYEFRVKAKND 29135
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 29136 AGYSEP 29141
Cdd:cd00063      80 GGESPP 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
907-989 1.66e-17

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 82.55  E-value: 1.66e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    907 KNVTVVEGESVTLECHISGYPSPKVTWYREDYQ-IESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSC 985
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569    986 YLAV 989
Cdd:smart00410    82 TLTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29253-29345 1.76e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 1.76e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29253 PGPVTGpIEVSSVSAESCVLSWSEPKDDGGtEITNYIVEKRESGTTAWQLINS-SVKRTQIKVTHLTKYKEYCFRVSSEN 29331
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 29332 RFGVSKPLESVPIV 29345
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14000-14082 1.87e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 82.28  E-value: 1.87e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14000 PSAPKELKFSDVTKDSVHLTWEPPDDDGG-SPLTGYVVEKRDMSRKtWTKVMDFVTDLEFTVPDLVQGKEYLFKVCARNK 14078
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  14079 CGPG 14082
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
4480-4569 2.10e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 82.31  E-value: 2.10e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAG 4559
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4560 SSSSSATVAV 4569
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17922-18011 2.29e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.54  E-value: 2.29e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17922 PGPPKDLHHVDVDKTEVSLVWNKPDRDGGsPITGYLVEYQEEGAKDWIKFKT--VKNLECVVTGLQQGKTYRFRVKAENI 17999
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 18000 IGLGLPDTTIPI 18011
Cdd:cd00063      80 GGESPPSESVTV 91
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15640-16002 2.61e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 92.37  E-value: 2.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15640 VTGRPVPTKVWTIEEGELDKERVVIENVGTKSELIIKNALRKDHG---RYVITATNSCGSKFAAARVEVF---DVPGPVL 15713
Cdd:COG3401     158 TTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGttyYYRVAATDTGGESAPSNEVSVTtptTPPSAPT 237
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15714 DLKPVVTNRKMCLLNWSDPADDGgseITGFIIERKDAKMHTWRQPIETERSKCDITGLIEGQEYKFRVIAKNKFGcgppV 15793
Cdd:COG3401     238 GLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAG----N 310
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15794 EIGP--ILAVDP-LGPPTSPERLTYTERTKSTITLDWkEPRSDGGspIQGYIIEKRRHDKPDFERVNKrLCPTTSFLVDN 15870
Cdd:COG3401     311 ESAPsnVVSVTTdLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTG 386
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15871 LDEHQMYEFRVKAVNDIG-ESEPSLPlnVVIQDDEVPPTIKLRLAVRGDTIKVKAGEPVNI----PADVTGLPMPKIEWS 15945
Cdd:COG3401     387 LTPGTTYYYKVTAVDAAGnESAPSEE--VSATTASAASGESLTASVDAVPLTDVAGATAAAsaasNPGVSAAVLADGGDT 464
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 15946 KNEKVIEKPTDALNITKEEVSRSEAKTElSIPKAVREDKGTYTITASNRLGSVFRNV 16002
Cdd:COG3401     465 GNAVPFTTTSSTVTATTTDTTTANLSVT-TGSLVGGSGASSVTNSVSVIGASAAAAV 520
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23350-23438 2.75e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.16  E-value: 2.75e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23350 PGPPNNPKVMDVTRSSVFLSWTKPIYDGGcEIQGYIVEKCDVSVGEWTMCTPPTGiNKTNLEVEKLLEKHEYNFRICAIN 23429
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*....
gi 1958765569 23430 KAGVGEHAD 23438
Cdd:cd00063      79 GGGESPPSE 87
I-set pfam07679
Immunoglobulin I-set domain;
6729-6818 2.89e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 2.89e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6729 PSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNNAG 6808
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6809 QASCTTRLFV 6818
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5884-5973 2.95e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 2.95e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESG 5963
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5964 VERCYAFLLV 5973
Cdd:pfam07679    81 EAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19311-19394 3.45e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 81.51  E-value: 3.45e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19311 PDPPRKVEVTEMTKNSATLAWLPPLRDGGakiDGYIISYREEDQPAD-RWTEYSV-VKDLSLIITGLKEGKKYKFRVAAR 19388
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYRVEYREEGsEWKEVNVtPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  19389 NAVGVS 19394
Cdd:smart00060    78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4581-4663 3.48e-17

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 81.78  E-value: 3.48e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4581 PSYLMLPGESARLHCKLKGSPVIQVTWFKNN-KELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCST 4659
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   4660 EVVI 4663
Cdd:smart00410    82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
14899-14988 3.61e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 3.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14899 PTIDLETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLG 14978
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 14979 SATASINVKV 14988
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7952-8040 3.76e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.53  E-value: 3.76e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLG 8031
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  8032 TASSSAKLI 8040
Cdd:pfam07679    81 EAEASAELT 89
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16829-16916 3.84e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 81.51  E-value: 3.84e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16829 PGAPDKPTVSSVTRNSMTVNWEEPEYDGG-SPVTGYWLEMKDtTSKRWKRVNRDPIKamtlgVSYKVTGLIEGSDYQFRV 16907
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSS-----TSYTLTGLKPGTEYEFRV 74

                     ....*....
gi 1958765569  16908 YAINAAGVG 16916
Cdd:smart00060    75 RAVNGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
5229-5317 5.13e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.15  E-value: 5.13e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEVG 5308
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  5309 SSTCSARVT 5317
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29653-29744 5.34e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.39  E-value: 5.34e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29653 PGPCGKLTVSRVTEEKCTLAWSLPQEDGGaEITHYIVERRETSRLNWVIVEAECLT-LSYVVTRLIKNNEYTFRVRAVNK 29731
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 29732 YGLGVPIESEPIV 29744
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16010-16094 5.51e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 81.12  E-value: 5.51e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16010 PSPPRNLAVTDIKAESCYLTWDAPL-DNGGSEITHYIIDKRDasrKKSEWEEVTNTAVERRYGIWKLIPNGQYEFRVRAV 16088
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPdDGITGYIVGYRVEYRE---EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  16089 NKYGTS 16094
Cdd:smart00060    78 NGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
7011-7099 6.54e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.15  E-value: 6.54e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLG 7090
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  7091 TASSTARLT 7099
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19901-19992 6.61e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 6.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19901 PGPPASVKINKMYADRAMLSWEPPlEDGGSEITNYIVDKRETSRPNWAQVSAT-VPITSCTVEKLIEGHEYQFRICAENK 19979
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 19980 YGVGDPIFTEPVI 19992
Cdd:cd00063      80 GGESPPSESVTVT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5703-5787 6.62e-17

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 81.01  E-value: 6.62e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5703 PSPVLVLRnGQSTTFECQVTGTPEIRVSWYLDGNE-ITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDAGTASC 5781
Cdd:smart00410     1 PPSVTVKE-GESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                     ....*.
gi 1958765569   5782 SIELKV 5787
Cdd:smart00410    80 GTTLTV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
31440-31532 6.77e-17

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 81.31  E-value: 6.77e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEI--IADGLKYRVQEfKGGYHQLIIASVTDDDATVYQVRAT 31517
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKIES-EYGVHVLHIRRVTVEDSAVYSAVAK 79
                            90
                    ....*....|....*
gi 1958765569 31518 NQGGSVSGTASLEVE 31532
Cdd:cd20951      80 NIHGEASSSASVVVE 94
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7576-7666 7.42e-17

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 81.09  E-value: 7.42e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7576 PPSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVA 7655
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  7656 GQDESSALLTV 7666
Cdd:cd20972      81 GSDTTSAEIFV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16424-16506 7.46e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 80.74  E-value: 7.46e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16424 PGPPKDLKVSDITRGSCRLSWKMPDDDGGDR-IKGYVIEKKTIDGKaWTKVNPNCGSTAFVVPDLISEQQYFFRVRAENR 16502
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  16503 FGIG 16506
Cdd:smart00060    80 AGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17822-17909 7.73e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 7.73e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17822 PGPPRDLEVSEIRKDSCYLTWKEPLDDGGSvVTNYVVERKDVATAQWSPLSTT-SKKKSHMAKHLNEGNQYLFRVAAENQ 17900
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*....
gi 1958765569 17901 YGRGPFVET 17909
Cdd:cd00063      80 GGESPPSES 88
fn3 pfam00041
Fibronectin type III domain;
19312-19396 9.82e-17

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 80.54  E-value: 9.82e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19312 DPPRKVEVTEMTKNSATLAWLPPlRDGGAKIDGYIISYREEDQPaDRWTEYSVVKDL-SLIITGLKEGKKYKFRVAARNA 19390
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSG-EPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 19391 VGVSMP 19396
Cdd:pfam00041    79 GGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
6073-6162 1.14e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 80.38  E-value: 1.14e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAG 6152
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6153 DNACSGILTV 6162
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18613-18706 1.16e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.62  E-value: 1.16e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18613 PGEPENLHIADKGKTFVYLKWRRPDYDGGsPNLSYHVERRLKGSADWERVHKGSIKETHYMVDKCVENQIYEFRVQTKNE 18692
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 18693 GGESDWVRTEEVVV 18706
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
14212-14292 1.17e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 80.38  E-value: 1.17e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14212 LTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVN 14291
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 14292 V 14292
Cdd:pfam07679    90 V 90
I-set pfam07679
Immunoglobulin I-set domain;
19817-19897 1.24e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 80.38  E-value: 1.24e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 19897 V 19897
Cdd:pfam07679    90 V 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
13804-13887 1.30e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.97  E-value: 1.30e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13804 PSPPVNLSASEQTQSSVQLTWEPPLKDGG-SPILGYIIERQEEGkDNWIRCNMKPvPELTYKVTGLQKGNKYLYRVSAEN 13882
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  13883 AAGVS 13887
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
9292-9380 1.47e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.99  E-value: 1.47e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGE 9371
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDG-QPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  9372 IESNVNLQV 9380
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7387-7477 1.75e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.99  E-value: 1.75e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7387 PRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDkGEVIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKNDA 7466
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  7467 GMRECSALLTV 7477
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25414-25497 1.84e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.58  E-value: 1.84e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25414 PGPPSTPEASAITKDSMVLTWTRPVDDGG-AEIEGYILEKRDKEGiRWTKCNKKTlTDLRFRVTGLTEGHSYEFRVAAEN 25492
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  25493 AAGVG 25497
Cdd:smart00060    79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14992-15078 1.86e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 1.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14992 PGPCKDIKASDITKSSCKLTWEPPEFDGGsPILHYVLERREAGRRTYIPVMSGE-NKLSWTVKDLIPNGEYFFRVKAVNK 15070
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 15071 IGGGEYIE 15078
Cdd:cd00063      80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19504-19592 1.86e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 1.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19504 PGPPQPPfDISEIDADACSLSWHiPLEDGGSNITNYIVEKCDVSRGDWVTA-LASVTKTSCRVGKLIPGQEYIFRVRAEN 19582
Cdd:cd00063       1 PSPPTNL-RVTDVTSTSVTLSWT-PPEDDGGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|
gi 1958765569 19583 RFGISEPLTS 19592
Cdd:cd00063      79 GGGESPPSES 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24725-24806 2.03e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.58  E-value: 2.03e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24725 PSPPGKVTLTDVSQTSASLMWEKPEHDGG-SRILGYVVEMQPKGTEKWSVVAESKVCSAVVSGLSSGQEYQFRVKAYNEK 24803
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  24804 GKS 24806
Cdd:smart00060    81 GEG 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
33698-33787 2.20e-16

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 79.77  E-value: 2.20e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISV---SRSRNMYTLEIRNASVSDSGKYTVKAKN 33774
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKykiESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 33775 FRGQCSATASLTV 33787
Cdd:cd20951      81 IHGEASSSASVVV 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22464-22546 2.49e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.20  E-value: 2.49e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22464 PGPPQNLKIKEVTKTSVTLTWEPPLLDGG-SKIKNYIVEKRESTRKaYSTVATNCHKTSWKIDQLQEGCSYYFRVLAENE 22542
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  22543 YGIG 22546
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20101-20185 2.57e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.20  E-value: 2.57e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20101 PGPPAFPKVYDTTRSSVSLSWGKPAFDGG-SPIIGYLVEvKRADSDHWVRCNLPEKlqKTRFEVTGLMENTEYQFRVYAV 20179
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVE-YREEGSEWKEVNVTPS--STSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  20180 NKIGYS 20185
Cdd:smart00060    78 NGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
31440-31531 2.63e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 2.63e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGlKYRVQeFKGGYHQLIIASVTDDDATVYQVRATNQ 31519
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD-RFKVT-YEGGTYTLTISNVQPDDSGKYTCVATNS 78
                            90
                    ....*....|..
gi 1958765569 31520 GGSVSGTASLEV 31531
Cdd:pfam07679    79 AGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28766-28849 2.75e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.20  E-value: 2.75e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28766 PSAPAVVKVTDTSKTTVSLEWARPVFDGGME-IIGYIIEMCKADlGDWHKVNTEPcVKTRYTVTDLQAGEEYKFRVSAIN 28844
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEG-SEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  28845 GAGKG 28849
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24331-24414 3.24e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.24e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24331 PGPPKSLEVTNIAKDSMTVCWNRPDSDGG-SEIIGYIVEKRDRSGiRWIKCNkRRITDLRLRVTGLTEDHEYEFRVSAEN 24409
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  24410 AAGVG 24414
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27282-27362 3.28e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.28e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27282 PPRNVRITDISKNSVNLSWQQPAFDGG-SKITGYIVERRDlPDGRWTKASfTNVIETQFTVSGLTQNSQYEFRVFARNAV 27360
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ..
gi 1958765569  27361 GS 27362
Cdd:smart00060    81 GE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21380-21462 3.31e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.31e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21380 PGPVLNLRPTDITKDSVTLHWDLPLIDGG-SRITNYIVEKREaTRKSYSTVTTKCHKCTYKVTGLTEGCEYFFRVMAENE 21458
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  21459 YGIG 21462
Cdd:smart00060    80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
20102-20188 3.62e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 78.61  E-value: 3.62e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20102 GPPAFPKVYDTTRSSVSLSWgKPAFDGGSPIIGYLVEVKRADS-DHWVRCNLPEklQKTRFEVTGLMENTEYQFRVYAVN 20180
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSgEPWNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*...
gi 1958765569 20181 KIGYSDPS 20188
Cdd:pfam00041    78 GGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26790-26872 3.76e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.76e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26790 PGPPANITVREVTKETAVLSWDVPENDGG-APVKNYHIEKREASKKaWVSVTNNCSRLSYKVTNLQEGAVYYFRVSGENE 26868
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  26869 FGVG 26872
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22561-22642 3.87e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.87e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22561 PLPPGKITLMDVTRNSVSLSWEKPEHDGG-SRILGYIVEMQSKGSDKWATCATVKVTEATITGLIQGEEYSFRVSAQNEK 22639
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  22640 GIS 22642
Cdd:smart00060    81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15314-15405 3.96e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 3.96e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15314 PGPPINFVFEDIRKDSVLCKWEPPLDDGGsEIINYTLEKKDKtkPDSEWIVITSTLRN-CKYSVTKLIEGKEYLFRVRAE 15392
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREK--GSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|...
gi 1958765569 15393 NRFGPGPPCVSKP 15405
Cdd:cd00063      78 NGGGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15521-15607 4.12e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 4.12e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15521 RVADTSSTTIELEWEPPAfNGGGEIMGYFVDKQLVGTNEWSRCTEKMVKVRQFTVKEIREGADYKLRVSAVNAAGEGPPG 15600
Cdd:cd00063       8 RVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86

                    ....*..
gi 1958765569 15601 ETEPVTV 15607
Cdd:cd00063      87 ESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25808-25889 4.22e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.43  E-value: 4.22e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25808 PLPPGRVTLVDVTRNTATIKWEKPESDGG-SKITGYVVEMQTKGSEKWSTCTQVKTLEATISGLTAGEEYVFRVAAVNEK 25886
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  25887 GRS 25889
Cdd:smart00060    81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28961-29045 4.82e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.69  E-value: 4.82e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28961 PGPPGPITFKDVTRGSATLMWDAPLLDGGaRIHHYVIEKREASRRSWQVVSEK-CTRQILKVSDLTEGVPYYFRVSAENE 29039
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 29040 YGVGEP 29045
Cdd:cd00063      80 GGESPP 85
I-set pfam07679
Immunoglobulin I-set domain;
6446-6536 4.86e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 78.45  E-value: 4.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKeKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDG 6525
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK-DGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  6526 GVRENMASLTV 6536
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22167-22250 4.88e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.43  E-value: 4.88e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22167 PDPPKNPEVTTITKDSMVVCWGHPDSDGG-SEIINYIVERRDKaGQRWVKCNKKAlTDLRFKVSGLTEGHEYEFRIMAEN 22245
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  22246 AAGVS 22250
Cdd:smart00060    79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8804-8886 5.48e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 78.32  E-value: 5.48e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8804 EPLKVTVGDSASLQCQLAGTPEIGVSWYK-GDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGEVSSST 8882
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   8883 FLTV 8886
Cdd:smart00410    82 TLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26887-26968 5.54e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.04  E-value: 5.54e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26887 PSPPEKLGVTSVSKDSVSLSWLKPEHDGG-SRILHYVVEALEKGQKNWVKCAVVKTTHHVVSGLREGHEYFFRVFAENQA 26965
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  26966 GLS 26968
Cdd:smart00060    81 GEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7113-7196 5.59e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 78.32  E-value: 5.59e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7113 PVSIDVIAGESADFECHVTGAQPMRVTWSKDN-KEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCS 7191
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   7192 AQLSV 7196
Cdd:smart00410    81 TTLTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20396-20484 6.33e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.31  E-value: 6.33e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20396 PGPVVDLKVLAVTKSSCTIGWKKPRSDGGsRITGYVVDF-LTEENKWQRVMKSLSLQYST--KDLKEGKEYTFRVSAENE 20472
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYrEKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 20473 NGEGTPSEIMVV 20484
Cdd:cd00063      80 GGESPPSESVTV 91
I-set pfam07679
Immunoglobulin I-set domain;
9671-9757 6.70e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 78.07  E-value: 6.70e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9671 QFTKRIQNIVVSEHQSATFECEVSFD-DAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARlEPRG 9749
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT-NSAG 80

                    ....*...
gi 1958765569  9750 EARSTAEL 9757
Cdd:pfam07679    81 EAEASAEL 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15314-15398 6.87e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.04  E-value: 6.87e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15314 PGPPINFVFEDIRKDSVLCKWEPPLDDGG-SEIINYTLEKKDKtkpDSEWIVITSTLRNCKYSVTKLIEGKEYLFRVRAE 15392
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE---GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  15393 NRFGPG 15398
Cdd:smart00060    78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16729-16812 7.95e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 77.65  E-value: 7.95e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16729 PGPPVGpIKFESISADQMTLSWLPPKDDGG-SKITNYVIEKREANRKtWVRVSSEPKECMYTIPKLLEGHEYVFRIMAQN 16807
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  16808 KYGIG 16812
Cdd:smart00060    79 GAGEG 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1038-1127 1.06e-15

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 77.54  E-value: 1.06e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVsYNKQTGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM-LVRENGRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|
gi 1958765569  1118 HGETSASASL 1127
Cdd:cd05744      80 AGENSFNAEL 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24628-24719 1.11e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.54  E-value: 1.11e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24628 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGaKVKNYVIDKRESTRKAYANVSSKCSK-TSFKVENLTEGAIYYFRVMAENE 24706
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 24707 FGVGVPAETSDAV 24719
Cdd:cd00063      80 GGESPPSESVTVT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7584-7666 1.30e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 77.16  E-value: 1.30e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7584 KDTTATLGASVVLECRVSGSAPISVGWFLDGNE-IISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQDESSA 7662
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   7663 LLTV 7666
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6547-6629 1.37e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 77.16  E-value: 1.37e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6547 GSMTVTVGETCSLECKVAGTPELSVEWYKDG-KLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTA 6625
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   6626 VVDV 6629
Cdd:smart00410    82 TLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14992-15074 1.47e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.88  E-value: 1.47e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14992 PGPCKDIKASDITKSSCKLTWEPPEFDGG-SPILHYVLERREAGRRtYIPVMSGENKLSWTVKDLIPNGEYFFRVKAVNK 15070
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  15071 IGGG 15074
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
24835-24913 1.64e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.91  E-value: 1.64e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 24835 VQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVIV 24913
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
3019-3102 1.81e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.91  E-value: 1.81e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3019 EFRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVA----GG 3093
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  3094 NMSTANLFV 3102
Cdd:pfam07679    82 AEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27679-27763 1.91e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.50  E-value: 1.91e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27679 PGPPAKIRIADSTKSSITLGWSKPVYDGG-SDVTGYVVEMRQgEEEEWTIVSTKGeaRTTEYVVSNLKPGVNYYFQVSAV 27757
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  27758 NCAGQG 27763
Cdd:smart00060    78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20000-20083 1.97e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.50  E-value: 1.97e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20000 PGRCDPPVISNITKDHMTVSWKAPADDGG-SPITGYLVEKRETQAvNWTKVNRKPvIERTLKATGLQEGTEYEFRVTAIN 20078
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  20079 KAGPG 20083
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23546-23628 2.07e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.50  E-value: 2.07e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23546 PSPPVNLKVTEITKDSVSITWEPPLLDGG-SKIKNYIVEKREaTRKSYAAVVTNCHKNSWKIDQLQEGCSYYFRVTAENE 23624
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  23625 YGIG 23628
Cdd:smart00060    80 AGEG 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6932-7001 2.38e-15

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 75.83  E-value: 2.38e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6932 VSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTAASKTV 7001
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
fn3 pfam00041
Fibronectin type III domain;
19212-19296 2.61e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 76.30  E-value: 2.61e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19212 GPVSDLKVSDVTKTSCHVSWAPPEnDGGSPVTHYIVEKREA---ERKTWSTVTPEvkKTSFNVTNLVPGNEYFFRVTAVN 19288
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnsgEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*...
gi 1958765569 19289 EYGPGVPT 19296
Cdd:pfam00041    78 GGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
18026-18112 2.83e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.53  E-value: 2.83e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18026 VKLIEGLVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKT 18105
Cdd:pfam07679     4 TQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAE 83

                    ....*..
gi 1958765569 18106 VAVHLTV 18112
Cdd:pfam07679    84 ASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7209-7290 2.90e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 76.39  E-value: 2.90e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7209 SKVAKQGESIQLECKISGSPEIKVVWFRNDSE-LHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVGHASCSTA 7287
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   7288 LKV 7290
Cdd:smart00410    83 LTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29854-29938 2.93e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.11  E-value: 2.93e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29854 PGPPSAPRVVDTTKSSISLAWTKPMYDGGTD-IIGYVLEMQEKDtDQWCRVHTNTTirNNEFTVPDLKMGQKYSFRVAAV 29932
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEG-SEWKEVNVTPS--STSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  29933 NAKGMS 29938
Cdd:smart00060    78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18809-18891 3.23e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.11  E-value: 3.23e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18809 PGPVRNLKIADVSSDRCTIRWDPPEDDGG-CEIQNYILEKCEsKRMVWSTYSANVLTPGATVTRLIEGNEYIFRVRAENK 18887
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  18888 IGTG 18891
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
1249-1337 3.28e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.14  E-value: 3.28e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFlQDGRASLRIPVVLPEDEGIYTAFASNIKGN 1328
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTY-EGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  1329 AICSGKLYV 1337
Cdd:pfam07679    82 AEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4299-4381 3.29e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 76.00  E-value: 3.29e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4299 EPLEVALGHLAKFTCEIQGAPNVRFQWFK-AGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYGSVSCTA 4377
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   4378 TLTV 4381
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
13805-13890 3.30e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.91  E-value: 3.30e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13805 SPPVNLSASEQTQSSVQLTWEPPlKDGGSPILGYIIERQEEGK-DNWIRCNMKPvPELTYKVTGLQKGNKYLYRVSAENA 13883
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSgEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 13884 AGVSDPS 13890
Cdd:pfam00041    79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
31634-31715 3.50e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.73  E-value: 3.50e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31634 PDPPRGVKVSDVSRDSVNLTWTEPASDGG-SKVTNYIVEKCaTTAERWLRV-GQARETRYTVVNLFGKTSYQFRVIAENK 31711
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYR-EEGSEWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  31712 FGLS 31715
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28368-28447 3.74e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.73  E-value: 3.74e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28368 DPPGTPDYIDVTRETITLKWNPPLRDGG-SKIVAYSIEKRQGSDRWVRCNfTDVSECQYTVSGLSPGDRYEFRIIARNAV 28446
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     .
gi 1958765569  28447 G 28447
Cdd:smart00060    81 G 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31235-31328 4.06e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.00  E-value: 4.06e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31235 PDKPTGpIVIEALLKNSVVISWKAPADDGGSwITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQN 31314
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 31315 TFGISEPLEVASVV 31328
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23835-23918 4.08e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.73  E-value: 4.08e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23835 PDPPKGpVKFDEVSAESITLSWNPPLYTGG-CQITNYIVQKRDTTTTvWDVVSATVARTTLKVTKLKTGTEYQFRIFAEN 23913
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  23914 RYGQS 23918
Cdd:smart00060    79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9296-9380 4.36e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 75.62  E-value: 4.36e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9296 PQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGEIESN 9375
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   9376 VNLQV 9380
Cdd:smart00410    81 TTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30545-30628 4.59e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.73  E-value: 4.59e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30545 PGKPQNPRVTDTTRTSVSLAWSVPEDEGG-SKVTGYLIEMQKVDqREWTKCNTTPTKiREYTLTHLPQGAEYRFRVLACN 30623
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSS-TSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  30624 AGGPG 30628
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
6824-6909 4.75e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 4.75e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6824 FVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAGRD 6903
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*.
gi 1958765569  6904 SCDALV 6909
Cdd:pfam07679    83 EASAEL 88
I-set pfam07679
Immunoglobulin I-set domain;
6166-6255 4.84e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 4.84e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6166 PSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTNDVG 6245
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6246 SDSCTTMLLV 6255
Cdd:pfam07679    81 EAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
14498-14581 4.97e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.53  E-value: 4.97e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14498 PPGKPTVKDIGKTSLVLNWTKPEhDGGAKIESYVIEMLKTGT-DDWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKAG 14576
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....*
gi 1958765569 14577 ESEPS 14581
Cdd:pfam00041    81 EGPPS 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4591-4659 5.18e-15

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 75.06  E-value: 5.18e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4591 ARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCST 4659
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23643-23724 5.80e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.34  E-value: 5.80e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23643 PQPPGKITVDDVTRNSVSLSWTKPEHDGG-SKIIQYIVEMQAKNTDKWSECARVKSLEAVITSLTQGEEYLFRVIAVNEK 23721
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  23722 GRS 23724
Cdd:smart00060    81 GEG 83
I-set pfam07679
Immunoglobulin I-set domain;
8706-8790 5.82e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.37  E-value: 5.82e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8706 FVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKD 8785
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*
gi 1958765569  8786 SCSAQ 8790
Cdd:pfam07679    83 EASAE 87
I-set pfam07679
Immunoglobulin I-set domain;
27792-27874 7.01e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.37  E-value: 7.01e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27792 SVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQpKSSTVS 27871
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE-AEASAE 87

                    ...
gi 1958765569 27872 VKV 27874
Cdd:pfam07679    88 LTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18514-18604 7.21e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 75.23  E-value: 7.21e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18514 PGPCQNLKVSNVTKENCTISWENPLDNGGsEITNFIVEYRKPNQKGWSIVASDVTKR---LIKaNLLANNEYYFRVCAEN 18590
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSEtsyTLT-GLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 18591 KVGVGPTIETKTPI 18604
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26000-26082 7.40e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.96  E-value: 7.40e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26000 PGPPGPIRIDEVSCDNVSISWTPPEYDGG-CQISNYIVEKRETtSTTWQVVSQAVARTSIKIVRLTTGSEYQFRVCAENR 26078
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  26079 YGKS 26082
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29058-29139 7.55e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.96  E-value: 7.55e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29058 PAPPRRLDVVDTSKSSAVLAWLKPEHDGG-SRITSYLLEMRQKGSDFWVEAGHTKQLTFTVERLVENTEYEFRVKAKNDA 29136
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  29137 GYS 29139
Cdd:smart00060    81 GEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
33901-33982 7.86e-15

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 74.93  E-value: 7.86e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33901 ISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQsqeQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDSATV 33980
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLK---ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATI 78

                    ..
gi 1958765569 33981 NI 33982
Cdd:cd05748      79 NV 80
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
15919-16006 9.37e-15

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 74.55  E-value: 9.37e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15919 TIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIeKPTDALNITKEEVSrseakTELSIPKAVREDKGTYTITASNRLGSV 15998
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPL-KETGRVQIETTASS-----TSLVIKNAKRSDSGKYTLTLKNSAGEK 74

                    ....*...
gi 1958765569 15999 FRNVHVEV 16006
Cdd:cd05748      75 SATINVKV 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16524-16612 9.44e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 9.44e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16524 PDLPIKLKIGLITKNTVHLSWKPPKNDGG-SPVTHYIVEclawdpTGKKKEAWRQCNRrDVEELEFTVEDLVEGGEYEFR 16602
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVE------YREEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFR 73
                             90
                     ....*....|
gi 1958765569  16603 VKAVNEAGVS 16612
Cdd:smart00060    74 VRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30850-30925 9.44e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 9.44e-15
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  30850 VLDVTKSSVSLSWSRPKDDGGSRVTGYYIERKETSTDKWVRHNKTQITTTmYTVTGLVPDAEYQFRIIAQNDVGLS 30925
Cdd:smart00060     9 VTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTS-YTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26495-26578 1.00e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 1.00e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26495 PSPPTSLEITSVTKDSMTLCWSRPETDGG-SDISGYIIERREKNSlRWMRVNKKPVyDLRVKSTGLREGCEYEYRVFAEN 26573
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPS-STSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  26574 AAGLS 26578
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21671-21754 1.01e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 1.01e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21671 PGPPTGpIKFDEVSSDFVTFSWEPPENDGGV-PISNYVVEMRQTDSTtWVELATTVIRTTYKATRLTTGVEYQFRVKAQN 21749
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  21750 RYGVG 21754
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
17626-17712 1.04e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 74.76  E-value: 1.04e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17626 SPPINPEAIDTTCNSVDLTWQPPRhDGGSKILGYIVEYQKVGDEEWrrANHTPESCPETKYKVTGLRDGQTYKFRVLAVN 17705
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEP--WNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 17706 EAGESDP 17712
Cdd:pfam00041    78 GGGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
3577-3667 1.04e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 1.04e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIiHNPDGSGTFIVNDPQRGDSGLYICKAENLW 3656
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV-TYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  3657 GTSTCTAELLV 3667
Cdd:pfam07679    80 GEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6268-6349 1.07e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 74.46  E-value: 1.07e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6268 SKIVKAGDSARLECKITGSPEIRVVWYRNEHE-LTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTK 6346
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   6347 VIV 6349
Cdd:smart00410    83 LTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19901-19983 1.15e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 1.15e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19901 PGPPASVKINKMYADRAMLSWEPPLEDGG-SEITNYIVDKRETSrPNWAQVSATVPITSCTVEKLIEGHEYQFRICAENK 19979
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  19980 YGVG 19983
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17229-17312 1.22e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.19  E-value: 1.22e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17229 PERPEDLEVKEVTKNTVTLTWNPPKYDGG-SEIINYVLESRLIGTEkfHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVN 17307
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE--WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  17308 IVGQG 17312
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
4667-4753 1.35e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 1.35e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4667 PSFIKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEVG 4746
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*..
gi 1958765569  4747 KCGCVAT 4753
Cdd:pfam07679    81 EAEASAE 87
I-set pfam07679
Immunoglobulin I-set domain;
24147-24227 1.36e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 1.36e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24147 IVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNVK 24226
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 24227 V 24227
Cdd:pfam07679    90 V 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30050-30141 1.50e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.46  E-value: 1.50e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30050 PGPCPSVNVKEVSRDSVTITWEIPTIDGGaPVNNYIIEKREAAMRAFKTVTTKCSKTL-YRISGLVEGTMYYFRVLPENI 30128
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETsYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 30129 YGIGEPCETSDAV 30141
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20396-20476 1.71e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 1.71e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20396 PGPVVDLKVLAVTKSSCTIGWKKPRSDGG-SRITGYVVDFLTEENKWQRVMKSLS-LQYSTKDLKEGKEYTFRVSAENEN 20473
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSsTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  20474 GEG 20476
Cdd:smart00060    81 GEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
17340-17420 1.95e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 73.78  E-value: 1.95e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17340 LTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFCQVN 17419
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 17420 V 17420
Cdd:cd05748      82 V 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15415-15497 2.04e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 2.04e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15415 PDAPDKPIVDDVTSNSMVVKWNEPKDNG--SPILGYWLEKREVNSThWSRVNKAlLSSLKTKVDGLLEGLTYVFRVCAEN 15492
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGSE-WKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  15493 AAGPG 15497
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20985-21067 2.10e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 2.10e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20985 PGPPGPIEISNVSAEKATLTWTPPLEDGG-SPIKAYVLEKRETSRLlWTVVSEDIQACRHVVTKLIQGNEYLFRVSAVNH 21063
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  21064 YGKG 21067
Cdd:smart00060    80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
27282-27361 2.39e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.60  E-value: 2.39e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27282 PPRNVRITDISKNSVNLSWQqPAFDGGSKITGYIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAVG 27361
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21091-21167 2.41e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.41e-14
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  21091 EISNVTKNTATVSWKRPIDDGG-SEITGYHVERREKKGlRWVRATKTPvSDLRCKVTGLQEGNTYEFRVSAENRAGIG 21167
Cdd:smart00060     8 RVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4387-4474 2.42e-14

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 73.99  E-value: 2.42e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPS---PDCRITDADNKHSLELSNLTVQDRGVYSCKASN 4463
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSsipGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|.
gi 1958765569  4464 KFGADICQAEL 4474
Cdd:cd20951      81 IHGEASSSASV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33704-33787 2.47e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 73.69  E-value: 2.47e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33704 PRSQNINEGQNVLFSCEISGEPSPEIEWFKNNL-PISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQCSAT 33782
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  33783 ASLTV 33787
Cdd:smart00410    81 TTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29653-29735 2.68e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.68e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29653 PGPCGKLTVSRVTEEKCTLAWSLPQEDGG-AEITHYIVERRETSRlNWVIVEAECLTLSYVVTRLIKNNEYTFRVRAVNK 29731
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  29732 YGLG 29735
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21477-21558 2.71e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.71e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21477 PLPPDSLNIMDITKNTVSLAWPKPRHDGG-SKITGYVIEAQRKGSDQWTHISTVKGLECVVRNLTEGEEYTFQVMAVNSA 21555
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  21556 GRS 21558
Cdd:smart00060    81 GEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8997-9078 2.86e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 73.31  E-value: 2.86e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8997 PVDAVVGESADLECHVTGTQPIKVTWAKDNRE-IRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQ 9075
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   9076 LNI 9078
Cdd:smart00410    83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
16830-16919 2.96e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 2.96e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16830 GAPDKPTVSSVTRNSMTVNWEEPEyDGGSPVTGY---WLEMKDTTSKRWKRVNRDPIkamtlgvSYKVTGLIEGSDYQFR 16906
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYeveYRPKNSGEPWNEITVPGTTT-------SVTLTGLKPGTEYEVR 72
                            90
                    ....*....|...
gi 1958765569 16907 VYAINAAGVGPAS 16919
Cdd:pfam00041    73 VQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23249-23332 3.10e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 3.10e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23249 PDAPKAPEVTAVTKDSMIVVWERPASDGG-SEILGYVLEKRDKEGiRWTRCHKRlIGELRLRVTGLLENHNYEFRVSAEN 23327
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  23328 AAGLS 23332
Cdd:smart00060    79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16940-17025 3.33e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 73.30  E-value: 3.33e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16940 KVTDWTKSSVDLEWSPPlKDGGSKITGYIVEYKEEGKEEWEKGKDKEVRGTKLVVTGLKEGAFYKFRVRAVNIAGVGEPG 17019
Cdd:cd00063       8 RVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86

                    ....*.
gi 1958765569 17020 EVTDII 17025
Cdd:cd00063      87 ESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
19998-20086 3.36e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 3.36e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19998 DPPGRcdpPVISNITKDHMTVSWKAPaDDGGSPITGYLVEKRETQAVNWTKVNRKPVIERTLKATGLQEGTEYEFRVTAI 20077
Cdd:pfam00041     1 SAPSN---LTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 20078 NKAGPGKPS 20086
Cdd:pfam00041    77 NGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22753-22836 3.38e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 3.38e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22753 PGPPTGpVKMDEVTADSVTLSWEPPKYDGGSS-INNYIVEKRDTSTTaWQIVSATVARTTIKASRLKTGCEYQFRIAAEN 22831
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  22832 RYGKS 22836
Cdd:smart00060    79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
31053-31132 3.61e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.92  E-value: 3.61e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31053 DVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELV-QSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSK 31131
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     .
gi 1958765569  31132 L 31132
Cdd:smart00410    83 L 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25116-25195 3.66e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 3.66e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25116 DPPGRPEAIIITRNSVTLKWKKPTYDGG-SKITGYIVEKKDlPDGRWMKASfTNVVETEFTVTGLVEDQRYEFRVIARNA 25194
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     .
gi 1958765569  25195 A 25195
Cdd:smart00060    80 A 80
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27811-28075 3.97e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 81.97  E-value: 3.97e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27811 PPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKY---ILTIENGVGQPKSSTVSVKVLDT-PAACQKLQV 27886
Cdd:COG3401     162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYyyrVAATDTGGESAPSNEVSVTTPTTpPSAPTGLTA 241
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27887 KHVSLGTVTLLWDPPlidGGSPIINYVIEKRDATKRTWSIVShKCSGTSFKVMDLSEKTPFFFRVLAENEIGI-GEPCET 27965
Cdd:COG3401     242 TADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVA-TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNV 317
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27966 TEPVKAAEVPAPIRDLSMKDSTKTSVVLSWTKPDfdgGSIITDYLVERKGKGEQAWSH-AGISKTCEIEIGQLKEQSVLE 28044
Cdd:COG3401     318 VSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKiAETVTTTSYTDTGLTPGTTYY 394
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 28045 FRVSARNEKG----QSDPVTIGPLTVKELVITPEV 28075
Cdd:COG3401     395 YKVTAVDAAGnesaPSEEVSATTASAASGESLTAS 429
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28961-29043 4.28e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 4.28e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28961 PGPPGPITFKDVTRGSATLMWDAPLLDGG-ARIHHYVIEKREASRRsWQVVSEKCTRQILKVSDLTEGVPYYFRVSAENE 29039
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  29040 YGVG 29043
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17922-18003 4.28e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 4.28e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17922 PGPPKDLHHVDVDKTEVSLVWNKPDRDGG-SPITGYLVEYQEEGAKDWIKFKTVKNLECVVTGLQQGKTYRFRVKAENII 18000
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  18001 GLG 18003
Cdd:smart00060    81 GEG 83
I-set pfam07679
Immunoglobulin I-set domain;
9085-9175 4.46e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 73.06  E-value: 4.46e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLSeTIEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATNDA 9164
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  9165 GSALCTSSIVI 9175
Cdd:pfam07679    80 GEAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
26597-26681 4.63e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.83  E-value: 4.63e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26597 SPPSKPKIVDSGKTTITIGWvKPLFDGGAPITGYTVEYKKSEETDWKVAIQSFRGT-EYTMSGLTTGAEYVFRVRSLNKV 26675
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 26676 GASDPS 26681
Cdd:pfam00041    80 GEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
18713-18805 5.16e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.68  E-value: 5.16e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18713 PVLDLKLSGVlTVKAGDTIRLEAGVRGKPFPEVAWTKDKdaTDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATN 18792
Cdd:pfam07679     1 PKFTQKPKDV-EVQEGESARFTCTVTGTPDPEVSWFKDG--QPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 18793 PAGSFVAYATVNV 18805
Cdd:pfam07679    78 SAGEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8141-8218 5.21e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.68  E-value: 5.21e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8141 PRFIKKLdQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:pfam07679     1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29253-29336 5.35e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 5.35e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29253 PGPVTGpIEVSSVSAESCVLSWSEPKDDGGT-EITNYIVEKRESGTTaWQLINSSVKRTQIKVTHLTKYKEYCFRVSSEN 29331
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  29332 RFGVS 29336
Cdd:smart00060    79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5984-6066 5.39e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.54  E-value: 5.39e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5984 KSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQ-IVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDA 6062
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   6063 YLRV 6066
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
25810-25891 5.41e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 5.41e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25810 PPGRVTLVDVTRNTATIKWEKPEsDGGSKITGYVVEMQTKGSEKWSTCTQVK--TLEATISGLTAGEEYVFRVAAVNEKG 25887
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPgtTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 25888 RSDP 25891
Cdd:pfam00041    81 EGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17822-17904 5.51e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 5.51e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17822 PGPPRDLEVSEIRKDSCYLTWKEPLDDGG-SVVTNYVVERKDVATaQWSPLSTTSKKKSHMAKHLNEGNQYLFRVAAENQ 17900
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  17901 YGRG 17904
Cdd:smart00060    80 AGEG 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8797-8887 5.70e-14

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 72.84  E-value: 5.70e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTT---CKMHFKNNVATLVFTQVDSNDSGEYICRAEN 8873
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  8874 SVGEVSSSTFLTVQ 8887
Cdd:cd20951      81 IHGEASSSASVVVE 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6454-6536 5.77e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.54  E-value: 5.77e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6454 SLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDGGVRENMAS 6533
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   6534 LTV 6536
Cdd:smart00410    83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
28665-28751 5.85e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 5.85e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28665 DAPGIPEPSNVTGNSITLTWTRPEsDGGNEIQHYILERREKKSTRWVKVISkRPISETRFKVTGLVEGNEYEFHVMAENA 28744
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEIT-VPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 28745 AGVGPAS 28751
Cdd:pfam00041    79 GGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
30546-30630 6.02e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 6.02e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30546 GKPQNPRVTDTTRTSVSLAWSVPEDeGGSKVTGYLIEMQKVD-QREWTKCNTTPTKIReYTLTHLPQGAEYRFRVLACNA 30624
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNsGEPWNEITVPGTTTS-VTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 30625 GGPGEP 30630
Cdd:pfam00041    79 GGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
21092-21170 6.64e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 6.64e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 21092 ISNVTKNTATVSWKRPiDDGGSEITGYHVERREKKGLRWVRATKTPVSDLRCKVTGLQEGNTYEFRVSAENRAGIGPPS 21170
Cdd:pfam00041     8 VTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24628-24710 6.76e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.26  E-value: 6.76e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24628 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEF 24707
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  24708 GVG 24710
Cdd:smart00060    81 GEG 83
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
32306-32396 7.03e-14

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 72.62  E-value: 7.03e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGlDYYALHIRDTLPEDTGYYRVTATNTA 32385
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEG-DLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569 32386 GSTSCQAHLQV 32396
Cdd:cd20972      81 GSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9190-9271 7.36e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.15  E-value: 7.36e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9190 PVTASEGDFLQLSCHVQGSEPIRIQWLR-AGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSDTSKCK 9268
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   9269 VTI 9271
Cdd:smart00410    83 LTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6922-7000 7.73e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.15  E-value: 7.73e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6922 EPLEASVGDSVSLQCQVAGTPEITVSWFK-GDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTAASKT 7000
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18908-18991 8.22e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.88  E-value: 8.22e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18908 PGRPDPPEVTKVSKEEMTVVWNAPEYDGGKS-ITGYYLEKKEKHAvRWVPVNKSAiPERRLKVQNLLPGHEYQFRVKAEN 18986
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  18987 EVGIG 18991
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
23065-23145 8.31e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.29  E-value: 8.31e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23065 VVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNVK 23144
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 23145 V 23145
Cdd:pfam07679    90 V 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13-97 8.60e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.15  E-value: 8.60e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     13 QSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTlPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATST 92
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569     93 AELLV 97
Cdd:smart00410    81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
2756-2839 8.81e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.29  E-value: 8.81e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2756 KIIKKPKDVTALENATVAFEVSVSHDTVP-VKWFHKNVEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVV----GQ 2830
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2831 LECKAKLFV 2839
Cdd:pfam07679    82 AEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
31154-31229 9.91e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 71.85  E-value: 9.91e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31154 VGSTLRLHVMYIGRPVPAMTWYHGQKLLQNSESITIENTEHYTHLVMKNVQRKtHAGKYKVQLSNVFGTVDAILDV 31229
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRS-DSGKYTLTLKNSAGEKSATINV 80
I-set pfam07679
Immunoglobulin I-set domain;
2038-2128 1.15e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.90  E-value: 1.15e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIeRSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIA 2117
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPL-RSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  2118 GETSSHAFLLV 2128
Cdd:pfam07679    80 GEAEASAELTV 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
7480-7561 1.16e-13

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 72.00  E-value: 1.16e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7480 PARIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSV 7559
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  7560 GK 7561
Cdd:cd05747      83 GK 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15807-15890 1.27e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 1.27e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15807 PTSPERLTYTERTKSTITLDWKEPRSDGG-SPIQGYIIEKRRHDkPDFERVNKRlCPTTSFLVDNLDEHQMYEFRVKAVN 15885
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  15886 DIGES 15890
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
30850-30928 1.39e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 71.29  E-value: 1.39e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 30850 VLDVTKSSVSLSWSRPkDDGGSRVTGYYIERKETSTDKWVRHNKTQITTTMYTVTGLVPDAEYQFRIIAQNDVGLSETS 30928
Cdd:pfam00041     8 VTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7199-7290 1.42e-13

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 71.46  E-value: 1.42e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7199 PPKFIKKLDTSKVAkQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNG 7278
Cdd:cd20972       1 PPQFIQKLRSQEVA-EGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  7279 VGHASCSTALKV 7290
Cdd:cd20972      80 VGSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12983-13047 1.57e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 71.38  E-value: 1.57e-13
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  12983 NLEVSEGDTIKLVCEVS-KPGAEVTWYK-GDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCR 13047
Cdd:smart00410     3 SVTVKEGESVTLSCEASgSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCA 69
fn3 pfam00041
Fibronectin type III domain;
27680-27765 1.64e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 71.29  E-value: 1.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27680 GPPAKIRIADSTKSSITLGWSKPVyDGGSDVTGYVVEMRQ-GEEEEWTIVSTKGEarTTEYVVSNLKPGVNYYFQVSAVN 27758
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPkNSGEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 27759 CAGQGEP 27765
Cdd:pfam00041    78 GGGEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7874-7942 1.73e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 70.82  E-value: 1.73e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7874 TLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSAV 7942
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
31337-31420 1.76e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.76e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31337 PSVPGKPTITAVTKDSCVVAWKPPASDGGAKIRNYYLEKREKKQNKWIAVTTEEiRETVFSVQNLIEGLEYEFRVKCENL 31416
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  31417 GGES 31420
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19504-19587 1.79e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.79e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19504 PGPPqPPFDISEIDADACSLSWHIPLEDGG-SNITNYIVEKCDVSrGDWVTALASVTKTSCRVGKLIPGQEYIFRVRAEN 19582
Cdd:smart00060     1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  19583 RFGIS 19587
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24432-24516 1.85e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.85e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24432 PGPPTNVHIVDTTKNSITLAWGKPIYDGG-SDILGYVVEICKADeEEWQIVTPQTglRVTRFEISKLIEHQEYKIRVCAL 24510
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  24511 NKVGLG 24516
Cdd:smart00060    78 NGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
9581-9663 2.36e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 70.75  E-value: 2.36e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9581 PAWERHLQDVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTCK----HE 9655
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVatnsAG 80

                    ....*...
gi 1958765569  9656 DLETSAEL 9663
Cdd:pfam07679    81 EAEASAEL 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
31062-31130 2.51e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 70.05  E-value: 2.51e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31062 AQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSS 31130
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7487-7570 2.74e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.61  E-value: 2.74e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7487 PEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRE-LSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGKSSCT 7565
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   7566 VSVHV 7570
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7863-7945 2.77e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.61  E-value: 2.77e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7863 EHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPA-YKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSA 7941
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   7942 VLVI 7945
Cdd:smart00410    82 TLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5716-5783 2.83e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 70.05  E-value: 2.83e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5716 TFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDA-GTASCSI 5783
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
fn3 pfam00041
Fibronectin type III domain;
16218-16305 3.01e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 3.01e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16218 GPPSCPEVKDKTKSSISLAWKPPaKDGGSPIKGYIVEMQEEGTTD-WKKVNEPdklLTACECVVPNLKELRKYRFRVKAV 16296
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVP---GTTTSVTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 16297 NEAGESEPS 16305
Cdd:pfam00041    77 NGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14696-14779 3.03e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.34  E-value: 3.03e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14696 PGPPYALTVVDVTKRHVDLKWEPPKNDGGR-PIQRYIIEKKEKlGTRWVKAgKTSGPDCNFRVTDVIEGTEVQFQVRAEN 14774
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  14775 EAGVG 14779
Cdd:smart00060    79 GAGEG 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4967-5035 3.68e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 69.67  E-value: 3.68e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4967 RLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSRGA 5035
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14797-14881 4.31e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.95  E-value: 4.31e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14797 PSPPLDLHVTDAGRKHIAIAWKPPEK-NGGSPIIGYHVEMCPVGTEkWMRVNSRPiKDLKFKVeEGVVPDKEYVLRVRAV 14875
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDdGITGYIVGYRVEYREEGSE-WKEVNVTP-SSTSYTL-TGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  14876 NAVGVS 14881
Cdd:smart00060    78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9677-9758 4.74e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.84  E-value: 4.74e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9677 QNIVVSEHQSATFECEVS-FDDAIVTWYK-GPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEpRGEARST 9754
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNS-SGSASSG 80

                     ....
gi 1958765569   9755 AELY 9758
Cdd:smart00410    81 TTLT 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8048-8137 4.80e-13

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 70.22  E-value: 4.80e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVEN-TATLTVLKVAKGDAGQYTCYASNVA 8126
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  8127 GKDSCSAQLGV 8137
Cdd:cd05744      81 GENSFNAELVV 91
fn3 pfam00041
Fibronectin type III domain;
20300-20383 4.99e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 4.99e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20300 GPPVNVTVKEISKDSAYITWDPPIiDGGSPIINYVVEKRDAER-KSWSTVTTECPKTSFRVSNLEEGKSYFFRVFAENEY 20378
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 20379 GIGDP 20383
Cdd:pfam00041    80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
25415-25500 5.04e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 5.04e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25415 GPPSTPEASAITKDSMVLTWTRPvDDGGAEIEGYILEKRDKEGIRWTKCNKKTLTDLRFRVTGLTEGHSYEFRVAAENAA 25494
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 25495 GVGEPS 25500
Cdd:pfam00041    80 GEGPPS 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
3304-3391 5.08e-13

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 69.92  E-value: 5.08e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3304 PPAIVTPLQDAVTSEGRPARFQCQVSGTDL-KVSWYCRDKKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAV 3382
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTpVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....*....
gi 1958765569  3383 GQVSSTATL 3391
Cdd:cd20972      81 GSDTTSAEI 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
31455-31531 5.12e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.84  E-value: 5.12e-13
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  31455 SNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVqEFKGGYHQLIIASVTDDDATVYQVRATNQGGSVSGTASLEV 31531
Cdd:smart00410    10 ESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSV-SRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6558-6626 5.33e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 69.28  E-value: 5.33e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6558 SLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAV 6626
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
I-set pfam07679
Immunoglobulin I-set domain;
19417-19500 5.40e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 5.40e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19417 PEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKI 19496
Cdd:pfam07679     7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASA 86

                    ....
gi 1958765569 19497 KVTV 19500
Cdd:pfam07679    87 ELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
13521-13598 5.56e-13

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 69.54  E-value: 5.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13521 LVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTK---TVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKAEGFINLQ 13597
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgrvQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 13598 V 13598
Cdd:cd05748      82 V 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5994-6059 5.76e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 69.28  E-value: 5.76e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5994 VTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSS 6059
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
fn3 pfam00041
Fibronectin type III domain;
15809-15893 5.78e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 5.78e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15809 SPERLTYTERTKSTITLDWKEPRsDGGSPIQGYIIEKRRHDKPD--FERVNKRlcPTTSFLVDNLDEHQMYEFRVKAVND 15886
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEpwNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 15887 IGESEPS 15893
Cdd:pfam00041    79 GGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
5322-5411 5.83e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 5.83e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5322 PSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAG 5401
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5402 IQRCSALLSV 5411
Cdd:pfam07679    81 EAEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4292-4381 5.96e-13

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 69.76  E-value: 5.96e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESD---KCSIRSSNYISSLEILRTQVVDCGEYTCKASN 4368
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569  4369 EYGSVSCTATLTV 4381
Cdd:cd20951      81 IHGEASSSASVVV 93
fn3 pfam00041
Fibronectin type III domain;
22269-22354 6.01e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 6.01e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22269 GPPGNPRVLDTSRSSISIAWNKPiYDGGSEITGYMVEIALP-EEDEWQVVTPPAGlkATSYTITNLIENQEYKIRIYAMN 22347
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnSGEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 22348 SEGLGEP 22354
Cdd:pfam00041    78 GGGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
20900-20981 6.49e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.59  E-value: 6.49e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20900 LTVKAGDSIVLSaISILGKPLPKSSWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEHVKV 20979
Cdd:pfam07679    10 VEVQEGESARFT-CTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569 20980 SV 20981
Cdd:pfam07679    89 TV 90
I-set pfam07679
Immunoglobulin I-set domain;
29569-29649 6.56e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.59  E-value: 6.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29569 VTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMVK 29648
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 29649 V 29649
Cdd:pfam07679    90 V 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
33418-33504 6.72e-13

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 69.69  E-value: 6.72e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33418 IVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSV 33497
Cdd:cd05747       6 ILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQ 85

                    ....*..
gi 1958765569 33498 SSSCKLT 33504
Cdd:cd05747      86 EAQFTLT 92
I-set pfam07679
Immunoglobulin I-set domain;
12976-13047 7.23e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.59  E-value: 7.23e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12976 VFTKNLANLEVSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCR 13047
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV 74
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3591-3667 7.48e-13

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 69.53  E-value: 7.48e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  3591 GIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIIHNPDGSGTFIVNDPQRGDSGLYICKAENLWGTSTCTAELLV 3667
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
fn3 pfam00041
Fibronectin type III domain;
24726-24808 8.29e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 8.29e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24726 SPPGKVTLTDVSQTSASLMWEKPEhDGGSRILGYVVEMQPKGTE---KWSVVAESKVcSAVVSGLSSGQEYQFRVKAYNE 24802
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGepwNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 24803 KGKSDP 24808
Cdd:pfam00041    79 GGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4770-4849 8.67e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.07  E-value: 8.67e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4770 TALAGQTVTLQAAVRGSEPISVMWMK-GQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEAGSQTSVGELI 4848
Cdd:smart00410     5 TVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84

                     .
gi 1958765569   4849 V 4849
Cdd:smart00410    85 V 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30743-30823 8.69e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 8.69e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30743 PEGPLEYDDIQTRSVRVSWRPPADDGG-ADILGYILERREVpKAAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFG 30821
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81

                     ..
gi 1958765569  30822 IS 30823
Cdd:smart00060    82 EG 83
I-set pfam07679
Immunoglobulin I-set domain;
29966-30046 8.87e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.21  E-value: 8.87e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29966 KTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLA--NRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVL 30043
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 30044 VKV 30046
Cdd:pfam07679    88 LTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18514-18595 9.22e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 9.22e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18514 PGPCQNLKVSNVTKENCTISWENPL-DNGGSEITNFIVEYRKPNQKGWSIVASDVTKRLIKANLLANNEYYFRVCAENKV 18592
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  18593 GVG 18595
Cdd:smart00060    81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27975-28066 9.58e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 69.45  E-value: 9.58e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27975 PAPIRDLSMKDSTKTSVVLSWTKPDFDGGSiITDYLVERKGKGEQAWSHA--GISKTCEIEIGQLKEQSVLEFRVSARNE 28052
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 28053 KGQSDPVTIGPLTV 28066
Cdd:cd00063      80 GGESPPSESVTVTT 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
111-193 9.74e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.07  E-value: 9.74e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    111 QSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAE-IQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTA 189
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569    190 DLLV 193
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
27792-27874 1.01e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.07  E-value: 1.01e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27792 SVIAKAGEDVQLLIPFKGRPPPTVTWRKD-EKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQpKSSTV 27870
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQgGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS-ASSGT 81

                     ....
gi 1958765569  27871 SVKV 27874
Cdd:smart00410    82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
7670-7759 1.02e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.21  E-value: 1.02e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7670 PSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTNDAG 7749
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7750 SASCTTHLFV 7759
Cdd:pfam07679    81 EAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15097-15175 1.05e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 1.05e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15097 DVEVHNPTAKAMTITWKPPLYDGG-SKIMGYIIEKLAKGeDRWKRCNEHlVPVLTYTAKGLEEGKEYQFRVRAENAAGIG 15175
Cdd:smart00060     6 NLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
23753-23828 1.07e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.21  E-value: 1.07e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 23753 VQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIE 23828
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1801-1890 1.08e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 69.37  E-value: 1.08e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRV----RYDGIHYLDIVDCKSYDTGEVKVTAEN 1876
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKykieSEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  1877 PEGVTEHKVKLEIQ 1890
Cdd:cd20951      81 IHGEASSSASVVVE 94
fn3 pfam00041
Fibronectin type III domain;
17232-17315 1.10e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 1.10e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17232 PEDLEVKEVTKNTVTLTWNPPKyDGGSEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQ 17311
Cdd:pfam00041     3 PSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                    ....
gi 1958765569 17312 GKPS 17315
Cdd:pfam00041    82 GPPS 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5154-5222 1.21e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 68.12  E-value: 1.21e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5154 QLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTSI 5222
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
I-set pfam07679
Immunoglobulin I-set domain;
12175-12258 1.39e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.82  E-value: 1.39e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12175 PYFTVKLHDKTGVEKDEIILKCEVSKDVP--VKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC----DCG 12248
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSAG 80
                            90
                    ....*....|
gi 1958765569 12249 TDTTKANVTV 12258
Cdd:pfam07679    81 EAEASAELTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8892-8982 1.41e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 68.76  E-value: 1.41e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8892 PPSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPI 8971
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8972 GSASSSAKLIL 8982
Cdd:cd20972      81 GSDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
23547-23630 1.42e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 1.42e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23547 SPPVNLKVTEITKDSVSITWEPPlLDGGSKIKNYIVEKREATRKSYAAVVTNC-HKNSWKIDQLQEGCSYYFRVTAENEY 23625
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPgTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 23626 GIGLP 23630
Cdd:pfam00041    80 GEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30050-30132 1.43e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.41  E-value: 1.43e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30050 PGPCPSVNVKEVSRDSVTITWEIPTIDGG-APVNNYIIEKREAAMRaFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENI 30128
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  30129 YGIG 30132
Cdd:smart00060    80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
15416-15500 1.64e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.21  E-value: 1.64e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15416 DAPDKPIVDDVTSNSMVVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKALLSSLKTKVDGLLEGLTYVFRVCAENAAG 15495
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....*
gi 1958765569 15496 PGKFS 15500
Cdd:pfam00041    81 EGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
1682-1754 1.90e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.44  E-value: 1.90e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  1682 FECRLTpiGDPTMVVEWLHDGKPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:pfam07679    20 FTCTVT--GTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3461-3550 1.92e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 68.60  E-value: 1.92e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSAD---YKFVFDGNNHSLIILFTRFQDEGEYTCMASN 3537
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569  3538 EYGRAVCSAHLKV 3550
Cdd:cd20951      81 IHGEASSSASVVV 93
I-set pfam07679
Immunoglobulin I-set domain;
5604-5693 1.93e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.44  E-value: 1.93e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5604 PYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSV-WKDDTSTiLELFSAKAADSGTYICQLSNDV 5682
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVtYEGGTYT-LTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  5683 GTTSSKATIFV 5693
Cdd:pfam07679    80 GEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33423-33505 1.95e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 68.30  E-value: 1.95e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33423 RDTTVSSDSVAKFVIKVTGEPQPTVTWTKDG-KAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSC 33501
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  33502 KLTI 33505
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4393-4476 2.08e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.08e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4393 PKSLTTFVGKAAKFLCTVSGTPVIETIWQKDG-TALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKFGADICQ 4471
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   4472 AELTI 4476
Cdd:smart00410    81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
29855-29941 2.13e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.21  E-value: 2.13e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29855 GPPSAPRVVDTTKSSISLAWTKPMYDGGtDIIGYVLEMQEKDT---DQWCRVHTNTTirnnEFTVPDLKMGQKYSFRVAA 29931
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSgepWNEITVPGTTT----SVTLTGLKPGTEYEVRVQA 75
                            90
                    ....*....|
gi 1958765569 29932 VNAKGMSDYS 29941
Cdd:pfam00041    76 VNGGGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5891-5973 2.23e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.23e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5891 ENVTTVLKSSATFQSTVAGSPPISITWLKDD-QILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGVERCYA 5969
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   5970 FLLV 5973
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
24433-24517 2.31e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 2.31e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24433 GPPTNVHIVDTTKNSITLAWgKPIYDGGSDILGYVVEICKADEEE---WQIVTPQTglrvTRFEISKLIEHQEYKIRVCA 24509
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEpwnEITVPGTT----TSVTLTGLKPGTEYEVRVQA 75

                    ....*...
gi 1958765569 24510 LNKVGLGE 24517
Cdd:pfam00041    76 VNGGGEGP 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5525-5600 2.34e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.34e-12
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   5525 GSFIDLECIVAGSHPISIQWFKDDQE-ISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTV 5600
Cdd:smart00410     9 GESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7394-7477 2.37e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.37e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7394 SDVSTLIGDPVELQAVVEGFQPISVVWLKDKGEVIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKNDAGMRECSA 7473
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   7474 LLTV 7477
Cdd:smart00410    82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
28480-28560 2.40e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 2.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDGVEI--ERRMNMEITDvlGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEIT 28557
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrsSDRFKVTYEG--GTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 28558 VKV 28560
Cdd:pfam07679    88 LTV 90
I-set pfam07679
Immunoglobulin I-set domain;
27382-27474 2.47e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 2.47e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27382 PVIDLPLEYTEVvkyRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRN 27461
Cdd:pfam07679     1 PKFTQKPKDVEV---QEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 27462 AMGSASATIRVQI 27474
Cdd:pfam07679    78 SAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7300-7382 2.61e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.61e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7300 PPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQ-VRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCA 7378
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....
gi 1958765569   7379 CTVK 7382
Cdd:smart00410    81 TTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
7765-7852 2.67e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 2.67e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7765 FVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEAGQD 7844
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*...
gi 1958765569  7845 ICEALVSV 7852
Cdd:pfam07679    83 EASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
16731-16814 2.80e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 2.80e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16731 PPVGPIKFESISADQMTLSWLPPkDDGGSKITNYVIEKREANR-KTWVRVSSEPKECMYTIPKLLEGHEYVFRIMAQNKY 16809
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 16810 GIGEP 16814
Cdd:pfam00041    80 GEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7023-7099 2.93e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.53  E-value: 2.93e-12
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   7023 TVGLPVTLTCRLNGSAPIHVCWYRDG-VLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSTARLT 7099
Cdd:smart00410     7 KEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7107-7196 2.97e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 67.91  E-value: 2.97e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPH-LRILKVGKGDSGQYTCQATNDV 7185
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  7186 GKDMCSAQLSV 7196
Cdd:cd05744      81 GENSFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
4199-4286 3.03e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.67  E-value: 3.03e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4199 PTILKPLVDTISEKGDTVHLTSSISNAK--EVNWYFKGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNG 4276
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4277 KAMTSAKLTV 4286
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28571-28656 3.24e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 3.24e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28571 IRFTNITGEKMTLWWEAPLNDGcAPVTHYIIEKRETSRLAWALIE-DHCEAQSYTAIKLITGNEYQFRVSAVNKFGVGRP 28649
Cdd:cd00063       7 LRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85

                    ....*..
gi 1958765569 28650 LESDPVV 28656
Cdd:cd00063      86 SESVTVT 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8518-8607 3.46e-12

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 67.42  E-value: 3.46e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRK-LKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAIsSGRKYQTTLTDNTcaLTVNMLEDADAGDYTCIATNVA 8596
Cdd:cd20978       1 PKFIQKpEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDGT--LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  8597 GSDECSAPLTV 8607
Cdd:cd20978      78 GDIYTETLLHV 88
I-set pfam07679
Immunoglobulin I-set domain;
1516-1607 3.61e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.67  E-value: 3.61e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKN-SDIIVPHKYpRIRIEGtkGEAALKIDSTISQDSAWYTATAIN 1594
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDgQPLRSSDRF-KVTYEG--GTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569  1595 KAGRDTTRCKVNI 1607
Cdd:pfam07679    78 SAGEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
32886-32975 3.64e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.67  E-value: 3.64e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32886 PRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNYKG 32965
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 32966 EASDYATLDV 32975
Cdd:pfam07679    81 EAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
31235-31319 3.68e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 3.68e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31235 PDKPTGpIVIEALLKNSVVISWKAPADDGGSW-ITNYVVEKCEakEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQ 31313
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYRE--EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  31314 NTFGIS 31319
Cdd:smart00060    78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6735-6818 3.74e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.53  E-value: 3.74e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6735 PEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVK-GDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNNAGQASCT 6813
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   6814 TRLFV 6818
Cdd:smart00410    81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
11628-11719 3.83e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 3.83e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11628 KFVKEIKDIVLTEaesvGSSAIFECLVSPSTAIT-TWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRL 11706
Cdd:pfam07679     2 KFTQKPKDVEVQE----GESARFTCTVTGTPDPEvSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 11707 GNKEKTSTAKLIV 11719
Cdd:pfam07679    78 SAGEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
13065-13148 3.83e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 3.83e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13065 EFISKPQNLEILEGEKAEFVCTIS-KESFEVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVV----MVGA 13139
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSAGE 81

                    ....*....
gi 1958765569 13140 ARAAAHLTV 13148
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
17742-17818 4.02e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 4.02e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 17742 IKVGDTLRLSAIIKGVPFPKVTWKKEDREAPT--KAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSsdRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5603-5693 4.05e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 67.61  E-value: 4.05e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5603 PPYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSNDV 5682
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  5683 GTTSSKATIFV 5693
Cdd:cd20972      81 GSDTTSAEIFV 91
I-set pfam07679
Immunoglobulin I-set domain;
20513-20584 4.06e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 4.06e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 20513 RLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKV 20584
Cdd:pfam07679    19 RFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
5514-5600 4.08e-12

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 67.21  E-value: 4.08e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5514 TKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSF-HDNTAFLEISQLEGTDSGTYTCSATNKAGHS 5592
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  5593 QCSGHLTV 5600
Cdd:cd20973      81 TCSAELTV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3206-3288 4.08e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.15  E-value: 4.08e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3206 QPVTVQSGKPARF-CAViAGRPQPKISWYKE-EQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTS 3283
Cdd:smart00410     2 PSVTVKEGESVTLsCEA-SGSPPPEVTWYKQgGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   3284 ASLSV 3288
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8617-8700 4.91e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.15  E-value: 4.91e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8617 PDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELV-PGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAGRASCT 8695
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   8696 TQLFV 8700
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4967-5038 5.16e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.15  E-value: 5.16e-12
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569   4967 RLDCKIAGSLPMRVSWFKDG-KEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSRGALIV 5038
Cdd:smart00410    13 TLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
12087-12170 5.38e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 5.38e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12087 KFISPLEDQTVKEGQTATFVCELS-HEKMHVVWFKNDVKLHTTRTVLMSSEGKTYKLEIRETTLDDISQIKAQVKN---- 12161
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsage 81

                    ....*....
gi 1958765569 12162 LSSTANLKV 12170
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5423-5504 5.65e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 5.65e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5423 SIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKASI 5502
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569  5503 NV 5504
Cdd:pfam07679    89 TV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7028-7095 5.65e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 66.20  E-value: 5.65e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7028 VTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASST 7095
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8234-8317 6.15e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 66.84  E-value: 6.15e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8234 PPVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDV 8313
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....
gi 1958765569  8314 GSDT 8317
Cdd:cd20972      81 GSDT 84
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12985-13052 6.18e-12

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 66.50  E-value: 6.18e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 12985 EVSEGDTIKLVCEVSKPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCRLPSSR 13052
Cdd:cd20967       8 QVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEK 75
I-set pfam07679
Immunoglobulin I-set domain;
21983-22063 6.29e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 6.29e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21983 ITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNVK 22062
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 22063 V 22063
Cdd:pfam07679    90 V 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
19817-19897 6.46e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 66.76  E-value: 6.46e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDS-TPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  19896 KV 19897
Cdd:smart00410    84 TV 85
fn3 pfam00041
Fibronectin type III domain;
22465-22548 6.68e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.67  E-value: 6.68e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22465 GPPQNLKIKEVTKTSVTLTWEPPlLDGGSKIKNYIVEKRESTRKAYSTVATNC-HKTSWKIDQLQEGCSYYFRVLAENEY 22543
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPgTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 22544 GIGLP 22548
Cdd:pfam00041    80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
26888-26970 6.94e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.67  E-value: 6.94e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26888 SPPEKLGVTSVSKDSVSLSWLKPEhDGGSRILHYVVEALEKG-QKNWVKCAVVKTTHHV-VSGLREGHEYFFRVFAENQA 26965
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNsGEPWNEITVPGTTTSVtLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 26966 GLSDP 26970
Cdd:pfam00041    80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
17923-18005 7.22e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.67  E-value: 7.22e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17923 GPPKDLHHVDVDKTEVSLVWNKPDrDGGSPITGYLVEYQEEGAKDWIKFKTVKN--LECVVTGLQQGKTYRFRVKAENII 18000
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGttTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 18001 GLGLP 18005
Cdd:pfam00041    80 GEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4497-4559 1.02e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.81  E-value: 1.02e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  4497 IHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAG 4559
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8905-8981 1.03e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.03e-11
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   8905 TVGLPVVFECAVSGSEPISVSWYKDG-KPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPIGSASSSAKLI 8981
Cdd:smart00410     7 KEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32319-32396 1.16e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.16e-11
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  32319 EGQSVCFEIRVSGIPAPTLKWEKDG-QPLSLGPHIEIVHEGLDYYaLHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:smart00410     8 EGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTST-LTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9006-9074 1.19e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.43  E-value: 1.19e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9006 ADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEV-GKDSCTA 9074
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8428-8511 1.25e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.25e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8428 PESIKVTTGDTCTLECMVSGTPELSTKWFKDG-KELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCT 8506
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   8507 VSIQV 8511
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1807-1889 1.32e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.32e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNG-QLIRKSKRFRVRYDG-IHYLDIVDCKSYDTGEVKVTAENPEGVTEHK 1884
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGsTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   1885 VKLEI 1889
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8054-8135 1.32e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.32e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8054 PVSVDLALGESGSFKCHVTGTAPIKITWAKDNRE-IRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDSCS 8132
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ...
gi 1958765569   8133 AQL 8135
Cdd:smart00410    81 TTL 83
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6072-6162 1.36e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 66.07  E-value: 1.36e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6072 PPSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVA 6151
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  6152 GDNACSGILTV 6162
Cdd:cd20972      81 GSDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
22563-22644 1.41e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.51  E-value: 1.41e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22563 PPGKITLMDVTRNSVSLSWEKPEhDGGSRILGYIVEMQSKGS-DKWATCATVKVT-EATITGLIQGEEYSFRVSAQNEKG 22640
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 22641 ISDP 22644
Cdd:pfam00041    81 EGPP 84
fn3 pfam00041
Fibronectin type III domain;
24919-25002 1.51e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.51  E-value: 1.51e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24919 PPVGPVKFDEVSADFVVISWEPPAYTGGcQISNYIVEKRDTTTTN-WQMVSATVARTTIKVSKLKTGTEYQFRIFAENRY 24997
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 24998 GKSTP 25002
Cdd:pfam00041    80 GEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5143-5225 1.60e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.60  E-value: 1.60e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5143 PSQLLKKGDATQLVCKVTGTPPIKITWFANDRE-LRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTS 5221
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   5222 IVIV 5225
Cdd:smart00410    82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
15920-16006 1.65e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 65.74  E-value: 1.65e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15920 IKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIeKPTDALNITKEEVSrseakTELSIPKAVREDKGTYTITASNRLGSVF 15999
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPL-RSSDRFKVTYEGGT-----YTLTISNVQPDDSGKYTCVATNSAGEAE 83

                    ....*..
gi 1958765569 16000 RNVHVEV 16006
Cdd:pfam07679    84 ASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
15097-15178 1.67e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.51  E-value: 1.67e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15097 DVEVHNPTAKAMTITWKPPLyDGGSKIMGYIIEKLAKG-EDRWKRCNEHLVPVlTYTAKGLEEGKEYQFRVRAENAAGIG 15175
Cdd:pfam00041     5 NLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNsGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    ...
gi 1958765569 15176 EPS 15178
Cdd:pfam00041    83 PPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19604-19687 1.72e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.33  E-value: 1.72e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19604 PSEPKNARVTKVNKDCIFVAWDRPDSDGG-SPITGYLIERKERNSlLWVKANdTIVRSTEYPCAGLVEGLEYSFRIYALN 19682
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  19683 KAGSS 19687
Cdd:smart00060    79 GAGEG 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6370-6432 1.82e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.04  E-value: 1.82e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  6370 VSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVG 6432
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30147-30230 1.99e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.33  E-value: 1.99e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30147 PLVPTKLEVVDVTKSTVTLAWEKPLYDGG-SRLTGYVLEACKAGtERWmKVVTLKPTVLDHTVISLNEGEQYLFRVRAQN 30225
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEW-KEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  30226 EKGVS 30230
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
2843-2926 2.13e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 65.36  E-value: 2.13e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2843 HITKTMRNIEVPETKAASFECEVSHFNVPS-MWLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVC----GN 2917
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEvSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2918 DQVSATLTV 2926
Cdd:pfam07679    82 AEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
21381-21465 2.26e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.26e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21381 GPVLNLRPTDITKDSVTLHWDLPLiDGGSRITNYIVEKREATRKSYS-TVTTKCHKCTYKVTGLTEGCEYFFRVMAENEY 21459
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 21460 GIGEPT 21465
Cdd:pfam00041    80 GEGPPS 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6259-6350 2.30e-11

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 65.52  E-value: 2.30e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASD---KYQMTFIDSVAVMQMNSLGTEDSGDFICEAQ 6335
Cdd:cd20951       1 PEFIIRLQ-SHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAK 79
                            90
                    ....*....|....*
gi 1958765569  6336 NPAGSTSCSTKVIVK 6350
Cdd:cd20951      80 NIHGEASSSASVVVE 94
fn3 pfam00041
Fibronectin type III domain;
24332-24417 2.35e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.35e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24332 GPPKSLEVTNIAKDSMTVCWNRPDsDGGSEIIGYIVEKRD-RSGIRWIKCNKRRITDlRLRVTGLTEDHEYEFRVSAENA 24410
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPkNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 24411 AGVGEPS 24417
Cdd:pfam00041    79 GGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
28270-28355 2.47e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.47e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28270 GPPGKPVIYNVTSDGMSLTWDAPVyDGGSEVTGFHVEKKERNSI-LWQRVNTSPISgREYRATGLIEGLDYQFRVYAENS 28348
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGePWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 28349 AGLSSPS 28355
Cdd:pfam00041    79 GGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
23836-23918 2.61e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.61e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23836 DPPKGpVKFDEVSAESITLSWNPPLYTGGcQITNYIVQKRDT-TTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENR 23914
Cdd:pfam00041     1 SAPSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....
gi 1958765569 23915 YGQS 23918
Cdd:pfam00041    79 GGEG 82
fn3 pfam00041
Fibronectin type III domain;
21479-21560 2.67e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.74  E-value: 2.67e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21479 PPDSLNIMDITKNTVSLAWPKPRhDGGSKITGYVIEAQRKGS-DQWTHISTVKGL-ECVVRNLTEGEEYTFQVMAVNSAG 21556
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 21557 RSAP 21560
Cdd:pfam00041    81 EGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
24832-24913 2.98e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 64.83  E-value: 2.98e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24832 TYSVQAGEDLKIEIPVIGRPRPKISWVKDG-EPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLS 24910
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  24911 VIV 24913
Cdd:smart00410    83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
21772-21857 3.03e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.74  E-value: 3.03e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21772 GPPGTPQVTAVTKDSMTISWHEPlSDGGSPILGYHIERKERNGI-LWQTVSkalVPGNI--FKSTGLTDGIAYEFRVIAE 21848
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGePWNEIT---VPGTTtsVTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 21849 NMAGKSKPS 21857
Cdd:pfam00041    77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
2407-2490 3.08e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.97  E-value: 3.08e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2407 VITPLKDVNVIEGTKAVLECKVS---VPDVTsvkWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYKL----MV 2479
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTgtpDPEVS---WFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSA 79
                            90
                    ....*....|.
gi 1958765569  2480 GRVETSCNLSV 2490
Cdd:pfam07679    80 GEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32209-32293 3.20e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 64.83  E-value: 3.20e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  32209 NKTAYVGENVRFGVTITVHPEPRVTWYKsgQKIKPGDDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARNKHGEDSCK 32288
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYK--QGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  32289 AKLTV 32293
Cdd:smart00410    81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
21587-21667 3.60e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.59  E-value: 3.60e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITIQ 21666
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 21667 V 21667
Cdd:pfam07679    90 V 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7969-8036 3.83e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.89  E-value: 3.83e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7969 VAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLGTASSS 8036
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9292-9380 4.05e-11

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 64.75  E-value: 4.05e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKG--KWRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKH 9369
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNgvPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|.
gi 1958765569  9370 GEIESNVNLQV 9380
Cdd:cd20951      83 GEASSSASVVV 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9199-9266 4.22e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.89  E-value: 4.22e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9199 LQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSDTSK 9266
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7293-7376 4.45e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 64.53  E-value: 4.45e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....
gi 1958765569  7373 GSDT 7376
Cdd:cd20972      81 GSDT 84
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5041-5131 4.54e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 64.53  E-value: 4.54e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5041 PPSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVA 5120
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  5121 GSVECSANLFV 5131
Cdd:cd20972      81 GSDTTSAEIFV 91
I-set pfam07679
Immunoglobulin I-set domain;
26706-26786 4.55e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.59  E-value: 4.55e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26706 KTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAY--IDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTFV 26783
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRfkVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 26784 VKV 26786
Cdd:pfam07679    88 LTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8335-8418 4.63e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 64.06  E-value: 4.63e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8335 SDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIVRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKNDAGVQECYA 8414
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   8415 TLSV 8418
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
31635-31718 4.69e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 4.69e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31635 DPPRGVKVSDVSRDSVNLTWTEPaSDGGSKVTNYIVEKCAT---TAERWLRVGqARETRYTVVNLFGKTSYQFRVIAENK 31711
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnsgEPWNEITVP-GTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 31712 FGLSKPS 31718
Cdd:pfam00041    79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17128-17211 4.83e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.17  E-value: 4.83e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17128 PGPVGIPFLSDNlTNDSCKLTWFSPEDDGG-SPITNYVIQKREADRRaWTPVTYTVTRQNATVQGLIQGKSYFFRIAAEN 17206
Cdd:smart00060     1 PSPPSNLRVTDV-TSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  17207 SIGMG 17211
Cdd:smart00060    79 GAGEG 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8162-8218 5.13e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.50  E-value: 5.13e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8162 ECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:cd00096       4 TCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60
fn3 pfam00041
Fibronectin type III domain;
30150-30232 5.23e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 5.23e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30150 PTKLEVVDVTKSTVTLAWEKPLyDGGSRLTGYVLEACKAGTERWMKVVTLKPTVLDHTVISLNEGEQYLFRVRAQNEKGV 30229
Cdd:pfam00041     3 PSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                    ...
gi 1958765569 30230 SEP 30232
Cdd:pfam00041    82 GPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5901-5966 5.44e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.50  E-value: 5.44e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5901 ATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGVER 5966
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
fn3 pfam00041
Fibronectin type III domain;
15521-15599 6.35e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 6.35e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15521 RVADTSSTTIELEWEPPaFNGGGEIMGYFVDKQLVGTNEWSRctEKMVK--VRQFTVKEIREGADYKLRVSAVNAAGEGP 15598
Cdd:pfam00041     7 TVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWN--EITVPgtTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83

                    .
gi 1958765569 15599 P 15599
Cdd:pfam00041    84 P 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
19417-19500 6.45e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.68  E-value: 6.45e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19417 PEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVT-SSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQK 19495
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  19496 IKVTV 19500
Cdd:smart00410    81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
22952-23038 6.48e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 6.48e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22952 DPPGRPEAIIVTRNSVTLQWKKPTyDGGSKITGYVVEKKELPDGRWMKASFTNIIDTQFEVTGLIEDHRYEFRVIARNAA 23031
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*..
gi 1958765569 23032 GvFSEPS 23038
Cdd:pfam00041    80 G-EGPPS 85
fn3 pfam00041
Fibronectin type III domain;
16535-16615 6.93e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 6.93e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16535 ITKNTVHLSWKPPKnDGGSPVTHYIVEClaWDPTGKKKEAWRqcnRRDVEELEFTVEDLVEGGEYEFRVKAVNEAGVSKP 16614
Cdd:pfam00041    11 VTSTSLTVSWTPPP-DGNGPITGYEVEY--RPKNSGEPWNEI---TVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84

                    .
gi 1958765569 16615 S 16615
Cdd:pfam00041    85 S 85
I-set pfam07679
Immunoglobulin I-set domain;
12711-12782 7.05e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 7.05e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12711 LRPLKDVTVTAGETATFDCELS-YEDIPVEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAK 12782
Cdd:pfam07679     4 TQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6085-6162 7.39e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.68  E-value: 7.39e-11
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569   6085 VLGSSIHMECKVSGSLPINAQWFKDG-KEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAGDNACSGILTV 6162
Cdd:smart00410     7 KEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
26198-26284 7.50e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 7.50e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26198 DPPGQPEVTNITRKSVSLKWSKPRyDGGAKITGYIVERRELPDGRWLKcNFTNV-QETYFEVTELTEDQRYEFRVFARNA 26276
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWN-EITVPgTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*...
gi 1958765569 26277 AdSVSEPS 26284
Cdd:pfam00041    79 G-GEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
15315-15400 9.38e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 9.38e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15315 GPPINFVFEDIRKDSVLCKWEPPlDDGGSEIINYTLEKKDKTKPDSE-WIVITSTLRNckYSVTKLIEGKEYLFRVRAEN 15393
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTS--VTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 15394 RFGPGPP 15400
Cdd:pfam00041    78 GGGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6654-6725 9.62e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.29  E-value: 9.62e-11
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569   6654 VLECKVAGSSPISIAWFHEK-TKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTV 6725
Cdd:smart00410    13 TLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
14907-14988 9.81e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.29  E-value: 9.81e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14907 DIVVIEGEKLSIPVPFRAVPVPTVSWHKDG-KEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASIN 14985
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  14986 VKV 14988
Cdd:smart00410    83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
23250-23335 1.07e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 1.07e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23250 DAPKAPEVTAVTKDSMIVVWERPaSDGGSEILGYVLEKRDKEGIRWTRcHKRLIG-ELRLRVTGLLENHNYEFRVSAENA 23328
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWN-EITVPGtTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 23329 AGLSEPS 23335
Cdd:pfam00041    79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18613-18696 1.13e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.02  E-value: 1.13e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18613 PGEPENLHIADKGKTFVYLKWRRPDYDGG-SPNLSYHVERRLKGSaDWERVHKgSIKETHYMVDKCVENQIYEFRVQTKN 18691
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  18692 EGGES 18696
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
28881-28957 1.19e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.19e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 28881 VRAGASIRLFIAYQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFTVKV 28957
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLrsSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12798-12881 1.24e-10

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 63.21  E-value: 1.24e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12798 EFTKPLEDQTVEEEATAVLECEVSRE-NAKVKWFKNGTEI---LKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAKD- 12872
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNi 81
                            90
                    ....*....|..
gi 1958765569 12873 ---FKTSCNLNV 12881
Cdd:cd20951      82 hgeASSSASVVV 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3468-3550 1.25e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.91  E-value: 1.25e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3468 SDVEISIEDVAKLSVTVVGCPKPKIQWFFNGM-LLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYGRAVCSA 3546
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   3547 HLKV 3550
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5048-5131 1.38e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.91  E-value: 1.38e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5048 PESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGS-CYITKEASESSLELYAVKTTDSGTYTCKVSNVAGSVECS 5126
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   5127 ANLFV 5131
Cdd:smart00410    81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
29060-29141 1.40e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 1.40e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29060 PPRRLDVVDTSKSSAVLAWLKPEhDGGSRITSYLLEMRQKGS-DFWVE---AGHTKqlTFTVERLVENTEYEFRVKAKND 29135
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEitvPGTTT--SVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 29136 AGYSEP 29141
Cdd:pfam00041    79 GGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
33230-33319 1.41e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.41e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33230 PKITQSLK-AEASR-DIAKLTCAVESSALcaKEVAWYKDGKKLKENGHFQFHYSaDGTYELKIHNLSESDCGEYVCEVSG 33307
Cdd:pfam07679     1 PKFTQKPKdVEVQEgESARFTCTVTGTPD--PEVSWFKDGQPLRSSDRFKVTYE-GGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|..
gi 1958765569 33308 EGGTSKTSFQFT 33319
Cdd:pfam07679    78 SAGEAEASAELT 89
I-set pfam07679
Immunoglobulin I-set domain;
12354-12428 1.44e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.44e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12354 FITPLSDVKVFEKDEAKFECEVSREPK-TFRWLKGTQEIAGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAEDK 12428
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
I-set pfam07679
Immunoglobulin I-set domain;
26311-26391 1.47e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.47e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26311 IVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNCK 26390
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 26391 V 26391
Cdd:pfam07679    90 V 90
I-set pfam07679
Immunoglobulin I-set domain;
25229-25310 1.51e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.51e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25229 IIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETaARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPITV 25308
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS-DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569 25309 KV 25310
Cdd:pfam07679    89 TV 90
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11121-11427 1.65e-10

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 70.18  E-value: 1.65e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11121 PEVPKEvvPEKKVAVPKKPEVPPAKVPEVPKKPVVEEKPVIEEKPaipvaeKVESPPTEVYEEPE----EVAAQEEEPAP 11196
Cdd:NF033839    281 QDTPKE--PGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKP------QLEKPKPEVKPQPEkpkpEVKPQLETPKP 352
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11197 VVEEEeyeappppapeipvpqvPEEPKKVV---PEKKypvikkpeppppkvpEVSKKPAPMKKVPVVKKPEPPEAEVPEV 11273
Cdd:NF033839    353 EVKPQ-----------------PEKPKPEVkpqPEKP---------------KPEVKPQPETPKPEVKPQPEKPKPEVKP 400
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11274 PKKLAPVKKEPVPVTKKPEVLPEkvPEAPKkitPEKRESapvpeepeappapveeiPEETIYEEKATITIGRKETPPvee 11353
Cdd:NF033839    401 QPEKPKPEVKPQPEKPKPEVKPQ--PEKPK---PEVKPQ-----------------PEKPKPEVKPQPEKPKPEVKP--- 455
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 11354 reierfiQPEEPGMEPQPE-ETPVQEPEPEKKVIEKPKLKPRPPIRAPSPPKEDVKEKIFQLKAVSKKKVPEKPE 11427
Cdd:NF033839    456 -------QPETPKPEVKPQpEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNKPK 523
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16940-17016 1.72e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.63  E-value: 1.72e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  16940 KVTDWTKSSVDLEWSPPLKDGG-SKITGYIVEYKEEGKEEWEKGKDkeVRGTKLVVTGLKEGAFYKFRVRAVNIAGVG 17016
Cdd:smart00060     8 RVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVT--PSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
23645-23726 1.75e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 1.75e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23645 PPGKITVDDVTRNSVSLSWTKPEhDGGSKIIQYIVEMQAKNT-DKWSECARVKSL-EAVITSLTQGEEYLFRVIAVNEKG 23722
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 23723 RSDP 23726
Cdd:pfam00041    81 EGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
25918-25996 1.85e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 62.66  E-value: 1.85e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 25918 VKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIV 25996
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
15919-16006 1.90e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.52  E-value: 1.90e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15919 TIKVKAGEPVNIPADVTGLPMPKIEWSKN--EKVIEKPtdalnitKEEVSRSEAKTELSIPKAVREDKGTYTITASNRLG 15996
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQggKLLAESG-------RFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG 75
                             90
                     ....*....|
gi 1958765569  15997 SVFRNVHVEV 16006
Cdd:smart00410    76 SASSGTTLTV 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8421-8511 1.96e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 62.60  E-value: 1.96e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8421 PATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8501 GKDSCTVSIQV 8511
Cdd:cd20972      81 GSDTTSAEIFV 91
I-set pfam07679
Immunoglobulin I-set domain;
13336-13419 2.23e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 2.23e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13336 EFVEHLEDQTVTEFDDAVFSCQLS-REKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVEDR--- 13411
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*....
gi 1958765569 13412 -KSRARLFV 13419
Cdd:pfam07679    82 aEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
19605-19690 2.35e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.35e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19605 SEPKNARVTKVNKDCIFVAWDRPDsDGGSPITGYLIERKERNSLlWVKANDTIVRST-EYPCAGLVEGLEYSFRIYALNK 19683
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSG-EPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 19684 AGSSPPS 19690
Cdd:pfam00041    79 GGEGPPS 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8713-8786 2.35e-10

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 62.22  E-value: 2.35e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  8713 YSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKDS 8786
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
fn3 pfam00041
Fibronectin type III domain;
29354-29439 2.37e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.37e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29354 SAPTRPEVYYVSANAMSIRWEEPyHDGGSKIVGYWVEKKERNTILWVKENKVPCLECNYKVTGLVEGLEYQFRTYALNAA 29433
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 29434 GVSKAS 29439
Cdd:pfam00041    80 GEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33898-33984 2.38e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 2.38e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGrrIQSQEQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                     ....*..
gi 1958765569  33978 ATVNINI 33984
Cdd:smart00410    79 SGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8243-8325 2.41e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 2.41e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8243 PVETLKGADVHLECELQGTPPFQVSWYKDKRE-LRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDTcvGS 8321
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS--SG 80

                     ....
gi 1958765569   8322 VTLK 8325
Cdd:smart00410    81 TTLT 84
fn3 pfam00041
Fibronectin type III domain;
19902-19985 2.44e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.44e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19902 GPPASVKINKMYADRAMLSWEPPlEDGGSEITNYIVDKRETSRPN-WAQVSATVPITSCTVEKLIEGHEYQFRICAENKY 19980
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 19981 GVGDP 19985
Cdd:pfam00041    80 GEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8532-8607 2.48e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 2.48e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   8532 GSSVVMECKVFGSPPISVLWLHDG-NAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAGSDECSAPLTV 8607
Cdd:smart00410     9 GESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
12442-12525 2.53e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 2.53e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12442 KFLTPLKDVTAKERENAVFTVELSHDNIP-VSWFKNDQRLHTSKRVSMHDEGKTHSITFKDLSIDDTSQIRVEAMGI--- 12517
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*....
gi 1958765569 12518 -SSEAKLTV 12525
Cdd:pfam07679    82 aEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
14996-15076 2.56e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.56e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14996 KDIKASDITKSSCKLTWEPPEfDGGSPILHYVLERREAGRRTY-IPVMSGENKLSWTVKDLIPNGEYFFRVKAVNKIGGG 15074
Cdd:pfam00041     4 SNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    ..
gi 1958765569 15075 EY 15076
Cdd:pfam00041    83 PP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
22670-22749 2.60e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 2.60e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDD-VPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNVI 22748
Cdd:smart00410     5 TVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84

                     .
gi 1958765569  22749 V 22749
Cdd:smart00410    85 V 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31610-31731 2.77e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.65  E-value: 2.77e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31610 FYVVCAKNRFGIDQKTVELDV---ADVPDPPRGVKVSDVSRDSVNLTWTEPASDGgskVTNYIVEKCATTAERWLRVGQA 31686
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVttpTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 31687 RETRYTVVNLFGKTSYQFRVIAENKFGlsKPSEPSEPTVTKEDKT 31731
Cdd:COG3401     283 TTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLT 325
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
13336-13420 2.93e-10

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 62.44  E-value: 2.93e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13336 EFVEHLEDQTVTEFDDAVFSCQLSRE-KANVKWYRNGREI---KEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVEDR 13411
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNI 81
                            90
                    ....*....|...
gi 1958765569 13412 ----KSRARLFVE 13420
Cdd:cd20951      82 hgeaSSSASVVVE 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7959-8040 3.32e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.75  E-value: 3.32e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7959 KDVHETLGFPVAFECRINGSEPLQVSWYKDG-QLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLGTASSSA 8037
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569   8038 KLI 8040
Cdd:smart00410    82 TLT 84
fn3 pfam00041
Fibronectin type III domain;
26791-26874 3.47e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 3.47e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26791 GPPANITVREVTKETAVLSWDVPEnDGGAPVKNYHIEKREASK-KAWVSVTNNCSRLSYKVTNLQEGAVYYFRVSGENEF 26869
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 26870 GVGVP 26874
Cdd:pfam00041    80 GEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
17340-17420 3.49e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 3.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17340 LTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFCQVN 17419
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 17420 V 17420
Cdd:pfam07679    90 V 90
I-set pfam07679
Immunoglobulin I-set domain;
2136-2222 3.49e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 3.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2136 FTQELQDVVAKEKDTmATFECETS-EPFVKVKWYKDGIEVHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSCVlVEDE-- 2212
Cdd:pfam07679     3 FTQKPKDVEVQEGES-ARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV-ATNSag 80
                            90
                    ....*....|
gi 1958765569  2213 NIKTTAKLIV 2222
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
2931-3013 4.24e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.50  E-value: 4.24e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2931 ITSMLKDINAEEKDTITFEVTVnyEG---ISYKWLKNGVEIKSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVA----G 3003
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTV--TGtpdPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaG 80
                            90
                    ....*....|
gi 1958765569  3004 KATSTATLYV 3013
Cdd:pfam07679    81 EAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1254-1337 4.28e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.37  E-value: 4.28e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   1254 KNYRILEGMGVTFHCKMSGYPLPKIAWYKDG-KRIRRGERYQMDFlQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICS 1332
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSR-SGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   1333 GKLYV 1337
Cdd:smart00410    81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
18909-18994 4.78e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 4.78e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18909 GRPDPPEVTKVSKEEMTVVWNAPEYDGGKsITGYYLEKKEK-HAVRWVPVNKSAiPERRLKVQNLLPGHEYQFRVKAENE 18987
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKnSGEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 18988 VGIGEPS 18994
Cdd:pfam00041    79 GGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4499-4569 4.81e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.37  E-value: 4.81e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569   4499 LECQVDEDRKVSITWSKDGQKLPAGKD-YKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAGSSSSSATVAV 4569
Cdd:smart00410    14 LSCEASGSPPPEVTWYKQGGKLLAESGrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
12530-12614 4.99e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.44  E-value: 4.99e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12530 PYFTGKLQDYTGVEKDEVVLQCEISKADAP-VKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC----DCG 12604
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPvVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSClatnSVG 81
                            90
                    ....*....|
gi 1958765569 12605 TDQTSGKLDI 12614
Cdd:cd20972      82 SDTTSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5808-5870 5.05e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 60.81  E-value: 5.05e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5808 VELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANEGG 5870
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
I-set pfam07679
Immunoglobulin I-set domain;
12798-12881 5.25e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.50  E-value: 5.25e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12798 EFTKPLEDQTVEEEATAVLECEVS-RENAKVKWFKNGTEILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAKD---- 12872
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsage 81

                    ....*....
gi 1958765569 12873 FKTSCNLNV 12881
Cdd:pfam07679    82 AEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
14798-14884 5.27e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 5.27e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14798 SPPLDLHVTDAGRKHIAIAWKPPEkNGGSPIIGYHVEMCPVGTEKWMRVNSRP-------IKDLKfkveegvvPDKEYVL 14870
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPgtttsvtLTGLK--------PGTEYEV 71
                            90
                    ....*....|....
gi 1958765569 14871 RVRAVNAVGVSDPS 14884
Cdd:pfam00041    72 RVQAVNGGGEGPPS 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1516-1607 5.29e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.44  E-value: 5.29e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIvpHKYPRIRIEGTKGEAALKIDSTISQDSAWYTATAINK 1595
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKEL--QNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  1596 AGRDTTRCKVNI 1607
Cdd:cd20972      80 VGSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8163-8231 6.38e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.98  E-value: 6.38e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8163 CKIGGSPEIKVLWYKDEVE-IQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARNAAGSASSSTSLKV 8231
Cdd:smart00410    16 CEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
24544-24624 6.39e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.12  E-value: 6.39e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24544 KGIVVRAGGSARIHIPFKGRPTPEITWSKEEGEFT--DKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVT 24621
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 24622 VKV 24624
Cdd:pfam07679    88 LTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
24544-24624 7.04e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.98  E-value: 7.04e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24544 KGIVVRAGGSARIHIPFKGRPTPEITWSKEEGE---FTDKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFV 24620
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  24621 TVKV 24624
Cdd:smart00410    82 TLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8611-8700 7.53e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 60.97  E-value: 7.53e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDS-VAELELFDVDTSQSGDYTCIVSNEA 8689
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  8690 GRASCTTQLFV 8700
Cdd:cd05744      81 GENSFNAELVV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
26706-26786 7.91e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 7.91e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26706 KTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDL---RTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTF 26782
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  26783 VVKV 26786
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
18810-18894 8.10e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 8.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18810 GPVRNLKIADVSSDRCTIRWDPPEDDGGcEIQNYILEKCESKRM-VWSTYSANVLTPGATVTRLIEGNEYIFRVRAENKI 18888
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 18889 GTGPPT 18894
Cdd:pfam00041    80 GEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1044-1127 8.39e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 8.39e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   1044 PVVQKLVEGGSVVFECQIGGNPKPHVYWKKSG-VPLTTGYRYKVSYNKQTGEcrLVIS-MTFaDDAGEYTIVIRNKHGET 1121
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTST--LTISnVTP-EDSGTYTCAATNSSGSA 77

                     ....*.
gi 1958765569   1122 SASASL 1127
Cdd:smart00410    78 SSGTTL 83
fn3 pfam00041
Fibronectin type III domain;
14697-14782 8.59e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 8.59e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14697 GPPYALTVVDVTKRHVDLKWEPPKnDGGRPIQRYIIEKKEKLGTRWVKAGKTSGPDCNFRVTDVIEGTEVQFQVRAENEA 14776
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 14777 GVGHPS 14782
Cdd:pfam00041    80 GEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
29966-30046 8.90e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 8.90e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29966 KTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLA---NRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATV 30042
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  30043 LVKV 30046
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6359-6436 9.16e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 9.16e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569   6359 PPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQ-LRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVGSDTC 6436
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28568-28647 9.86e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 60.32  E-value: 9.86e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28568 VGPIRFTNITGEKMTLWWEAPLNDGC-APVTHYIIEKRETSRlAWALIEDHCEAQSYTAIKLITGNEYQFRVSAVNKFGV 28646
Cdd:smart00060     4 PSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82

                     .
gi 1958765569  28647 G 28647
Cdd:smart00060    83 G 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5336-5411 1.00e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 1.00e-09
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   5336 GGTAAFQATLKGSLPITVTWLKDNDE-ITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSV 5411
Cdd:smart00410     9 GESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4760-4850 1.16e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.44  E-value: 1.16e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4760 PTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDG--KIKMSFSSGVAVLTISDVQIGLGGKYTCLAENE 4837
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  4838 AGSQTSVGELIVK 4850
Cdd:cd20974      81 SGQATSTAELLVL 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27975-28056 1.17e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 60.32  E-value: 1.17e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27975 PAPIRDLSMKDSTKTSVVLSWTKPDFDGG-SIITDYLVERKGKGEQAWSHAGISKTCEIEIGQLKEQSVLEFRVSARNEK 28053
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  28054 GQS 28056
Cdd:smart00060    81 GEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
18720-18805 1.28e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.21  E-value: 1.28e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18720 SGVLTVKAGDTIRLEAGVRGKPFPEVAWTKDkDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAGSFVA 18799
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQ-GGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                     ....*.
gi 1958765569  18800 YATVNV 18805
Cdd:smart00410    80 GTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6172-6255 1.30e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.21  E-value: 1.30e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6172 PERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLE-GSTSFLNLYSVDASKTGQYTCQVTNDVGSDSCT 6250
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRsGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   6251 TMLLV 6255
Cdd:smart00410    81 TTLTV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6728-6818 1.30e-09

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 60.34  E-value: 1.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6728 PPSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGAREL-VKGDRCNIyfEDTVAELELFNIDVSQSGEYTCVVSNN 6806
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTC--EAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  6807 AGQASCTTRLFV 6818
Cdd:cd20976      79 AGQVSCSAWVTV 90
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7386-7489 1.31e-09

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 60.74  E-value: 1.31e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7386 PPRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDKGEvIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKND 7465
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQ-IQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENK 79
                            90       100
                    ....*....|....*....|....
gi 1958765569  7466 AGMRECSALLTvleparIVEKPEP 7489
Cdd:cd05762      80 LGSRQAQVNLT------VVDKPDP 97
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
11643-11719 1.35e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.21  E-value: 1.35e-09
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  11643 SVGSSAIFECLVS-PSTAITTWMKDGSN-IRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLIV 11719
Cdd:smart00410     7 KEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7765-7852 1.38e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 60.51  E-value: 1.38e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7765 FVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPL---SQSPNCGITTTERSSILEILESTIEDYAQYACLIENEA 7841
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|.
gi 1958765569  7842 GQDICEALVSV 7852
Cdd:cd20951      83 GEASSSASVVV 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5246-5313 1.42e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 59.65  E-value: 1.42e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5246 VMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEVGSSTCS 5313
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
I-set pfam07679
Immunoglobulin I-set domain;
12530-12601 1.46e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.96  E-value: 1.46e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12530 PYFTGKLQDYTGVEKDEVVLQCEISKADAP-VKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC 12601
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73
I-set pfam07679
Immunoglobulin I-set domain;
30658-30736 1.49e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.96  E-value: 1.49e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30658 VFVRQGGVIRLTIPIKGKPFPICKWTKEGQDV--SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVK 30735
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrsSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 30736 V 30736
Cdd:pfam07679    90 V 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4213-4286 1.54e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 1.54e-09
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   4213 GDTVHLTSSISNAK--EVNWYF-KGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNGKAMTSAKLTV 4286
Cdd:smart00410     9 GESVTLSCEASGSPppEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28480-28560 1.76e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 1.76e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDGVE-IERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEITV 28558
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  28559 KV 28560
Cdd:smart00410    84 TV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5798-5878 1.78e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 1.78e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5798 EPVEVVKDSDVELECEVMGTTPFEVTWLKNN-KEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANEGGSCACTA 5876
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ..
gi 1958765569   5877 RV 5878
Cdd:smart00410    82 TL 83
PTZ00121 PTZ00121
MAEBL; Provisional
10032-10560 1.83e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 1.83e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10032 RRMEEEKV--QVTKVPEVSKKIVPQKPSRTPVQEEII----EVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKK 10105
Cdd:PTZ00121   1218 RKAEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIrkfeEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10106 TvtEEKIHVAVSKKIEPPPKVPEPPKKPVPEEVVPVPIPKKVEPPAVKVPEAPKKPVPEEKKPVPIPKKEPAA------- 10178
Cdd:PTZ00121   1298 A--EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekkkee 1375
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10179 PPKVPEAPKKPAPEEKTAVPVAKKKEAPPPKVTEVQKKVVTEEKITIIPQREESPPPAvpEIPKKKVPEEKRP--VPRKE 10256
Cdd:PTZ00121   1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKAdeAKKKA 1453
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10257 EVPPPKAPPKKPVPEEVVPVPIPKKAPP--RAEVSKKTVVEEKKFAAEERLSMAVPQRVELMRHEEEEWTYSEEEEqvsv 10334
Cdd:PTZ00121   1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---- 1529
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10335 svyreEERDEEEAEITEYEVLEEPEEYVVEEKLHVISKRVEVEPAKVPEKHEKKIIPRPKVPAKIEEPPPTKVPEPPKKm 10414
Cdd:PTZ00121   1530 -----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE- 1603
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10415 vPEKKVPAPPPKKVPPAKAPEEPKKPVPERRVPAEVVEIEEPPPTKvTEKHMKITQEEKVLVAVTKKEEPPRARVPEEPK 10494
Cdd:PTZ00121   1604 -EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 10495 KVVPEEKFPKLKPRREEEPPAKVTEVRKRAVKEEKVSIEVPKREprPTKEVTVTEEKKwsytREEE 10560
Cdd:PTZ00121   1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE--EENKIKAEEAKK----EAEE 1741
I-set pfam07679
Immunoglobulin I-set domain;
23462-23540 2.14e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.58  E-value: 2.14e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23462 KVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSS--FTSLVLDNVNRYDSGKYTLTLENSSG--TKSAF 23537
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEggTYTLTISNVQPDDSGKYTCVATNSAGeaEASAE 87

                    ...
gi 1958765569 23538 VTV 23540
Cdd:pfam07679    88 LTV 90
I-set pfam07679
Immunoglobulin I-set domain;
2582-2664 2.16e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.58  E-value: 2.16e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2582 ISKPLTDQTVAESQEAVFECEV-ANPESEGEWLKDGKHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYTYKVATS---- 2656
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVtGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSagea 82

                    ....*...
gi 1958765569  2657 KTSAKLKV 2664
Cdd:pfam07679    83 EASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
20397-20479 2.17e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.17e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20397 GPVVDLKVLAVTKSSCTIGWKKPRsDGGSRITGYVVDF--LTEENKWQRVMKSLSL-QYSTKDLKEGKEYTFRVSAENEN 20473
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYrpKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 20474 GEGTPS 20479
Cdd:pfam00041    80 GEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
16425-16508 2.21e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.21e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16425 GPPKDLKVSDITRGSCRLSWKMPDDDGGDrIKGYVIEKKTID-GKAWTKVNPNCGSTAFVVPDLISEQQYFFRVRAENRF 16503
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 16504 GIGPP 16508
Cdd:pfam00041    80 GEGPP 84
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12887-12958 2.22e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 59.74  E-value: 2.22e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12887 EFLRPLTDLQVKEKETARFECEIS-KENVKVQWFKDGAEI---KKGKKYDIISKGAVRILVINKCLLNDEAEYSCE 12958
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAV 77
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
17738-17818 2.38e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.44  E-value: 2.38e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17738 REQHIKVGDTLRLSAIIKGVPFPKVTWKKEDRE---APTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSV 17814
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  17815 KVLV 17818
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
31338-31423 2.42e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.42e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31338 SVPGKPTITAVTKDSCVVAWKPPaSDGGAKIRNYYLEKREKKQNKWIAVTTEEIRETVFSVQNLIEGLEYEFRVKCENLG 31417
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 31418 GESEWS 31423
Cdd:pfam00041    80 GEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
32111-32170 2.45e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.58  E-value: 2.45e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32111 QVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 32170
Cdd:pfam07679    31 EVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6654-6715 2.74e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 58.88  E-value: 2.74e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  6654 VLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAG 6715
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5424-5504 2.98e-09

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 59.14  E-value: 2.98e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5424 IDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGrsSCKASIN 5503
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG--EKSATIN 79

                    .
gi 1958765569  5504 V 5504
Cdd:cd05748      80 V 80
I-set pfam07679
Immunoglobulin I-set domain;
20213-20295 3.22e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 3.22e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20213 KTLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIV 20292
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 20293 VKV 20295
Cdd:pfam07679    88 LTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15521-15597 3.27e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 3.27e-09
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  15521 RVADTSSTTIELEWEPPAF-NGGGEIMGYFVDKQLVGTnEWSRCTEKmVKVRQFTVKEIREGADYKLRVSAVNAAGEG 15597
Cdd:smart00060     8 RVTDVTSTSVTLSWEPPPDdGITGYIVGYRVEYREEGS-EWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
12887-12959 3.62e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 3.62e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 12887 EFLRPLTDLQVKEKETARFECEIS-KENVKVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEV 12959
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVA 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
20504-20584 3.63e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.06  E-value: 3.63e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20504 YLAKENSNFRLKIPIKGKPAPSVSWKK-GEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSI 20582
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  20583 KV 20584
Cdd:smart00410    84 TV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5423-5504 3.88e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.67  E-value: 3.88e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5423 SIDVTQGDPATLQVKFSGTKEISAKWFKDGQE-LTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKAS 5501
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   5502 INV 5504
Cdd:smart00410    83 LTV 85
I-set pfam07679
Immunoglobulin I-set domain;
19128-19207 4.03e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 58.81  E-value: 4.03e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGID-NVVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVK 19206
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPlRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 19207 V 19207
Cdd:pfam07679    90 V 90
I-set pfam07679
Immunoglobulin I-set domain;
13153-13241 4.11e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 58.81  E-value: 4.11e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13153 RIVVPLKDTKVKEQQEAVFNCEVntEGA---KAKWFRNDEAIFDSSKYIILQKDLVYTLRIRDARLDDQANFSVSLTNHR 13229
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTV--TGTpdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|..
gi 1958765569 13230 GEnVKSAANLIV 13241
Cdd:pfam07679    80 GE-AEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
28962-29045 4.34e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 4.34e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28962 GPPGPITFKDVTRGSATLMWDAPLlDGGARIHHYVIEKREASR-RSWQVVSEKCTRQILKVSDLTEGVPYYFRVSAENEY 29040
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 29041 GVGEP 29045
Cdd:pfam00041    80 GEGPP 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9581-9665 4.36e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 58.66  E-value: 4.36e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9581 PAWERHLQDVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKPQGRVKTEV-EHKVHKLTIADVRAEDQGRYTC----KH 9654
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSgLPTPDLFWQLNGKPVRPDSAHKMLVrENGRHSLIIEPVTKRDAGIYTCiarnRA 80
                            90
                    ....*....|.
gi 1958765569  9655 EDLETSAELRI 9665
Cdd:cd05744      81 GENSFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
2494-2577 4.81e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 58.81  E-value: 4.81e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2494 KIIRGLRDLTCTETQNVVFEVELS-HSGIDVVWNFKGQEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGEYAFYA----GE 2568
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2569 NTTSGKLTV 2577
Cdd:pfam07679    82 AEASAELTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
9084-9175 4.89e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 58.75  E-value: 4.89e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9084 PPSFTKKLsETIEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATND 9163
Cdd:cd20972       1 PPQFIQKL-RSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  9164 AGSALCTSSIVI 9175
Cdd:cd20972      80 VGSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5610-5693 5.10e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 5.10e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5610 PQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAAR-SVWKDDTSTILELFSAKAADSGTYICQLSNDVGTTSSK 5688
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   5689 ATIFV 5693
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8712-8793 5.15e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 5.15e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8712 DYSIEKGKPLILEGTFSGTPPISVTWKKNGVN-VTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKDSCSAQ 8790
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   8791 ILI 8793
Cdd:smart00410    83 LTV 85
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11138-11611 5.24e-09

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 65.18  E-value: 5.24e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11138 KPEVPPAKVPEvPKKPvveEKPVIEEKPaIPVAEKVESPPTEVYEEPE----EVAAQEEEPAPVVEEEEYEAPPPPAPEI 11213
Cdd:NF033839    158 KPETPQPENPE-HQKP---TTPAPDTKP-SPQPEGKKPSVPDINQEKEkaklAVATYMSKILDDIQKHHLQKEKHRQIVA 232
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11214 PVPQVPEEPKKVVPEKKYPVikkpeppppkvpevskkpapmkkvPVVKKPEPPEAEVPEVPKKLAPVKKEPVPVTKKPEV 11293
Cdd:NF033839    233 LIKELDELKKQALSEIDNVN------------------------TKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPG 288
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11294 LPEkvPEAPKkitPEKRESapvpeepeappapveeiPEetiyeekatiTIGRKETPPVEEREIERFIQPEEPGMEPQPE- 11372
Cdd:NF033839    289 NKK--PSAPK---PGMQPS-----------------PQ----------PEKKEVKPEPETPKPEVKPQLEKPKPEVKPQp 336
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11373 ETPVQE--PEPEKkviEKPKLKPRPpirapSPPKEDVKEKifqlkavskkkvPEKPEVVEKVEPTPLKvPTAEKKVRKLL 11450
Cdd:NF033839    337 EKPKPEvkPQLET---PKPEVKPQP-----EKPKPEVKPQ------------PEKPKPEVKPQPETPK-PEVKPQPEKPK 395
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11451 PEPKPQPKEevvlksvlrkrpeeeepkvepkkvekvkkpeeppppPKAVEVEAPPEPKPKERKVPEPTKvPEIKPAIPLP 11530
Cdd:NF033839    396 PEVKPQPEK------------------------------------PKPEVKPQPEKPKPEVKPQPEKPK-PEVKPQPEKP 438
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11531 GPEPKPKPEPEVKTMKAPPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKPKGPIKgvAKKTPSPIEAERKKLRPGSGGE 11610
Cdd:NF033839    439 KPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDK--KPSTPNNLSKDKQPSNQASTNE 516

                    .
gi 1958765569 11611 K 11611
Cdd:NF033839    517 K 517
fn3 pfam00041
Fibronectin type III domain;
17823-17906 5.93e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 5.93e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17823 GPPRDLEVSEIRKDSCYLTWKEPlDDGGSVVTNYVVERKDV-ATAQWSPLSTTSKKKSHMAKHLNEGNQYLFRVAAENQY 17901
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 17902 GRGPF 17906
Cdd:pfam00041    80 GEGPP 84
PTZ00121 PTZ00121
MAEBL; Provisional
32984-33612 6.31e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.93  E-value: 6.31e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32984 ASQRRDEEVPKSVFPELTKTEAYAISSFKRTSEMEAASSVRevKSQMTETRESLSSYEHHVSAEMKSAASEEKSLEEkat 33063
Cdd:PTZ00121   1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR--KAEEVRKAEELRKAEDARKAEAARKAEEERKAEE--- 1216
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33064 VRKIKTTLAARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTA-KYKSTFEISSVQASDEGN 33142
Cdd:PTZ00121   1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKKKADEAK 1296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33143 YSVVVENTD---GKQEAQFTLTVQKAKAVEKAVTSPPRVKSPEPRVKSPETVKSPKRVKSPELVASHPKAVSPTETKPTE 33219
Cdd:PTZ00121   1297 KAEEKKKADeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33220 KGQqlpVPAPPKitqslKAEASRDIAKLTCAVESSALCAKEVAWYKDGKKLKEnghfqfhysadgtyELKihnlsesdcg 33299
Cdd:PTZ00121   1377 KKK---ADAAKK-----KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD--------------EAK---------- 1424
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33300 eyvceVSGEGGTSKTSFQFTGQSFKSIHEQVSSTTETKKSVQKTAESAEAKKATQKTAESAEAKKATQKTAESAEAKKPA 33379
Cdd:PTZ00121   1425 -----KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33380 QKTAESAEAKKPAQKTAEPTEAKKQEPIAPESVSSKpvivtglrdttvsSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQS 33459
Cdd:PTZ00121   1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK-------------ADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33460 SKYKLSNDKEEFIL---EILKtetsdgglyscTVANSAGSVSSSCKLTIKAVKDTEAQKVSTQKTSEVTAKKKESVQQEI 33536
Cdd:PTZ00121   1567 EEAKKAEEDKNMALrkaEEAK-----------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
                           570       580       590       600       610       620       630
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33537 SQKVLTSEEikmsEVKSHETLAIKEEASKVLIAEEVKKSAAASLEKSIVHEEVTKTSQASEEVKTHAEIKALSTQM 33612
Cdd:PTZ00121   1636 EQLKKKEAE----EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3312-3392 6.33e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 6.33e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3312 QDAVTSEGRPARFQCQVSGT-DLKVSWYCRD-KKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAVGQVSSTA 3389
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSpPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569   3390 TLR 3392
Cdd:smart00410    82 TLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9588-9665 6.51e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 6.51e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9588 QDVTLKEGQTCTMTCQFS-VPNVKSEWFRNG-RVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTC----KHEDLETSA 9661
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCaatnSSGSASSGT 81

                     ....
gi 1958765569   9662 ELRI 9665
Cdd:smart00410    82 TLTV 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12191-12258 6.63e-09

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 58.02  E-value: 6.63e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12191 EIILKCEVSK-DVPVKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTCDCGTDTTKANVTV 12258
Cdd:cd20967      14 KIRLTVELADpDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
fn3 pfam00041
Fibronectin type III domain;
19502-19589 1.02e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 1.02e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19502 DAPGPPQppfdISEIDADACSLSWHIPlEDGGSNITNYIVEKCDVSRGD-WVTALASVTKTSCRVGKLIPGQEYIFRVRA 19580
Cdd:pfam00041     1 SAPSNLT----VTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75

                    ....*....
gi 1958765569 19581 ENRFGISEP 19589
Cdd:pfam00041    76 VNGGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
31236-31321 1.12e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 1.12e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31236 DKPTGPIVIEaLLKNSVVISWKAPADDGGSwITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQNT 31315
Cdd:pfam00041     1 SAPSNLTVTD-VTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 31316 FGISEP 31321
Cdd:pfam00041    79 GGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
13247-13330 1.12e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 57.65  E-value: 1.12e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13247 RIIEPLKDIETMEKKSVTFWCKVN---RLNVTlkWTKNGEEVAFDNRISYRIDKYKHSLIIKDCGFPDEGEYIVTA---- 13319
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtpDPEVS--WFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsa 79
                            90
                    ....*....|.
gi 1958765569 13320 GQDKSVAELLI 13330
Cdd:pfam07679    80 GEAEASAELTV 90
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2601-2664 1.13e-08

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 57.25  E-value: 1.13e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2601 CEVANPESEGEWLKDGKHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYTYKVATSKTSAKLKV 2664
Cdd:cd20967      19 VELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
25918-25996 1.17e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.52  E-value: 1.17e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25918 VKANDQLKIDIPFKGRPQATVAWKKDG-QVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIV 25996
Cdd:smart00410     6 VKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4862-4942 1.22e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.52  E-value: 1.22e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4862 IQVTAGDPATLEYTVSGTPELKPKWYKDG-RPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTF 4940
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569   4941 TV 4942
Cdd:smart00410    84 TV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9092-9175 1.32e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 1.32e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9092 SETIEETEGNSFKLEGRVAGSQPITIAWYKNNVE-IHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATNDAGSALCT 9170
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   9171 SSIVI 9175
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
24146-24227 1.35e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 1.35e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24146 TIVVNAGETFRLEADVHGKPLPTIEWLR-GDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVN 24224
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  24225 VKV 24227
Cdd:smart00410    83 LTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1430-1507 1.41e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 1.41e-08
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   1430 EGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRAGKSTISVTLTV 1507
Cdd:smart00410     8 EGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
30056-30134 1.64e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 1.64e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30056 VNVKEVSRDSVTITWEIPTiDGGAPVNNYIIEKREA-AMRAFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENIYGIGEP 30134
Cdd:pfam00041     6 LTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1523-1607 1.66e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 1.66e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   1523 KNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKyPRIRIEGTKGEAALKIDSTISQDSAWYTATAINKAGRDTTR 1602
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   1603 CKVNI 1607
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32893-32975 1.80e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.74  E-value: 1.80e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  32893 RSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVE-LQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNYKGEASDYA 32971
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  32972 TLDV 32975
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
31549-31630 2.23e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.74  E-value: 2.23e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31549 VHALRGEVVSIKIPFSGKPDPVITWQK-GQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFGIDQKTVE 31627
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISN-VTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  31628 LDV 31630
Cdd:smart00410    83 LTV 85
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10808-11022 2.28e-08

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 63.25  E-value: 2.28e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10808 PPAKVPEIPKKPEEKVSVPVPKKEKAPPAKVPEvPKKPVPEEKAPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKkv 10887
Cdd:NF033839    292 PSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQ-LEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQ-- 368
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10888 eaPPAKAPEVPPKEVTPEKKVPvvppkkpeapppkvpeppkevvpekkvsmvppKRPEAPPAKV---PEASK-EVVPE-- 10961
Cdd:NF033839    369 --PEKPKPEVKPQPETPKPEVK--------------------------------PQPEKPKPEVkpqPEKPKpEVKPQpe 414
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10962 -KKVSVAPKKKPEAPAVK-VPEAPKKVV---PEKKVPVAAPkKPEAPAAEV---PEVPKAAV-PQKKIPE 11022
Cdd:NF033839    415 kPKPEVKPQPEKPKPEVKpQPEKPKPEVkpqPEKPKPEVKP-QPETPKPEVkpqPEKPKPEVkPQPEKPK 483
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1683-1754 2.42e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.82  E-value: 2.42e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  1683 ECRLTpiGDPTMVVEWLHDGKPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:cd20972      22 ECRVT--GNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
I-set pfam07679
Immunoglobulin I-set domain;
31554-31630 2.55e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 56.50  E-value: 2.55e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31554 GEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFGIDQKTVELDV 31630
Cdd:pfam07679    15 GESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISN-VQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7669-7759 2.59e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.82  E-value: 2.59e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7669 PPSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTNDA 7748
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  7749 GSASCTTHLFV 7759
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4684-4746 2.62e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 55.80  E-value: 2.62e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  4684 ALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEVG 4746
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23749-23830 2.66e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.36  E-value: 2.66e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23749 SSYSVQVGQDLKIEVPISGRPKPSISWTKDGA-PLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAI 23827
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569  23828 EII 23830
Cdd:smart00410    82 TLT 84
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8327-8429 3.08e-08

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 56.89  E-value: 3.08e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8327 PPQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIvRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKND 8406
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQI-QEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENK 79
                            90       100
                    ....*....|....*....|...
gi 1958765569  8407 AGVQECYATLsvlepaTIVEKPE 8429
Cdd:cd05762      80 LGSRQAQVNL------TVVDKPD 96
fn3 pfam00041
Fibronectin type III domain;
24629-24712 3.47e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 3.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24629 GPPQNLAVKEVRKDSVLLVWEPPIiDGGAKVKNYVI---DKRESTRKAYANVSSkcSKTSFKVENLTEGAIYYFRVMAEN 24705
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVeyrPKNSGEPWNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 24706 EFGVGVP 24712
Cdd:pfam00041    78 GGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
18518-18596 4.14e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 4.14e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18518 QNLKVSNVTKENCTISWEnPLDNGGSEITNFIVEYRKPNQKGW--SIVASDVTKRLIKANLLANNEYYFRVCAENKVGVG 18595
Cdd:pfam00041     4 SNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPwnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    .
gi 1958765569 18596 P 18596
Cdd:pfam00041    83 P 83
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6165-6255 4.39e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.05  E-value: 4.39e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6165 PPSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTNDV 6244
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  6245 GSDSCTTMLLV 6255
Cdd:cd20972      81 GSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7771-7852 4.50e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 55.59  E-value: 4.50e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7771 DTSVETGSPIVLEATYSGTPPIAVSWLKNEY-PLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEAGQDICEAL 7849
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   7850 VSV 7852
Cdd:smart00410    83 LTV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3019-3103 4.74e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.89  E-value: 4.74e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3019 EFRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRI---KIQKEKYVHRLLIPSARMSDAGKYTVVA--- 3091
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYKNGVPIDPSSIPgkyKIESEYGVHVLHIRRVTVEDSAVYSAVAkni 81
                            90
                    ....*....|...
gi 1958765569  3092 -GGNMSTANLFVE 3103
Cdd:cd20951      82 hGEASSSASVVVE 94
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
13154-13242 5.03e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.89  E-value: 5.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13154 IVVPLKDTKVKEQQEAVFNCEVNTE-GAKAKWFRNDEAI---FDSSKYIILQKDLVYTLRIRDARLDDQANFSVSLTNHR 13229
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|...
gi 1958765569 13230 GEnVKSAANLIVE 13242
Cdd:cd20951      83 GE-ASSSASVVVE 94
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6839-6902 5.19e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 55.03  E-value: 5.19e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  6839 IILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAGR 6902
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
13067-13148 5.70e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 55.48  E-value: 5.70e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13067 ISKPQNLEILEGEKAEFVCTISKESF-EVQWKRDDQTLESGdKYDIIADgkkRVLVVKDATLQDMGTYVV----MVGAAR 13141
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVpTVRWRKEDGELPKG-RYEILDD---HSLKIRKVTAGDMGSYTCvaenMVGKIE 76

                    ....*..
gi 1958765569 13142 AAAHLTV 13148
Cdd:cd05725      77 ASATLTV 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3025-3102 6.33e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 55.20  E-value: 6.33e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3025 KDIKVLEKKRAMFECEVS-EPDITVQWMKDGQE-LQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVAGGNM----STA 3098
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSgsasSGT 81

                     ....
gi 1958765569   3099 NLFV 3102
Cdd:smart00410    82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
17045-17124 6.57e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 55.34  E-value: 6.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17045 RIVVHAGGVIRIIAYVSGKPPPTVTWNMNERALPQEATIETTAI--SSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIV 17122
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEggTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569 17123 DV 17124
Cdd:pfam07679    89 TV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5346-5401 7.17e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 54.64  E-value: 7.17e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5346 KGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAG 5401
Cdd:cd00096       8 SGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
fn3 pfam00041
Fibronectin type III domain;
29659-29737 7.66e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 7.66e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29659 LTVSRVTEEKCTLAWSLPqEDGGAEITHYIVERRET---SRLNWVIVEAEclTLSYVVTRLIKNNEYTFRVRAVNKYGLG 29735
Cdd:pfam00041     6 LTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnsgEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    ..
gi 1958765569 29736 VP 29737
Cdd:pfam00041    83 PP 84
I-set pfam07679
Immunoglobulin I-set domain;
21296-21369 7.68e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 55.34  E-value: 7.68e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 21296 RTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLK--HRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKS 21369
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAE 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
28080-28152 8.32e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.88  E-value: 8.32e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 28080 IPGAQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDN 28152
Cdd:pfam13927     6 VSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
30257-30340 8.41e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 8.41e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30257 QKTIHVPAGRPIELVIPITGRPPPTASWFF-AGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSET 30335
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  30336 IKVVI 30340
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12715-12792 8.41e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 8.41e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12715 KDVTVTAGETATFDCELSYEDIP-VEWYL-KGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAG----EVQLTAKDFKTQA 12788
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPeVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGtytcAATNSSGSASSGT 81

                     ....
gi 1958765569  12789 NLFV 12792
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28877-28957 8.57e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 8.57e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28877 QTHIVRAGASIRLFIAYQGRPTPTAVWSKPDSNLSI---RADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITF 28953
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  28954 TVKV 28957
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2936-3013 9.55e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 9.55e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2936 KDINAEEKDTITFEVTVN-YEGISYKWLKNGVE-IKSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVA----GKATSTA 3009
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSGT 81

                     ....
gi 1958765569   3010 TLYV 3013
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12359-12433 1.01e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 1.01e-07
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  12359 SDVKVFEKDEAKFECEVSREPK-TFRWLK-GTQEIAGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAEDKRTSGK 12433
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPpEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78
I-set pfam07679
Immunoglobulin I-set domain;
13512-13598 1.12e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.96  E-value: 1.12e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13512 PKIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTK---TVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHG 13588
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSdrfKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 13589 KAEGFINLQV 13598
Cdd:pfam07679    81 EAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2849-2927 1.22e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 1.22e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2849 RNIEVPETKAASFECEVSHFNVPSM-WLKNGVE-IEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVCGND--QVSATL 2924
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVtWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSsgSASSGT 81

                     ...
gi 1958765569   2925 TVT 2927
Cdd:smart00410    82 TLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6829-6910 1.24e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 1.24e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6829 SDHSVEPGKSIILEGTYTGTLPISVTWKKDG-VVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAGRDSCDA 6907
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569   6908 LVS 6910
Cdd:smart00410    82 TLT 84
I-set pfam07679
Immunoglobulin I-set domain;
9498-9578 1.66e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.19  E-value: 1.66e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9498 IENQTVLKDNDAIFEIDIkINYPEIKLSWYKGTEKLEPSNKYEITINGDRHTLRVRNCQLKDQGNYRLVC----GPHIAS 9573
Cdd:pfam07679     7 PKDVEVQEGESARFTCTV-TGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGEAEAS 85

                    ....*
gi 1958765569  9574 AKLTV 9578
Cdd:pfam07679    86 AELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
2228-2312 1.74e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.19  E-value: 1.74e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2228 EFVKELQDIEVPESYSGELECIIS--PEnIEGKWYHNDVELKSNGKYSITSRRGRQNLTVKDVTKEDQGEYCFVV--DGK 2303
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtPD-PEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnSAG 80

                    ....*....
gi 1958765569  2304 KTTCKLKMK 2312
Cdd:pfam07679    81 EAEASAELT 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2045-2128 1.75e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 1.75e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2045 QSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVK-IERSDRIYWYWpEDNVCELVIRDVTAEDSASIMVKAINIAGETSSH 2123
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSR-SGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   2124 AFLLV 2128
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5236-5317 1.84e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 1.84e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5236 KSIEVLKEYDVMLLAEVAGTPPFEITWFKDN-TTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEVGSSTCSA 5314
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569   5315 RVT 5317
Cdd:smart00410    82 TLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28084-28147 1.91e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 1.91e-07
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  28084 QISVRIGHNVHLELPYKGKPKPSISWLKDGL-PLKESEYVRFSKTENKITLSIKNVKKENGGKYT 28147
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYT 67
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4870-4939 1.95e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.49  E-value: 1.95e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4870 ATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETT 4939
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
11648-11714 2.10e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.49  E-value: 2.10e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 11648 AIFECLVSPSTAIT-TWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTST 11714
Cdd:cd00096       1 VTLTCSASGNPPPTiTWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4674-4747 2.13e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.66  E-value: 2.13e-07
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569   4674 EPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQ-IRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEVGK 4747
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS 76
I-set pfam07679
Immunoglobulin I-set domain;
33612-33689 2.18e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.80  E-value: 2.18e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33612 MNITSGQRVTLKANIAGATD--VKWVLNGTELSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCIGKTSQGVVKCQFDLT 33689
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6446-6537 2.27e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.90  E-value: 2.27e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEV-VRESENVRISFVNNVATLQFAKAEPANAGKYICQVKND 6524
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIsTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  6525 GGVRENMASLTVL 6537
Cdd:cd20974      81 SGQATSTAELLVL 93
fn3 pfam00041
Fibronectin type III domain;
16940-17018 2.52e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 2.52e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16940 KVTDWTKSSVDLEWSPPlKDGGSKITGYIVEYKEEGKEEWEKGKDkeVRGTK--LVVTGLKEGAFYKFRVRAVNIAGVGE 17017
Cdd:pfam00041     7 TVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEIT--VPGTTtsVTLTGLKPGTEYEVRVQAVNGGGEGP 83

                    .
gi 1958765569 17018 P 17018
Cdd:pfam00041    84 P 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12185-12258 2.74e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.66  E-value: 2.74e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12185 TGVEKDEIILKCEVSKDVP--VKWFKDG-EEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC----DCGTDTTKANVT 12257
Cdd:smart00410     5 TVKEGESVTLSCEASGSPPpeVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCaatnSSGSASSGTTLT 84

                     .
gi 1958765569  12258 V 12258
Cdd:smart00410    85 V 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33245-33317 3.02e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.28  E-value: 3.02e-07
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  33245 AKLTCAVESSAlcAKEVAWYKDG-KKLKENGHFQFHYSaDGTYELKIHNLSESDCGEYVCEVSGEGGTSKTSFQ 33317
Cdd:smart00410    12 VTLSCEASGSP--PPEVTWYKQGgKLLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12717-12792 3.36e-07

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 53.01  E-value: 3.36e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12717 VTVTAGETATFDCELSYEDIPVEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAKDFKTQANLFV 12792
Cdd:cd20967       7 VQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23064-23145 3.86e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.28  E-value: 3.86e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23064 TVVVQAGESFKIDADIYGKPIPTTQWVKGDQE-LSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVN 23142
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  23143 VKV 23145
Cdd:smart00410    83 LTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23462-23542 4.51e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.89  E-value: 4.51e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23462 KVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEI---RDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFV 23538
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  23539 TVRV 23542
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12804-12881 4.64e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.89  E-value: 4.64e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12804 EDQTVEEEATAVLECEVS-RENAKVKWFKNGTE-ILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAK----DFKTSC 12877
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATnssgSASSGT 81

                     ....
gi 1958765569  12878 NLNV 12881
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13519-13598 5.27e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.89  E-value: 5.27e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13519 QDLVVDAGQPLTMVVPYDAYPKAEAEWFKEN-EPLSTK---TVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKAEGFI 13594
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESgrfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  13595 NLQV 13598
Cdd:smart00410    82 TLTV 85
THB pfam18362
Tri-helix bundle domain; This domain can be found in the myosin-binding motif (m-domain) ...
9414-9444 5.31e-07

Tri-helix bundle domain; This domain can be found in the myosin-binding motif (m-domain) region present in myosin-binding protein C (MyBP-C). MyBP-C is a sarcomeric assembly protein necessary for the regulation of sarcomere structure and function. The MyBP-C family of proteins consists mainly of modules with immunoglobulin (Ig) or fibronectin folds. This domain exhibits a three-helix bundle fold and there is a known actin-binding motif, LK(R/K)XK positioned in the third helix (alpha3), similar to that found in villin and related proteins.


Pssm-ID: 465725  Cd Length: 34  Bit Score: 51.20  E-value: 5.31e-07
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1958765569  9414 DIMELLKNVDPKEYEKYARMYGITDFRGLLQ 9444
Cdd:pfam18362     1 DVWEILSNAPPKDYEKIAFQYGITDLRGMLK 31
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32101-32170 6.54e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.51  E-value: 6.54e-07
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  32101 CKIENYDqSTQVTWYF-GVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 32170
Cdd:smart00410    16 CEASGSP-PPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2758-2839 7.90e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.50  E-value: 7.90e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2758 IKKPKDVTALENATVAFEVSVSHDTVP-VKWFHKNVEIKPSDKH-RLVSERKVHKLMLQNISPSDAGEYTAVV----GQL 2831
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPdLFWQLNGKPVRPDSAHkMLVRENGRHSLIIEPVTKRDAGIYTCIArnraGEN 83

                    ....*...
gi 1958765569  2832 ECKAKLFV 2839
Cdd:cd05744      84 SFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
2668-2752 8.72e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.26  E-value: 8.72e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2668 KIKKTLRNLTVTETQDAIFSVELT-HPDVKgVQWIKNGVVLDSNDKYEISVKGTLYSLKIKNCAMADESVYGFK----LG 2742
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPE-VSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVatnsAG 80
                            90
                    ....*....|
gi 1958765569  2743 RLGASARLHV 2752
Cdd:pfam07679    81 EAEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9671-9757 9.28e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.42  E-value: 9.28e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9671 QFTKRIQNIVVSEHQSATFECEVS-FDDAIVTWYKGPTELTESQ---KYNFRNDGRCHYMTIHNVTPDDEGVYSVIARlE 9746
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAK-N 80
                            90
                    ....*....|.
gi 1958765569  9747 PRGEARSTAEL 9757
Cdd:cd20951      81 IHGEASSSASV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13070-13148 9.48e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 9.48e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13070 PQNLEILEGEKAEFVCTIS-KESFEVQWKRDDQT-LESGDKYDIIADGKKRVLVVKDATLQDMGTYVVMV----GAARAA 13143
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSG 80

                     ....*
gi 1958765569  13144 AHLTV 13148
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
19128-19207 9.48e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 9.48e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVRKG--QVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNV 19205
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  19206 KV 19207
Cdd:smart00410    84 TV 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
33606-33688 1.03e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 51.86  E-value: 1.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33606 KALSTQMNITSGQRVTLKANIAGA-TDVKWVLNGTELSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCIGktsqGVVKC 33684
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELADPdAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA----GGEKC 76

                    ....
gi 1958765569 33685 QFDL 33688
Cdd:cd20967      77 SFEL 80
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10808-11185 1.09e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 57.86  E-value: 1.09e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10808 PPAKVPEIPKKPEEKVSVPVPKKEKAPPAKVPEVPKKPVPEEKAPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKKV 10887
Cdd:NF033839    159 PETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELD 238
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10888 EAPPAKAPEV--PPKEVTPEKKVPVVPPKKPEAPPPKVPEppkevvpekkvsmVPPKRPEAPPAKVPEASKevvPEKKVS 10965
Cdd:NF033839    239 ELKKQALSEIdnVNTKVEIENTVHKIFADMDAVVTKFKKG-------------LTQDTPKEPGNKKPSAPK---PGMQPS 302
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10966 VAPKKKPEAPAVKVPEAPKKVVPEKKVPVAAPKkPEAPAAEVPEVPKAAVPQ-KKIPEAVPpkpespppevyeepaeeiv 11044
Cdd:NF033839    303 PQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQ-PEKPKPEVKPQLETPKPEvKPQPEKPK------------------- 362
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11045 peeppeevveepepapppkvtvppkkpvpekkappavvkkpepppakapevPKEAP-PEKKVPSVVPkKPEAPPAKV--- 11120
Cdd:NF033839    363 ---------------------------------------------------PEVKPqPEKPKPEVKP-QPETPKPEVkpq 390
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 11121 PEVPK-EVVPE---KKVAVPKKPEVPPAKVPEVPKKPVVEEKPVIeEKPAIPVAEKVESPPTEVYEEPE 11185
Cdd:NF033839    391 PEKPKpEVKPQpekPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP-EKPKPEVKPQPEKPKPEVKPQPE 458
PHA03247 PHA03247
large tegument protein UL36; Provisional
10816-11190 1.13e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 1.13e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10816 PKKPEEKVSVPVPKKEK-APPAKVPEVPKKPVPEEKAPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKKVEAP-PAK 10893
Cdd:PHA03247   2589 PDAPPQSARPRAPVDDRgDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrRAR 2668
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10894 APEVPPKevtpekkvpvvppkkPEAPPPKVPEPPKEVVPEKKVSMVPPKRPEAPPAKVPEASKEVVPEKKVSVAPKKK-P 10972
Cdd:PHA03247   2669 RLGRAAQ---------------ASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAsP 2733
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10973 EAPAVKVPEAPKK--VVPEKKVPVAAPKKPEAPAAEVPEVPKAAVPQKKIPEAVPPKPESPPPEVyeepaeeivpeeppe 11050
Cdd:PHA03247   2734 ALPAAPAPPAVPAgpATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL--------------- 2798
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11051 evveepepapppkvtvppKKPVPEKKAPPAVVKKPEPPPAKAPEVPKEAPPEKKVPSVVPKKPEAPPAKVP--------- 11121
Cdd:PHA03247   2799 ------------------PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapgg 2860
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11122 EVPKEVVPEKKVAVPKKPEVPPA-KVPEVPKKPVVEEKPVIEEKPAIPVAEKVESPPTEVYEEPEEVAAQ 11190
Cdd:PHA03247   2861 DVRRRPPSRSPAAKPAAPARPPVrRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
I-set pfam07679
Immunoglobulin I-set domain;
12264-12347 1.23e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12264 KVEKPLYGVEVFVGETARFEIELS---EPDVhgQWKLKGEPLTASPDCEIIEDGKKHVLVLYNCQLDMTGEVSFQAAN-- 12338
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtpDPEV--SWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsa 79
                            90
                    ....*....|.
gi 1958765569 12339 --AKSAANLKV 12347
Cdd:pfam07679    80 geAEASAELTV 90
PRK10819 PRK10819
transport protein TonB; Provisional
11347-11462 1.27e-06

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 55.84  E-value: 1.27e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11347 ETPPVEEREIERFIQPE-EPgmEPQPE---ETPVQEPEPEKKVIEKPKLKPRPpirapsppkedvkekifqlkavsKKKV 11422
Cdd:PRK10819     59 EPPQAVQPPPEPVVEPEpEP--EPIPEppkEAPVVIPKPEPKPKPKPKPKPKP-----------------------VKKV 113
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1958765569 11423 PEKPE-VVEKVEPTPLKVPTAEKKVRKLLPEPKPQPKEEVV 11462
Cdd:PRK10819    114 EEQPKrEVKPVEPRPASPFENTAPARPTSSTATAAASKPVT 154
I-set pfam07679
Immunoglobulin I-set domain;
12000-12082 1.29e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12000 FAVPLKDVTVPEKRQARFECVLT--REANVIWSKGPDIIKASDKFDIIADGKKHILVINDSQFDDEGVYT--AEVEGKKT 12075
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTgtPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTcvATNSAGEA 82

                    ....*..
gi 1958765569 12076 SAQLFVT 12082
Cdd:pfam07679    83 EASAELT 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2317-2388 1.67e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 51.34  E-value: 1.67e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2317 AILQGLSDQKVCEGDIVQLEVKVS-LENVEGVWMKDGQEVQHSDRVHIVIDKQ-SHMLLIEDMTKEDAGNYSFT 2388
Cdd:cd05744       2 HFLQAPGDLEVQEGRLCRFDCKVSgLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCI 75
I-set pfam07679
Immunoglobulin I-set domain;
16332-16420 1.71e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.49  E-value: 1.71e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16332 LICKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKAmkDGIHDIPEDaqletaENSSVIVIPECTRAHSGKYSITAKNKAGQ 16411
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS--SDRFKVTYE------GGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569 16412 KTANCRVKV 16420
Cdd:pfam07679    82 AEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
18614-18698 1.80e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.26  E-value: 1.80e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18614 GEPENLHIADKGKTFVYLKWRRPDyDGGSPNLSYHVERRLKGSADWERVHKGSIKETHYMVDKCVENQIYEFRVQTKNEG 18693
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 18694 GESDW 18698
Cdd:pfam00041    80 GEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31212-31388 1.83e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 57.32  E-value: 1.83e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31212 YKVQLSNVFG-------TVDAILDVEiqdKPDKPTGpIVIEALLKNSVVISWKAPADDGgswITNYVVEKCEAKEGAeWQ 31284
Cdd:COG3401     300 YRVTAVDAAGnesapsnVVSVTTDLT---PPAAPSG-LTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGT-YT 371
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31285 LVSSAISVTTCRIVNLTENAGYYFRVSAQNTFGI-SEPLEVASVVIIKSPFEKPSVPGKPTITAVTKDSCVVAWKPPASD 31363
Cdd:COG3401     372 KIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNP 451
                           170       180
                    ....*....|....*....|....*
gi 1958765569 31364 GGAKIRNYYLEKREKKQNKWIAVTT 31388
Cdd:COG3401     452 GVSAAVLADGGDTGNAVPFTTTSST 476
I-set pfam07679
Immunoglobulin I-set domain;
26994-27078 1.96e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 1.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26994 PSHTVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTF 27073
Cdd:pfam07679     6 KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEAS 85

                    ....*
gi 1958765569 27074 INIIV 27078
Cdd:pfam07679    86 AELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
29169-29249 2.18e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 2.18e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29169 ITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLKETDRMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITVV 29248
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 29249 V 29249
Cdd:pfam07679    90 V 90
Titin_Z pfam09042
Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like ...
463-505 2.48e-06

Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. This interaction is essential for sarcomere assembly.


Pssm-ID: 462662  Cd Length: 43  Bit Score: 49.50  E-value: 2.48e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958765569   463 QKQMRKEAEKTAVTKVVVAADKAKEQELRLRTREEIITKQEQT 505
Cdd:pfam09042     1 QEKVREEDEKTAVSTVVVAVDKAKVLEPVSKSEEEIAAEQEQE 43
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11286-11617 2.77e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 56.32  E-value: 2.77e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11286 PVTKKPEVLPEKVPEAPKKITPEKRESAPVPEEPEAPPAPVEEIPEETIYEEKATITIGRKETPPVEEREIERFIQPEEP 11365
Cdd:NF033839    172 PTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNV 251
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11366 GMEPQPEETPVQEPEPEKKVIEKPKL-----KPRPPI-RAPSPPKEDVKekifqlkavSKKKVPEKPEVVEKVEPTPLKV 11439
Cdd:NF033839    252 NTKVEIENTVHKIFADMDAVVTKFKKgltqdTPKEPGnKKPSAPKPGMQ---------PSPQPEKKEVKPEPETPKPEVK 322
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11440 PTAEKKVrkllPEPKPQPKEEvvlKSVLRKRPEEEEPKVEPKKVEKVKKPEEPPPPPKAVEVEAPPEPKPKERKVPEPTK 11519
Cdd:NF033839    323 PQLEKPK----PEVKPQPEKP---KPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPK 395
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11520 vPEIKPAIPLPGPEPKPKPEPevktmKAPPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKPK-GPIKGVAKKTPSP-IE 11597
Cdd:NF033839    396 -PEVKPQPEKPKPEVKPQPEK-----PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvKPQPETPKPEVKPqPE 469
                           330       340
                    ....*....|....*....|
gi 1958765569 11598 AERKKLRPGSGGEKPPDEAP 11617
Cdd:NF033839    470 KPKPEVKPQPEKPKPDNSKP 489
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33245-33315 2.99e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.02  E-value: 2.99e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 33245 AKLTCAVESSAlcAKEVAWYKDGKKLKENGHFQFHYSaDGTYELKIHNLSESDCGEYVCEVSGEGGTSKTS 33315
Cdd:cd00096       1 VTLTCSASGNP--PPTITWYKNGKPLPPSSRDSRRSE-LGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
31832-31963 3.16e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 56.34  E-value: 3.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMifEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLk 31911
Cdd:NF033483     84 IVM--EYVDGRTLKDYIREHG-PLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT--KDGRVKVTDFGIARAL- 157
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31912 pgDNFRLLFTAP-----EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAET 31963
Cdd:NF033483    158 --SSTTMTQTNSvlgtvHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
17046-17124 3.18e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.58  E-value: 3.18e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17046 IVVHAGGVIRIIAYVSGKPPPTVTWNMNERALPQE---ATIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIV 17122
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAEsgrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  17123 DV 17124
Cdd:smart00410    84 TV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
25228-25310 3.54e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.20  E-value: 3.54e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25228 VIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPIT 25307
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  25308 VKV 25310
Cdd:smart00410    83 LTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
30248-30327 3.96e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.87  E-value: 3.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30248 PTIdlsTMPQKTIHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKN 30327
Cdd:pfam13927     2 PVI---TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2845-2927 4.00e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 50.27  E-value: 4.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2845 TKTMRNIEVPETKAASFECEVSHFNVPS-MWLKNGVEIEMSEKFKIVVQGK-LHQLIIMNTSTEDSAEYTFVCGNDQVSA 2922
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEvKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*
gi 1958765569  2923 TLTVT 2927
Cdd:cd20973      81 TCSAE 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12351-12427 4.29e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.50  E-value: 4.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12351 PLIFITPLSDvKVFEKDEAKFECEVSREPK-TFRWLKGTQEI--AGDDR-FELIKDGTRHSLVIKSAAFEDEAKYMFEAE 12426
Cdd:cd20951       1 PEFIIRLQSH-TVWEKSDAKLRVEVQGKPDpEVKWYKNGVPIdpSSIPGkYKIESEYGVHVLHIRRVTVEDSAVYSAVAK 79

                    .
gi 1958765569 12427 D 12427
Cdd:cd20951      80 N 80
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
21296-21376 4.44e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.20  E-value: 4.44e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21296 RTLVVRAGLSIRIFVPIKGRPAPEVTWTKDN---INLKHRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFV 21372
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgklLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  21373 NVRV 21376
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
27977-28058 4.45e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 4.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27977 PIRDLSMKDSTKTSVVLSWTKPdFDGGSIITDYLVERKGKG-EQAWSHAGISK-TCEIEIGQLKEQSVLEFRVSARNEKG 28054
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNsGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 28055 QSDP 28058
Cdd:pfam00041    81 EGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12894-12960 5.14e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 5.14e-06
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  12894 DLQVKEKETARFECEIS-KENVKVQWFKDGAE-IKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEVR 12960
Cdd:smart00410     3 SVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAT 71
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
26995-27078 5.14e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 5.14e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26995 SHTVYVRAGSNLKVDIPISGKPLPKVTLSRDG-VPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTF 27073
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  27074 INIIV 27078
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
21587-21667 5.78e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 5.78e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21587 VIARAGDNIKVEIPVLGRPKPTVTWKK-GDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITI 21665
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  21666 QV 21667
Cdd:smart00410    84 TV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2412-2490 6.43e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 6.43e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2412 KDVNVIEGTKAVLECKVSVPDVTSVKWYLNDEQ-IKPDDRVQSIVKGTKQRLVINRTHASDEGPYKLMV----GRVETSC 2486
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSGT 81

                     ....
gi 1958765569   2487 NLSV 2490
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13342-13419 7.45e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.43  E-value: 7.45e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13342 EDQTVTEFDDAVFSCQLS-REKANVKWYRNGRE-IKEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVE----DRKSRA 13415
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATnssgSASSGT 81

                     ....
gi 1958765569  13416 RLFV 13419
Cdd:smart00410    82 TLTV 85
PTZ00121 PTZ00121
MAEBL; Provisional
433-679 7.75e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 7.75e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   433 DMARVREPVISAVEQTAQRTTTTAVHVQPAQKQMRKEAEKTAVTKVVVAADKAKEQ---------ELRLRTREEIITKQE 503
Cdd:PTZ00121   1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieevmklyEEEKKMKAEEAKKAE 1616
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   504 QTHIAHEQIRKETEkafVPKVVISATKAKEQETRITGEITTKQEQKRITQETITK----ETRKTVVPKVIVATPKIKEQD 579
Cdd:PTZ00121   1617 EAKIKAEELKKAEE---EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEA 1693
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   580 VVSRSREAitTKRDQVQITQEKKRKETE----TTALSTIAVATTKAKEQETVLRSREAMTTRQEHIQVTHGKVGVGKKAE 655
Cdd:PTZ00121   1694 LKKEAEEA--KKAEELKKKEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
                           250       260
                    ....*....|....*....|....
gi 1958765569   656 AVATVVAAVDQARVREPREPRHVE 679
Cdd:PTZ00121   1772 EIRKEKEAVIEEELDEEDEKRRME 1795
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
30660-30736 8.54e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.43  E-value: 8.54e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30660 VRQGGVIRLTIPIKGKPFPICKWTKEGQDV---SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVKV 30736
Cdd:smart00410     6 VKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2234-2306 8.88e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.43  E-value: 8.88e-06
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569   2234 QDIEVPESYSGELECIIS-PENIEGKWYHNDVE-LKSNGKYSITSRRGRQNLTVKDVTKEDQGEY-CFVVDGKKTT 2306
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYtCAATNSSGSA 77
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3600-3667 9.79e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 9.79e-06
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   3600 VHGEPAPTVLWFKEDMPLYTNVCYTIIHNPDGSGTFIVNDPQRGDSGLYICKAENLWGTSTCTAELLV 3667
Cdd:smart00410    18 ASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15455-15622 1.21e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 54.62  E-value: 1.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15455 VNSTHWSRVNKALLSSLKTKVDGLLEGLTYVFRVCAENAAGPGKFSPPSDPKTARDpiSPPGPPVPRVADTSSTTIELEW 15534
Cdd:COG3401     176 ATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTT--PPSAPTGLTATADTPGSVTLSW 253
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15535 EPPAFNGggeIMGYFVDKQLVGTNEWSRCTEkmVKVRQFTVKEIREGADYKLRVSAVNAAG-EGPPgeTEPVTVAEPQEP 15613
Cdd:COG3401     254 DPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP--SNVVSVTTDLTP 326

                    ....*....
gi 1958765569 15614 PTVELDVSV 15622
Cdd:COG3401     327 PAAPSGLTA 335
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
13249-13330 1.26e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.03  E-value: 1.26e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13249 IEPLKDIETMEKKSVTFWCKVNRL-NVTLKWTKNGEEVAFDNRISYRIDKY-KHSLIIKDCGFPDEGEYIVTA----GQD 13322
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLpTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIArnraGEN 83

                    ....*...
gi 1958765569 13323 KSVAELLI 13330
Cdd:cd05744      84 SFNAELVV 91
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10144-10255 1.28e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 54.39  E-value: 1.28e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10144 PKKVEPPAVKVPEAPKKPV-PEEKKPVPIPKKEPAAP-PKVPEAPKKPAPE-----EKTAVPVAKKKEAPPPKVTEVQKK 10216
Cdd:NF033839    325 LEKPKPEVKPQPEKPKPEVkPQLETPKPEVKPQPEKPkPEVKPQPEKPKPEvkpqpETPKPEVKPQPEKPKPEVKPQPEK 404
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1958765569 10217 VVTEEKitiiPQrEESPPPAVPEIPKKKVPEEKrPVPRK 10255
Cdd:NF033839    405 PKPEVK----PQ-PEKPKPEVKPQPEKPKPEVK-PQPEK 437
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
31148-31231 1.30e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.30e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31148 EKYYGAVGSTLRLHVMYIGRPVPAMTWYH-GQKLLQNSESITIENTEHYTHLVMKNVQRKtHAGKYKVQLSNVFGTVDAI 31226
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPE-DSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  31227 LDVEI 31231
Cdd:smart00410    81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
31154-31231 1.30e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.79  E-value: 1.30e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31154 VGSTLRLHVMYIGRPVPAMTWYHGQKLLQNSESITIENTEHYTHLVMKNVQRkTHAGKYKVQLSNVFGTVDAILDVEI 31231
Cdd:pfam07679    14 EGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQP-DDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
29569-29649 1.45e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.45e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29569 VTIRAGSDLVLDAAVGGKPEPKIIWTK-GDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMV 29647
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  29648 KV 29649
Cdd:smart00410    84 TV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
11732-11802 1.66e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.66e-05
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  11732 EEVTVVKGQPLYLSCELNKERD--VVWRKDGKIVVEKPGRIVPGVIGLMRALTINDADDTDAGTYTVTVENAN 11802
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPpeVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12537-12601 1.68e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.68e-05
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  12537 QDYTGVEKDEVVLQCEISKADAP-VKWFKDG-KEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC 12601
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPeVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTC 68
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
15203-15310 1.74e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 48.35  E-value: 1.74e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15203 VKRGDEIALDATISGSPYPTITWIKDENVIVPeeikkrvappvrrkkgeaeeeepftlplTERLSINNSKQgESQLRVRD 15282
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKE----------------------------TGRVQIETTAS-STSLVIKN 54
                            90       100
                    ....*....|....*....|....*...
gi 1958765569 15283 SLRPDHGQYMIKVENDHGVAKAPCTVSV 15310
Cdd:cd05748      55 AKRSDSGKYTLTLKNSAGEKSATINVKV 82
fn3 pfam00041
Fibronectin type III domain;
28568-28649 2.13e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.18  E-value: 2.13e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28568 VGPIRFTNITGEKMTLWWEAPLNDGcAPVTHYIIEKRETSRL-AWALIEDHCEAQSYTAIKLITGNEYQFRVSAVNKFGV 28646
Cdd:pfam00041     3 PSNLTVTDVTSTSLTVSWTPPPDGN-GPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                    ...
gi 1958765569 28647 GRP 28649
Cdd:pfam00041    82 GPP 84
I-set pfam07679
Immunoglobulin I-set domain;
2318-2388 2.16e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.41  E-value: 2.16e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  2318 ILQGLSDQKVCEGDIVQLEVKVS-LENVEGVWMKDGQEVQHSDRVHIVIDKQSHMLLIEDMTKEDAGNYSFT 2388
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV 74
I-set pfam07679
Immunoglobulin I-set domain;
22380-22460 2.21e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.41  E-value: 2.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22380 KVVTIRACCTLRLFVPIKGRPAPEVKWAREhGESL---DKASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFV 22456
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLrssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASA 86

                    ....
gi 1958765569 22457 NVRV 22460
Cdd:pfam07679    87 ELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2761-2839 2.25e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.27  E-value: 2.25e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2761 PKDVTALENATVAFEVSVSHDTVPVKWFHKN--VEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVV----GQLECK 2834
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSG 80

                     ....*
gi 1958765569   2835 AKLFV 2839
Cdd:smart00410    81 TTLTV 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2414-2490 2.68e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 47.62  E-value: 2.68e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  2414 VNVIEGTKAVLECKVSVPDvTSVKWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYKLMVGRVETSCNLSV 2490
Cdd:cd20967       7 VQVSKGHKIRLTVELADPD-AEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
3113-3193 3.39e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 47.62  E-value: 3.39e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3113 KKEVQVIEKQRAVVEFEVNEDDVDAHWYKDGIEINFQVEERHQYVVERRihRMFISEARHSDAGEYTFVAGRNRSSVTLY 3192
Cdd:cd20967       4 QPAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKR--TLTVQQASLADAGEYQCVAGGEKCSFELF 81

                    .
gi 1958765569  3193 V 3193
Cdd:cd20967      82 V 82
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
26310-26391 3.63e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 3.63e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26310 VIVVKAGEVLKINADIAGRPLPVISWAKDGVE-IEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVN 26388
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  26389 CKV 26391
Cdd:smart00410    83 LTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
22389-22460 3.66e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 3.66e-05
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  22389 TLRLFVPIKGRPAPEVKWAREHGESL---DKASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFVNVRV 22460
Cdd:smart00410    11 SVTLSCEASGSPPPEVTWYKQGGKLLaesGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2138-2207 3.71e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 47.24  E-value: 3.71e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2138 QELQDVVAKEKDTMATFECETSEPFVKVKWYKDGIEVHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSCV 2207
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12005-12082 3.89e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 3.89e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12005 KDVTVPEKRQARFECVLT--REANVIWSK-GPDIIKASDKFDIIADGKKHILVINDSQFDDEGVYT--AEVEGKKTSAQL 12079
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgsPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTcaATNSSGSASSGT 81

                     ...
gi 1958765569  12080 FVT 12082
Cdd:smart00410    82 TLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2588-2664 5.97e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.73  E-value: 5.97e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2588 DQTVAESQEAVFECEV-ANPESEGEWLKDG-KHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYT----YKVATSKTSAK 2661
Cdd:smart00410     3 SVTVKEGESVTLSCEAsGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTcaatNSSGSASSGTT 82

                     ...
gi 1958765569   2662 LKV 2664
Cdd:smart00410    83 LTV 85
I-set pfam07679
Immunoglobulin I-set domain;
13425-13507 7.12e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 46.87  E-value: 7.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13425 EIIRPPQDILEAPGADVIFLAELNKDKV-EVQWLRNNMIVVQGDKHQMMSEGKIHRLQICDIKPRDQGEYRFIAKDK--- 13500
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*...
gi 1958765569 13501 -EARAKLE 13507
Cdd:pfam07679    82 aEASAELT 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33609-33689 7.41e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.73  E-value: 7.41e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33609 STQMNITSGQRVTLKANIAGATD--VKWVLNGTE-LSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCIGKTSQGVVKCQ 33685
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPpeVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....
gi 1958765569  33686 FDLT 33689
Cdd:smart00410    81 TTLT 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4227-4281 8.03e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.17  E-value: 8.03e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  4227 EVNWYFKGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNGKAMTS 4281
Cdd:cd00096      14 TITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10810-11303 8.73e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 51.69  E-value: 8.73e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10810 AKVPEIPKKPEEKVSVPVPKKEKAPPAKV-------PEVPKKPVPEEKapvpvpkkvePPPAKVPEVPKKPVPEKK---V 10879
Cdd:NF033839    123 SQLQKLMMESQSKVDEAVSKFEKDSSSSSssgsstkPETPQPENPEHQ----------KPTTPAPDTKPSPQPEGKkpsV 192
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10880 PAPTPKKVEAPPAKAPEVPPKEVTPEKKVPVVPPKKPEAPPPKVPEPPKEVVPEKKVSMVPPKRPEAPPAKVPEASKEVV 10959
Cdd:NF033839    193 PDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVV 272
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10960 PEKKVSVAP-------KKKPEAPAVKVPEAPKKVVPEKKVPVAAPKKPEAPAAEVPEVPKAAVPQKKIPEavppkpespp 11032
Cdd:NF033839    273 TKFKKGLTQdtpkepgNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPE---------- 342
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11033 pevyeepaeeivpeeppeevveepepapppkvtvppkkpvpekkappavvkkpepppakapeVPKEapPEKKVPSVVPKk 11112
Cdd:NF033839    343 --------------------------------------------------------------VKPQ--LETPKPEVKPQ- 357
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11113 PEAPPAKVPEVPKEVVPEkkvaVPKKPEVPPAKVPEVPKKPVVEEKPViEEKPAIPVAEKVESPPTEVYEEPEevaaqee 11192
Cdd:NF033839    358 PEKPKPEVKPQPEKPKPE----VKPQPETPKPEVKPQPEKPKPEVKPQ-PEKPKPEVKPQPEKPKPEVKPQPE------- 425
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11193 epapvveeeeyeappppapeIPVPQVPEEPKKVVPEkkypvikkpeppppkvpevsKKPAPMKKVPVVKKPEPPEAEvpe 11272
Cdd:NF033839    426 --------------------KPKPEVKPQPEKPKPE--------------------VKPQPEKPKPEVKPQPETPKP--- 462
                           490       500       510
                    ....*....|....*....|....*....|.
gi 1958765569 11273 vpkklapvKKEPVPVTKKPEVLPEkvPEAPK 11303
Cdd:NF033839    463 --------EVKPQPEKPKPEVKPQ--PEKPK 483
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
11732-11800 9.72e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.02  E-value: 9.72e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11732 EEVTVVKGQPLYLSCEL--NKERDVVWRKDGKIVVEKPGRIVPGVIGLMRaLTINDADDTDAGTYTVTVEN 11800
Cdd:pfam13927     9 SSVTVREGETVTLTCEAtgSPPPTITWYKNGEPISSGSTRSRSLSGSNST-LTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7676-7759 9.93e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 9.93e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7676 PDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSREL----------ESGEACTISLEDfVTELelleveplQSGDYSCLVT 7745
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaesgrfsvsRSGSTSTLTISN-VTPE--------DSGTYTCAAT 71
                             90
                     ....*....|....
gi 1958765569   7746 NDAGSASCTTHLFV 7759
Cdd:smart00410    72 NSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
29169-29249 1.01e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 1.01e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29169 ITCKAGSTFTIDVPISGRPAPKVTWKLEEMR-LKETDRMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITV 29247
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  29248 VV 29249
Cdd:smart00410    84 TV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
28081-28152 1.03e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.23  E-value: 1.03e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 28081 PGAQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLkESEYVRFSKTENkiTLSIKNVKKENGGKYTVILDN 28152
Cdd:cd20978       7 PEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDG--TLTIINVQPEDTGYYGCVATN 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13159-13241 1.45e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.96  E-value: 1.45e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13159 KDTKVKEQQEAVFNCEVN-TEGAKAKWFRND-EAIFDSSKYIILQKDLVYTLRIRDARLDDQANFSVSLTNHRGeNVKSA 13236
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SASSG 80

                     ....*
gi 1958765569  13237 ANLIV 13241
Cdd:smart00410    81 TTLTV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2931-3014 1.82e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.87  E-value: 1.82e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2931 ITSMLKDINAEEKDTITFEVTVnyEGI---SYKWLKNGVEIKSTD---RCQMRTKKLTHSLNIRNVHFGDAADYTFVA-- 3002
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEV--QGKpdpEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAkn 80
                            90
                    ....*....|....
gi 1958765569  3003 --GKATSTATLYVE 3014
Cdd:cd20951      81 ihGEASSSASVVVE 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12093-12170 2.09e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.19  E-value: 2.09e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12093 EDQTVKEGQTATFVCELS-HEKMHVVWFKNDVKLHTTR-TVLMSSEGKTYKLEIRETTLDDiS-----QIKAQVKNLSST 12165
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKLLAESgRFSVSRSGSTSTLTISNVTPED-SgtytcAATNSSGSASSG 80

                     ....*
gi 1958765569  12166 ANLKV 12170
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
11825-11889 2.75e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.19  E-value: 2.75e-04
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  11825 RDQHVKPKGTAVFTCHI-AKDTPNIKWFKGYDEiPLEPNDKTEILKEGNHLILKVKNAMPEDIDEY 11889
Cdd:smart00410     2 PSVTVKEGESVTLSCEAsGSPPPEVTWYKQGGK-LLAESGRFSVSRSGSTSTLTISNVTPEDSGTY 66
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
27392-27474 2.86e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 2.86e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27392 EVVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVC-VENSTDLASILIKDANRLNSGSYELKLRNAMGSASATI 27470
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFsVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  27471 RVQI 27474
Cdd:smart00410    82 TLTV 85
Titin_Z pfam09042
Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like ...
553-595 2.89e-04

Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. This interaction is essential for sarcomere assembly.


Pssm-ID: 462662  Cd Length: 43  Bit Score: 43.73  E-value: 2.89e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958765569   553 QETITKETRKTVVPKVIVATPKIKEQDVVSRSREAITTKRDQV 595
Cdd:pfam09042     1 QEKVREEDEKTAVSTVVVAVDKAKVLEPVSKSEEEIAAEQEQE 43
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9518-9578 3.44e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 3.44e-04
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   9518 NYPEIKLSWYK-GTEKLEPSNKYEITINGDRHTLRVRNCQLKDQGNYRlvC------GPHIASAKLTV 9578
Cdd:smart00410    20 GSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYT--CaatnssGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
21982-22063 3.54e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 3.54e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21982 TITLKAGEAFKLEADVSGRPPPTMEWAKDG-KELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFN 22060
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  22061 VKV 22063
Cdd:smart00410    83 LTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1678-1754 4.35e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 4.35e-04
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   1678 GPAHFECRLTpiGDPTMVVEWLHDG-KPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:smart00410    10 ESVTLSCEAS--GSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2229-2296 4.54e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.41  E-value: 4.54e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  2229 FVKELQDIEVPESYSGELECIIS----PENIegkWYHNDVELKSNGKYSITSRR-GRQNLTVKDVTKEDQGEY 2296
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSglptPDLF---WQLNGKPVRPDSAHKMLVREnGRHSLIIEPVTKRDAGIY 72
I-set pfam07679
Immunoglobulin I-set domain;
12620-12703 4.88e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.56  E-value: 4.88e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12620 KLVRPLYSVEVMETETARFETEISED-DIHANWKLKGEALLQTPECEIKEEGKIHVLILHNCRLDQTGGVDFQAAN---- 12694
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsage 81

                    ....*....
gi 1958765569 12695 VKSSAHLRV 12703
Cdd:pfam07679    82 AEASAELTV 90
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11366-11634 5.44e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 49.00  E-value: 5.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11366 GMEPQPEETPVQEPEPEKKVIEKPKLKPRPPIRAPSPPKEDVKEKIFQLKAVSKKKVPEKPEVVEKVEPTPLKVPTAEKK 11445
Cdd:NF033839    154 GSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVAL 233
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11446 VRKL-------LPE---PKPQPKEEVVLKSVLRKRPEEEEPKVEPKKVEKVKKPEEPPPPPKAVEVEAPPEPKPKERKVP 11515
Cdd:NF033839    234 IKELdelkkqaLSEidnVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPE 313
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11516 EPTKVPEIKPAIPLPGPEPKPKPEPEVKTMKA------PPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKP---KGPIK 11586
Cdd:NF033839    314 PETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPqletpkPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPevkPQPEK 393
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11587 GVAKKTPSPiEAERKKLRPGSGGEKP---PDEAPFTYQLKAVPLKFVKEIK 11634
Cdd:NF033839    394 PKPEVKPQP-EKPKPEVKPQPEKPKPevkPQPEKPKPEVKPQPEKPKPEVK 443
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2141-2222 5.78e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.03  E-value: 5.78e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2141 QDVVAKEKDTmATFECE-TSEPFVKVKWYKDGIE-VHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSC-VLVEDENIKTT 2217
Cdd:smart00410     2 PSVTVKEGES-VTLSCEaSGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCaATNSSGSASSG 80

                     ....*
gi 1958765569   2218 AKLIV 2222
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13253-13330 6.62e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.03  E-value: 6.62e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13253 KDIETMEKKSVTFWCKVN-RLNVTLKWTKNG-EEVAFDNRISYRIDKYKHSLIIKDCGFPDEGEYIVTA----GQDKSVA 13326
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSGT 81

                     ....
gi 1958765569  13327 ELLI 13330
Cdd:smart00410    82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
16335-16420 9.42e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 43.65  E-value: 9.42e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16335 KAGSQIRIPAVIKGRPTPKSSWEFDGKAKKAMKDGIhdipedaQLETAENSSVIVIPECTRAHSGKYSITAKNKAGQKTA 16414
Cdd:smart00410     7 KEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRF-------SVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                     ....*.
gi 1958765569  16415 NCRVKV 16420
Cdd:smart00410    80 GTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
3139-3193 1.19e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.40  E-value: 1.19e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  3139 WYKDGIEINfqVEERHQYVVERRIHRMFISEARHSDAGEYTFVA----GRNRSSVTLYV 3193
Cdd:pfam07679    34 WFKDGQPLR--SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGEAEASAELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9519-9564 1.41e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.70  E-value: 1.41e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569  9519 YPEIKLSWYKGTEKLEPSNKYEITINGDRHTLRVRNCQLKDQGNYR 9564
Cdd:cd00096      10 NPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYT 55
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2668-2753 1.53e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.18  E-value: 1.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2668 KIKKTLRNLTVTETQDAIFSVELT-HPDVKgVQWIKNGVVLDSND---KYEISVKGTLYSLKIKNCAMADESVYGFKL-- 2741
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPE-VKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAkn 80
                            90
                    ....*....|....
gi 1958765569  2742 --GRLGASARLHVE 2753
Cdd:cd20951      81 ihGEASSSASVVVE 94
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2514-2577 1.59e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.61  E-value: 1.59e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2514 VELSHSGIDVVWNFKGQEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGEYAFYAGENTTSGKLTV 2577
Cdd:cd20967      19 VELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11345-11617 1.63e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.46  E-value: 1.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11345 RKETPPVEEREIERFIQPE---EPGMEPQPEETPVQEPEPEKkviEKPKL-------KPRPPIRAPSPPKEDVKE---KI 11411
Cdd:NF033839    158 KPETPQPENPEHQKPTTPApdtKPSPQPEGKKPSVPDINQEK---EKAKLavatymsKILDDIQKHHLQKEKHRQivaLI 234
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11412 FQLKAVSKKKVPEKPEVVEKVEP--TPLKVPTAEKKVRKLLPEPKPQ--PKEEVvlksvlRKRPEEEEPKVEPKKVEKVK 11487
Cdd:NF033839    235 KELDELKKQALSEIDNVNTKVEIenTVHKIFADMDAVVTKFKKGLTQdtPKEPG------NKKPSAPKPGMQPSPQPEKK 308
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11488 KPEEPPPPPKAVEVEAPPEPKPKERKVPEPTKvPEIKPAIPLPGPEPKPKPEPEVKTMKAPPIEPAPTPIAAPVTapvvg 11567
Cdd:NF033839    309 EVKPEPETPKPEVKPQLEKPKPEVKPQPEKPK-PEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET----- 382
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11568 KKAEAKPKDEAAKPKGPIKGVAKKTPSPIEAERKKLRPGSGGEKP-PDEAP 11617
Cdd:NF033839    383 PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPkPEVKP 433
I-set pfam07679
Immunoglobulin I-set domain;
15200-15310 1.69e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 1.69e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15200 SLEVKRGDEIALDATISGSPYPTITWIKDENVIVPeeikkrvappvrrkkgeaeeeepftlplTERLSINNsKQGESQLR 15279
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS----------------------------SDRFKVTY-EGGTYTLT 59
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1958765569 15280 VRDSLRPDHGQYMIKVENDHGVAKAPCTVSV 15310
Cdd:pfam07679    60 ISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2329-2403 1.83e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.88  E-value: 1.83e-03
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   2329 EGDIVQLEVKVS-LENVEGVWMKDGQE-VQHSDRVHIVIDKQSHMLLIEDMTKEDAGNYSFTIPALGLSTSGNVSVY 2403
Cdd:smart00410     8 EGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10811-11003 2.29e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.07  E-value: 2.29e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10811 KVPEIPKKPEEKVSVPVPKKEKAPPAKVPEvPKKPVPEEKAPvpvpkkvepppakvPEVPK---KPVPEKkvpaPTPKKV 10887
Cdd:NF033839    372 PKPEVKPQPETPKPEVKPQPEKPKPEVKPQ-PEKPKPEVKPQ--------------PEKPKpevKPQPEK----PKPEVK 432
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10888 EAPPAKAPEVPPKEVTpekkvpvvppkkpeapppkvpeppkevvpekkvsmvppKRPEAPPAkvPEAskevvPEKKVsva 10967
Cdd:NF033839    433 PQPEKPKPEVKPQPEK--------------------------------------PKPEVKPQ--PET-----PKPEV--- 464
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 1958765569 10968 pKKKPEAPAVKVPEAPKKVVPEKKVPVAAPKKPEAP 11003
Cdd:NF033839    465 -KPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTP 499
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12086-12170 2.30e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 42.79  E-value: 2.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12086 LKFISPLEDQTVKEGQTATFVCELSHE-KMHVVWFKNDVKL---HTTRTVLMSSEGKTYKLEIRETTLDDISQIKAQVKN 12161
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 12162 ----LSSTANLKV 12170
Cdd:cd20951      81 ihgeASSSASVVV 93
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
12003-12067 2.60e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 42.18  E-value: 2.60e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 12003 PLKDVTVPEKRQARFECVLTREAN--VIWSKGPDIIKASDKFDIIADGKKHI-LVINDSQFDDEGVYT 12067
Cdd:cd20973       3 TLRDKEVVEGSAARFDCKVEGYPDpeVKWMKDDNPIVESRRFQIDQDEDGLCsLIISDVCGDDSGKYT 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2674-2737 2.66e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 2.66e-03
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569   2674 RNLTVTETQDAIFSVELTHPDVKGVQWIKNG-VVLDSNDKYEISVKGTLYSLKIKNCAMADESVY 2737
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTY 66
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
15200-15310 2.74e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 2.74e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15200 SLEVKRGDEIALDATISGSPYPTITWIKDENVIVPEeikkrvappvrrkkgeaeeeepftlplTERLSINNSKqGESQLR 15279
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAE---------------------------SGRFSVSRSG-STSTLT 54
                             90       100       110
                     ....*....|....*....|....*....|.
gi 1958765569  15280 VRDSLRPDHGQYMIKVENDHGVAKAPCTVSV 15310
Cdd:smart00410    55 ISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
20057-20203 5.23e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 46.09  E-value: 5.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20057 RTLKATGLQEGTEYEFRVTAINKAgPGKpsDASKAVYAQDPLYPPGPPA-------FPKVYDTT-RSSVSLSWGKPAFDg 20128
Cdd:COG4733     489 QLFRVVSIEENEDGTYTITAVQHA-PEK--YAAIDAGAFDDVPPQWPPVnvttsesLSVVAQGTaVTTLTVSWDAPAGA- 564
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 20129 gspiIGYLVEVkRADSDHWVrcNLPEKLQkTRFEVTGLMENTeYQFRVYAVNKIGY-SDPSDVPDKHCPKDILIPP 20203
Cdd:COG4733     565 ----VAYEVEW-RRDDGNWV--SVPRTSG-TSFEVPGIYAGD-YEVRVRAINALGVsSAWAASSETTVTGKTAPPP 631
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12274-12348 6.86e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 41.25  E-value: 6.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12274 VFVGETARFEIELS-EPDVHGQWKLKGEPLTAS---PDCEIIEDGKKHVLVLYNCQLDMTGEVSFQAAN----AKSAANL 12345
Cdd:cd20951      12 VWEKSDAKLRVEVQgKPDPEVKWYKNGVPIDPSsipGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNihgeASSSASV 91

                    ...
gi 1958765569 12346 KVK 12348
Cdd:cd20951      92 VVE 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3114-3193 7.80e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.95  E-value: 7.80e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3114 KEVQVIEKQRAVVEFEVNED-DVDAHWYKDGIEINFQvEERHQYVVERRIHRMFISEARHSDAGEYTFVA----GRNRSS 3188
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSpPPEVTWYKQGGKLLAE-SGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSG 80

                     ....*
gi 1958765569   3189 VTLYV 3193
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
20213-20295 9.67e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.57  E-value: 9.67e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20213 KTLILRAGVTMRLYVPVKGRPPPKITWSKPN---VNLRERIglDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEY 20289
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgklLAESGRF--SVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                     ....*.
gi 1958765569  20290 TIVVKV 20295
Cdd:smart00410    80 GTTLTV 85
 
Name Accession Description Interval E-value
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
31762-32038 1.41e-175

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 543.30  E-value: 1.41e-175
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14104       1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14104      81 VDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLKPGDKFRLQYT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKE 32001
Cdd:cd14104     161 SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKE 240
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1958765569 32002 RKSRMTASEALKHPWLKQRMDRVSTKVIRTLRHRRYY 32038
Cdd:cd14104     241 RKSRMTAQEALNHPWLKQGMETVSSKDIKTTRHRRYY 277
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
31769-32016 1.04e-120

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 384.70  E-value: 1.04e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERI 31848
Cdd:cd14006       1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31849 NTSaFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFTAPEYYAP 31928
Cdd:cd14006      81 AER-GSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARKLNPGEELKEIFGTPEFVAP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31929 EVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTA 32008
Cdd:cd14006     160 EIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEPRKRPTA 239

                    ....*...
gi 1958765569 32009 SEALKHPW 32016
Cdd:cd14006     240 QEALQHPW 247
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
31769-32017 2.06e-100

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 326.49  E-value: 2.06e-100
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKG-TDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFER 31847
Cdd:cd14103       1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKaKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFER 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31848 INTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFTAPEYYA 31927
Cdd:cd14103      81 VVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLARKYDPDKKLKVLFGTPEFVA 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31928 PEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMT 32007
Cdd:cd14103     161 PEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPRKRMS 240
                           250
                    ....*....|
gi 1958765569 32008 ASEALKHPWL 32017
Cdd:cd14103     241 AAQCLQHPWL 250
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
31760-32017 3.61e-83

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 277.54  E-value: 3.61e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK-GTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14114       1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPhESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEF 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd14114      81 LSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHLDPKESVKV 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLL 31998
Cdd:cd14114     161 TTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLL 240
                           250
                    ....*....|....*....
gi 1958765569 31999 VKERKSRMTASEALKHPWL 32017
Cdd:cd14114     241 LADPNKRMTIHQALEHPWL 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
31767-32017 1.33e-78

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 264.47  E-value: 1.33e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG-TDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd14193      10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSqKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFTAPEY 31925
Cdd:cd14193      90 DRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGLARRYKPREKLRVNFGTPEF 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31926 YAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSR 32005
Cdd:cd14193     170 LAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISKLLIKEKSWR 249
                           250
                    ....*....|..
gi 1958765569 32006 MTASEALKHPWL 32017
Cdd:cd14193     250 MSASEALKHPWL 261
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
31767-32017 2.27e-78

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 263.75  E-value: 2.27e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT-DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd14192      10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAkEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELF 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFTAPEY 31925
Cdd:cd14192      90 DRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGLARRYKPREKLKVNFGTPEF 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31926 YAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSR 32005
Cdd:cd14192     170 LAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSCR 249
                           250
                    ....*....|..
gi 1958765569 32006 MTASEALKHPWL 32017
Cdd:cd14192     250 MSATQCLKHEWL 261
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
31762-32016 2.37e-77

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 260.87  E-value: 2.37e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd05117       1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkkKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR-KNSIIKIIEFGQARQLKPGDNFR 31917
Cdd:cd05117      81 CTGGELFDRI-VKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdPDSPIKIIDFGLAKIFEEGEKLK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRL 31997
Cdd:cd05117     160 TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRL 239
                           250
                    ....*....|....*....
gi 1958765569 31998 LVKERKSRMTASEALKHPW 32016
Cdd:cd05117     240 LVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
31763-32017 7.41e-76

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 256.30  E-value: 7.41e-76
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:smart00220     1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRerILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                             90       100       110       120       130       140       150       160
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31841 GLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLLF 31920
Cdd:smart00220    81 GGDLFDLLKKRGR-LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD--EDGHVKLADFGLARQLDPGEKLTTFV 157
                            170       180       190       200       210       220       230       240
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31921 TAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETN-QQMIENIMNAEYTFDEEaFQEISLEAMDFIDRLLV 31999
Cdd:smart00220   158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPP-EWDISPEAKDLIRKLLV 236
                            250
                     ....*....|....*...
gi 1958765569  32000 KERKSRMTASEALKHPWL 32017
Cdd:smart00220   237 KDPEKRLTAEEALQHPFF 254
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
31767-32017 2.53e-74

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 252.15  E-value: 2.53e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT-DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd14190      10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSkDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELF 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFTAPEY 31925
Cdd:cd14190      90 ERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGLARRYNPREKLKVNFGTPEF 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31926 YAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSR 32005
Cdd:cd14190     170 LSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSAR 249
                           250
                    ....*....|..
gi 1958765569 32006 MTASEALKHPWL 32017
Cdd:cd14190     250 MSATQCLKHPWL 261
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
31763-32017 1.19e-72

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 247.22  E-value: 1.19e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV-KGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14191       4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14191      84 GELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRLENAGSLKVLFG 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKE 32001
Cdd:cd14191     164 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKD 243
                           250
                    ....*....|....*.
gi 1958765569 32002 RKSRMTASEALKHPWL 32017
Cdd:cd14191     244 MKARLTCTQCLQHPWL 259
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
31763-32017 2.37e-71

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 243.93  E-value: 2.37e-71
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK-------GTDQVLVKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd14105       7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRrskasrrGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLI 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRK--NSIIKIIEFGQARQLKPG 31913
Cdd:cd14105      87 LELVAGGELFDFLAEKE-SLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpIPRIKLIDFGLAHKIEDG 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd14105     166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSELAKDF 245
                           250       260
                    ....*....|....*....|....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14105     246 IRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
31761-32017 9.87e-68

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 233.76  E-value: 9.87e-68
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK-------GTDQVLVKKEISILNIARHRNILYLHESFESMEELV 31833
Cdd:cd14194       5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRrtkssrrGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVI 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRK--NSIIKIIEFGQARQLK 31911
Cdd:cd14194      85 LILELVAGGELFDFLAEKE-SLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpKPRIKIIDFGLAHKID 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAM 31991
Cdd:cd14194     164 FGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAK 243
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14194     244 DFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
31763-32017 1.30e-67

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 233.31  E-value: 1.30e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK-------GTDQVLVKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd14196       7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrGVSREEIEREVSILRQVLHPNIITLHDVYENRTDVVLI 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSI--IKIIEFGQARQLKPG 31913
Cdd:cd14196      87 LELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIphIKLIDFGLAHEIEDG 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd14196     166 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSELAKDF 245
                           250       260
                    ....*....|....*....|....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14196     246 IRKLLVKETRKRLTIQEALRHPWI 269
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
31755-32017 1.88e-67

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 232.63  E-value: 1.88e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31755 KTKELYEKYMI-AEDLGRGEFGIVHRCVETSSKKTFMAKFVKV--KGTDQVL-VKKEISILNIAR-HRNILYLHESFESM 31829
Cdd:cd14106       1 STENINEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKrrRGQDCRNeILHEIAVLELCKdCPRVVNLHEVYETR 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGLDIFeRINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY-QTRKNSIIKIIEFGQAR 31908
Cdd:cd14106      81 SELILILELAAGGELQ-TLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtSEFPLGDIKLCDFGISR 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31909 QLKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISL 31988
Cdd:cd14106     160 VIGEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSP 239
                           250       260
                    ....*....|....*....|....*....
gi 1958765569 31989 EAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14106     240 LAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
31763-32018 1.62e-65

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 227.58  E-value: 1.62e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK-------GTDQVLVKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd14195       7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRrlsssrrGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIEFGQARQLKPG 31913
Cdd:cd14195      87 LELVSGGELFDFLAEKE-SLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldKNVPNPRIKLIDFGIAHKIEAG 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd14195     166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDF 245
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd14195     246 IRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
31755-32017 1.79e-60

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 212.87  E-value: 1.79e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31755 KTKELYEKYMIA--EDLGRGEFGIVHRCVETSSKKTFMAKFVKV--KGTD-QVLVKKEISILNIAR-HRNILYLHESFES 31828
Cdd:cd14197       1 RSEPFQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKrrKGQDcRMEIIHEIAVLELAQaNPWVINLHEVYET 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31829 MEELVMIFEFISGLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSI--IKIIEFG 31905
Cdd:cd14197      81 ASEMILVLEYAAGGEIFNQCVADREEaFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILL-TSESPLgdIKIVDFG 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31906 QARQLKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQE 31985
Cdd:cd14197     160 LSRILKNSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEH 239
                           250       260       270
                    ....*....|....*....|....*....|..
gi 1958765569 31986 ISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14197     240 LSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
31760-32017 1.01e-56

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 202.20  E-value: 1.01e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL---------VKKEISILN-IARHRNILYLHESFESM 31829
Cdd:cd14093       2 YAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSEneaeelreaTRREIEILRqVSGHPNIIELHDVFESP 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ 31909
Cdd:cd14093      82 TFIFLVFELCRKGELFDYL-TEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN--VKISDFGFATR 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LKPGDNFRLLFTAPEYYAPEVHQ------HDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAF 31983
Cdd:cd14093     159 LDEGEKLRELCGTPGYLAPEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPEW 238
                           250       260       270
                    ....*....|....*....|....*....|....
gi 1958765569 31984 QEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14093     239 DDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
31763-32017 2.10e-56

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 201.30  E-value: 2.10e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMI-AEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK--GTD-QVLVKKEISILNIARHR-NILYLHESFESMEELVMIFE 31837
Cdd:cd14198       9 YILtSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRrrGQDcRAEILHEIAVLELAKSNpRVVNLHEVYETTSEIILILE 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFER-INTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqtrkNSI-----IKIIEFGQARQLK 31911
Cdd:cd14198      89 YAAGGEIFNLcVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILL----SSIyplgdIKIVDFGMSRKIG 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAM 31991
Cdd:cd14198     165 HACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQLAT 244
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14198     245 DFIQKLLVKNPEKRPTAEICLSHSWL 270
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
32081-32170 6.69e-56

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 192.56  E-value: 6.69e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32081 PVSGQIMHAIGEEGGYVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYG 32160
Cdd:cd20927       1 PVSGQIMHAVGEEGGHVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYG 80
                            90
                    ....*....|
gi 1958765569 32161 EDSSYAELFV 32170
Cdd:cd20927      81 EDSSYAELFV 90
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
31763-32017 4.42e-54

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 193.97  E-value: 4.42e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGl 31842
Cdd:cd14108       4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE- 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFTA 31922
Cdd:cd14108      83 ELLERI-TKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAQELTPNEPQYCKYGT 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKER 32002
Cdd:cd14108     162 PEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVLVSDR 241
                           250
                    ....*....|....*
gi 1958765569 32003 kSRMTASEALKHPWL 32017
Cdd:cd14108     242 -LRPDAEETLEHPWF 255
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
33070-33161 2.33e-53

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 185.25  E-value: 2.33e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33070 TLAARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVEN 33149
Cdd:cd05747       1 TLPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVEN 80
                            90
                    ....*....|..
gi 1958765569 33150 TDGKQEAQFTLT 33161
Cdd:cd05747      81 SEGKQEAQFTLT 92
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
31761-32017 3.22e-53

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 191.57  E-value: 3.22e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAE-DLGRGEFGIVHRCVETSSKKTFMAKfvkVKGTDQVLVKkEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14109       3 ELYEIGEeDEKRAAQGAPFHVTERSTGRNFLAQ---LRYGDPFLMR-EVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 S--GLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrkNSIIKIIEFGQARQLKPGDNFR 31917
Cdd:cd14109      79 AstIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ---DDKLKLADFGQSRRLLRGKLTT 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRL 31997
Cdd:cd14109     156 LIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKKL 235
                           250       260
                    ....*....|....*....|
gi 1958765569 31998 LVKERKSRMTASEALKHPWL 32017
Cdd:cd14109     236 LVYIPESRLTVDEALNHPWF 255
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31763-32028 1.66e-50

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 185.03  E-value: 1.66e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKvKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd14085       5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLK-KTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQT-RKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14085      84 ELFDRIVEKGY-YSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpAPDAPLKIADFGLSKIVDQQVTMKTVCG 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE-TNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVK 32000
Cdd:cd14085     163 TPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDErGDQYMFKRILNCDYDFVSPWWDDVSLNAKDLVKKLIVL 242
                           250       260       270
                    ....*....|....*....|....*....|....
gi 1958765569 32001 ERKSRMTASEALKHPWLKQR------MDRVSTKV 32028
Cdd:cd14085     243 DPKKRLTTQQALQHPWVTGKaanfahMDTAQKKL 276
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
31762-32016 1.82e-50

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 183.83  E-value: 1.82e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd14098       1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIvkrKVAGNDKNLqlFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERI--NTSAFELNEREVVsyvRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd14098      81 EYVEGGDLMDFImaWGAIPEQHARELT---KQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKVIHTGT 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPEYYAPEV-HQHDV-----VSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISL 31988
Cdd:cd14098     158 FLVTFCGTMAYLAPEIlMSKEQnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISE 237
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31989 EAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14098     238 EAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
31769-32016 3.53e-50

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 182.47  E-value: 3.53e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERI 31848
Cdd:cd14115       1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31849 nTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNS-IIKIIEFGQARQLKPGDNFRLLFTAPEYYA 31927
Cdd:cd14115      81 -MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQISGHRHVHHLLGNPEFAA 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31928 PEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMT 32007
Cdd:cd14115     160 PEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRPT 239

                    ....*....
gi 1958765569 32008 ASEALKHPW 32016
Cdd:cd14115     240 AATCLQHPW 248
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
31762-32017 5.03e-50

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 182.35  E-value: 5.03e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14087       2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATG 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY-QTRKNSIIKIIEFGQARQLKPGDNFRLLF 31920
Cdd:cd14087      82 GELFDRIIAKG-SFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyHPGPDSKIMITDFGLASTRKKGPNCLMKT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 T--APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLL 31998
Cdd:cd14087     161 TcgTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLL 240
                           250
                    ....*....|....*....
gi 1958765569 31999 VKERKSRMTASEALKHPWL 32017
Cdd:cd14087     241 TVNPGERLSATQALKHPWI 259
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31761-32036 6.61e-50

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 183.39  E-value: 6.61e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14086       1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIIntkKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR-KNSIIKIIEFGQARQLKPGDNF 31916
Cdd:cd14086      81 LVTGGELFEDIVAREF-YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKsKGAAVKLADFGLAIEVQGDQQA 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFTA-PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFID 31995
Cdd:cd14086     160 WFGFAGtPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLIN 239
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 1958765569 31996 RLLVKERKSRMTASEALKHPWLKQRmDRVSTKVirtlrHRR 32036
Cdd:cd14086     240 QMLTVNPAKRITAAEALKHPWICQR-DRVASMV-----HRQ 274
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
31762-32016 1.33e-49

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 180.98  E-value: 1.33e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQvLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14095       1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIdkaKCKGKEH-MIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSII--KIIEFGQARQLKpgdnf 31916
Cdd:cd14095      80 VKGGDLFDAI-TSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKslKLADFGLATEVK----- 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFT---APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ--MIENIMNAEYTFDEEAFQEISLEAM 31991
Cdd:cd14095     154 EPLFTvcgTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQeeLFDLILAGEFEFLSPYWDNISDSAK 233
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14095     234 DLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
31765-32018 1.94e-48

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 177.67  E-value: 1.94e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHRCVETSSKKT------FMAKFVKVKGTDQVlvKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14007       4 IGKPLGKGKFGNVYLAREKKSGFIvalkviSKSQLQKSGLEHQL--RREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKpgDNFRL 31918
Cdd:cd14007      82 APNGELYKELKKQK-RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE--LKLADFGWSVHAP--SNRRK 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LF--TaPEYYAPEV---HQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDF 31993
Cdd:cd14007     157 TFcgT-LDYLPPEMvegKEYD---YKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPS----SVSPEAKDL 228
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd14007     229 ISKLLQKDPSKRLSLEQVLNHPWIK 253
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6-98 1.99e-48

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 171.00  E-value: 1.99e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNG 85
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569    86 SGQATSTAELLVT 98
Cdd:cd20974      81 SGQATSTAELLVL 93
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31761-32016 7.29e-48

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 176.02  E-value: 7.29e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK---VKGTDQVLvKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14083       3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDkkaLKGKEDSL-ENEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQT-RKNSIIKIIEFGQARQLKPGDnf 31916
Cdd:cd14083      82 LVTGGELFDRIVEKGS-YTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSpDEDSKIMISDFGLSKMEDSGV-- 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 rlLFTA---PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd14083     159 --MSTAcgtPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDF 236
                           250       260
                    ....*....|....*....|...
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14083     237 IRHLMEKDPNKRYTCEQALEHPW 259
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
31769-32017 2.47e-47

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 175.05  E-value: 2.47e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSS---------------KKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFES--MEE 31831
Cdd:cd14008       1 LGRGSFGKVKLALDTETgqlyaikifnksrlrKRREGKNDRGKIKNALDDVRREIAIMKKLDHPNIVRLYEVIDDpeSDK 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISGLDIFER-INTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQL 31910
Cdd:cd14008      81 LYLVLEYCEGGPVMELdSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLT--ADGTVKISDFGVSEMF 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNfRLLFTA--PEYYAPEVHQHDVVS---SATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfqE 31985
Cdd:cd14008     159 EDGND-TLQKTAgtPAFLAPELCDGDSKTysgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPP--E 235
                           250       260       270
                    ....*....|....*....|....*....|..
gi 1958765569 31986 ISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14008     236 LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
31763-32017 3.46e-47

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 174.31  E-value: 3.46e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd14107       4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCSSE 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENI--IYQTRKNsiIKIIEFGQARQLKPGDNFRLLF 31920
Cdd:cd14107      84 ELLDRLFLKGV-VTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNIlmVSPTRED--IKICDFGFAQEITPSEHQFSKY 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 TAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVK 32000
Cdd:cd14107     161 GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQP 240
                           250
                    ....*....|....*..
gi 1958765569 32001 ERKSRMTASEALKHPWL 32017
Cdd:cd14107     241 DPEKRPSASECLSHEWF 257
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
31757-32017 5.11e-47

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 174.12  E-value: 5.11e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK---------VKGTDQVLVKKEISILNIARHRNILYLHESFE 31827
Cdd:cd14084       2 KELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINkrkftigsrREINKPRNIETEIEILKKLSHPCIIKIEDFFD 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31828 SMEELVMIFEFISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKN-SIIKIIEFGQ 31906
Cdd:cd14084      82 AEDDYYIVLELMEGGELFDRV-VSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeCLIKITDFGL 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARQLKPGDNFRLLFTAPEYYAPEVHQHDVV---SSATDMWSLGTLVYVLLSGINPFLAE-TNQQMIENIMNAEYTFDEEA 31982
Cdd:cd14084     161 SKILGETSLMKTLCGTPTYLAPEVLRSFGTegyTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQILSGKYTFIPKA 240
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 31983 FQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14084     241 WKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
31762-32016 5.47e-47

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 173.47  E-value: 5.47e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14003       1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIdksKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINtSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd14003      81 ASGGELFDYIV-NNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN--LKIIDFGLSNEFRGGSLLKT 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRL 31997
Cdd:cd14003     158 FCGTPAYAAPEVlLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPS----HLSPDARDLIRRM 233
                           250
                    ....*....|....*....
gi 1958765569 31998 LVKERKSRMTASEALKHPW 32016
Cdd:cd14003     234 LVVDPSKRITIEEILNHPW 252
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
31763-32017 1.11e-46

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 172.85  E-value: 1.11e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd14113       9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQG 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY-QTRKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14113      89 RLLDYV-VRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVdQSLSKPTIKLADFGDAVQLNTTYYIHQLLG 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKE 32001
Cdd:cd14113     168 SPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFVCFLLQMD 247
                           250
                    ....*....|....*.
gi 1958765569 32002 RKSRMTASEALKHPWL 32017
Cdd:cd14113     248 PAKRPSAALCLQEQWL 263
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31761-32017 1.27e-46

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 172.90  E-value: 1.27e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTD--QVLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14167       3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEgkETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQL 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQT-RKNSIIKIIEFGQARQLKPGDNFR 31917
Cdd:cd14167      83 VSGGELFDRIVEKGF-YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSlDEDSKIMISDFGLSKIEGSGSVMS 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRL 31997
Cdd:cd14167     162 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIQHL 241
                           250       260
                    ....*....|....*....|
gi 1958765569 31998 LVKERKSRMTASEALKHPWL 32017
Cdd:cd14167     242 MEKDPEKRFTCEQALQHPWI 261
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31761-32046 1.55e-46

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 173.25  E-value: 1.55e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK-VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14166       3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKkSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLV 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQT-RKNSIIKIIEFGQARQLKPGdnfrL 31918
Cdd:cd14166      83 SGGELFDRILERGV-YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTpDENSKIMITDFGLSKMEQNG----I 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTA---PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFID 31995
Cdd:cd14166     158 MSTAcgtPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIR 237
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31996 RLLVKERKSRMTASEALKHPWLKQrmdrvstkviRTLRHRRYYHTL---IKKDL 32046
Cdd:cd14166     238 HLLEKNPSKRYTCEKALSHPWIIG----------NTALHRDIYPSVseqIQKNF 281
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
103-193 3.04e-45

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 161.98  E-value: 3.04e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   103 PPNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSV 182
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569   183 GRATSTADLLV 193
Cdd:cd20972      81 GSDTTSAEIFV 91
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
31759-32019 5.54e-45

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 168.55  E-value: 5.54e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK----------KEISILN-IARHRNILYLHESFE 31827
Cdd:cd14182       1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEevqelreatlKEIDILRkVSGHPNIIQLKDTYE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31828 SMEELVMIFEFISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQA 31907
Cdd:cd14182      81 TNTFFFLVFDLMKKGELFDYL-TEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN--IKLTDFGFS 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLKPGDNFRLLFTAPEYYAPEVHQ------HDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEE 31981
Cdd:cd14182     158 CQLDPGEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSP 237
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1958765569 31982 AFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd14182     238 EWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
31761-32027 6.25e-45

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 169.26  E-value: 6.25e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTF------MAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd14094       3 DVYELCEVIGKGPFSVVRRCIHRETGQQFavkivdVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDI-FERIN--TSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSI-IKIIEFGQARQL 31910
Cdd:cd14094      83 VFEFMDGADLcFEIVKraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQL 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDnfrlLFTA-----PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAeTNQQMIENIMNAEYTFDEEAFQE 31985
Cdd:cd14094     163 GESG----LVAGgrvgtPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSH 237
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 31986 ISLEAMDFIDRLLVKERKSRMTASEALKHPWLKQRMDRVSTK 32027
Cdd:cd14094     238 ISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRI 279
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
31769-32016 4.16e-44

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 165.00  E-value: 4.16e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTF-MAKFVK--VKGTDQVL-VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05123       1 LGKGSFGKVLLVRKKDTGKLYaMKVLRKkeIIKRKEVEhTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINtSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFTA-P 31923
Cdd:cd05123      81 FSHLS-KEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH--IKLTDFGLAKELSSDGDRTYTFCGtP 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31924 EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRLLVKERK 32003
Cdd:cd05123     158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPE----YVSPEAKSLISGLLQKDPT 233
                           250
                    ....*....|....*.
gi 1958765569 32004 SRMTA--SEALK-HPW 32016
Cdd:cd05123     234 KRLGSggAEEIKaHPF 249
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
31758-32016 4.90e-44

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 166.05  E-value: 4.90e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYekYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTDQVLVKKEISILNIAR-HRNILYLHESFESMEELVMI 31835
Cdd:cd14090       1 DLY--KLTGELLGEGAYASVQTCINLYTGKEYAVKIIeKHPGHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLV 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQT-RKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd14090      79 FEKMRGGPLLSHIEKRVH-FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESmDKVSPVKICDFDLGSGIKLSS 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAP---------EYYAPEVHQHDVVSSAT-----DMWSLGTLVYVLLSGINPFLAE--------------TNQQ 31966
Cdd:cd14090     158 TSMTPVTTPelltpvgsaEYMAPEVVDAFVGEALSydkrcDLWSLGVILYIMLCGYPPFYGRcgedcgwdrgeacqDCQE 237
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31967 MI-ENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14090     238 LLfHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
31767-32026 1.57e-43

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 165.55  E-value: 1.57e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVkvkgTDQVLVKKEISILNIAR-HRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd14092      12 EALGDGSFSVCRKCVHKKTGQEFAVKIV----SRRLDTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGGELL 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERI-NTSAFelNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY-QTRKNSIIKIIEFGQARqLKPgDNFRL---LF 31920
Cdd:cd14092      88 ERIrKKKRF--TESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtDEDDDAEIKIVDFGFAR-LKP-ENQPLktpCF 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 TAPeYYAPEVHQHDVVSS----ATDMWSLGTLVYVLLSGINPFLAETNQ----QMIENIMNAEYTFDEEAFQEISLEAMD 31992
Cdd:cd14092     164 TLP-YAAPEVLKQALSTQgydeSCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFSFDGEEWKNVSSEAKS 242
                           250       260       270
                    ....*....|....*....|....*....|....
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWLKQRMDRVST 32026
Cdd:cd14092     243 LIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSST 276
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
31757-32017 6.69e-43

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 162.45  E-value: 6.69e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV---KGTDQVL------VKKEISILN-IARHRNILYLHESF 31826
Cdd:cd14181       6 KEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVtaeRLSPEQLeevrssTLKEIHILRqVSGHPSIITLIDSY 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31827 ESMEELVMIFEFISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQ 31906
Cdd:cd14181      86 ESSTFIFLVFDLMRRGELFDYL-TEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLD--DQLHIKLSDFGF 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARQLKPGDNFRLLFTAPEYYAPEV------HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDE 31980
Cdd:cd14181     163 SCHLEPGEKLRELCGTPGYLAPEIlkcsmdETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSS 242
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1958765569 31981 EAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14181     243 PEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
31769-32015 9.05e-43

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 159.74  E-value: 9.05e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFE 31846
Cdd:cd00180       1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLeeLLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31847 RINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqtRKNSIIKIIEFGQARQLKPGDNFRLLF---TAP 31923
Cdd:cd00180      81 LLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL--DSDGTVKLADFGLAKDLDSDDSLLKTTggtTPP 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31924 EYYAPEVHQHDVVSSATDMWSLGTLVYvllsginpflaetnqqmienimnaeytfdeeafqEISlEAMDFIDRLLVKERK 32003
Cdd:cd00180     159 YYAPPELLGGRYYGPKVDIWSLGVILY----------------------------------ELE-ELKDLIRRMLQYDPK 203
                           250
                    ....*....|..
gi 1958765569 32004 SRMTASEALKHP 32015
Cdd:cd00180     204 KRPSAKELLEHL 215
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
31763-32016 7.27e-42

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 159.69  E-value: 7.27e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAK------FVKVKGTDQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd05581       3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldkrhIIKEKKVKYVTIEKEV--LSRLAHPGIVKLYYTFQDESKLYFVL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNF 31916
Cdd:cd05581      81 EYAPNGDLLEYIRKYGS-LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLD--EDMHIKITDFGTAKVLGPDSSP 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFTA------------------PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTF 31978
Cdd:cd05581     158 ESTKGDadsqiaynqaraasfvgtAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEF 237
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 31979 DEEAFQeislEAMDFIDRLLVKERKSRMTASE-----ALK-HPW 32016
Cdd:cd05581     238 PENFPP----DAKDLIQKLLVLDPSKRLGVNEnggydELKaHPF 277
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
18713-18806 8.54e-42

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 152.12  E-value: 8.54e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18713 PVLDLKLSGVLtVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATN 18792
Cdd:cd20974       1 PVFTQPLQSVV-VLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569 18793 PAGSFVAYATVNVL 18806
Cdd:cd20974      80 GSGQATSTAELLVL 93
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31763-32017 1.30e-41

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 158.90  E-value: 1.30e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT--DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd14169       5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALrgKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR-KNSIIKIIEFGQARQLKPGdnfrLL 31919
Cdd:cd14169      85 GGELFDRIIERGS-YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPfEDSKIMISDFGLSKIEAQG----ML 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTA---PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDR 31996
Cdd:cd14169     160 STAcgtPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRH 239
                           250       260
                    ....*....|....*....|.
gi 1958765569 31997 LLVKERKSRMTASEALKHPWL 32017
Cdd:cd14169     240 LLERDPEKRFTCEQALQHPWI 260
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31757-32017 2.11e-41

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 159.06  E-value: 2.11e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEkymIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTD--QVLVKKEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd14168       9 KKIFE---FKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKgkESSIENEIAVLRKIKHENIVALEDIYESPNHLYL 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKN-SIIKIIEFGQARQLKPG 31913
Cdd:cd14168      86 VMQLVSGGELFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEeSKIMISDFGLSKMEGKG 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd14168     165 DVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSAKDF 244
                           250       260
                    ....*....|....*....|....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14168     245 IRNLMEKDPNKRYTCEQALRHPWI 268
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
31763-32020 2.36e-41

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 158.57  E-value: 2.36e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDqvlVKKEISIL-NIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14091       2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRD---PSEEIEILlRYGQHPNIITLRDVYDDGNSVYLVTELLRG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIEFGQARQLKpGDNFRLL 31919
Cdd:cd14091      79 GELLDRILRQKF-FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYadESGDPESLRICDFGFAKQLR-AENGLLM 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 ---FTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLA---ETNQQMIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd14091     157 tpcYTA-NFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASgpnDTPEVILARIGSGKIDLSGGNWDHVSDSAKDL 235
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWLKQR 32020
Cdd:cd14091     236 VRKMLHVDPSQRPTAAQVLQHPWIRNR 262
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
31761-32017 5.99e-41

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 156.14  E-value: 5.99e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd14111       3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCS 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSiIKIIEFGQARQ-----LKPGDn 31915
Cdd:cd14111      83 GKELLHSL-IDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMV-TNLNA-IKIVDFGSAQSfnplsLRQLG- 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 fRLLFTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEytFDE-EAFQEISLEAMDFI 31994
Cdd:cd14111     159 -RRTGTL-EYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAK--FDAfKLYPNVSQSASLFL 234
                           250       260
                    ....*....|....*....|...
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14111     235 KKVLSSYPWSRPTTKDCFAHAWL 257
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
31763-32016 9.32e-41

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 155.49  E-value: 9.32e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQvLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14185       2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIdksKLKGKED-MIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR--KNSIIKIIEFGQARQLKpgdnfR 31917
Cdd:cd14185      81 RGGDLFDAI-IESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNpdKSTTLKLADFGLAKYVT-----G 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFT---APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLA-ETNQQMIENIMN-AEYTFDEEAFQEISLEAMD 31992
Cdd:cd14185     155 PIFTvcgTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQlGHYEFLPPYWDNISEAAKD 234
                           250       260
                    ....*....|....*....|....
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14185     235 LISRLLVVDPEKRYTAKQVLQHPW 258
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2038-2129 1.81e-39

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 145.64  E-value: 1.81e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERS--DRIYWYWPEDNVCELVIRDVTAEDSASIMVKAIN 2115
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSsiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  2116 IAGETSSHAFLLVQ 2129
Cdd:cd20951      81 IHGEASSSASVVVE 94
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
31762-32013 1.92e-39

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 151.97  E-value: 1.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK-GTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14014       1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPElAEDEEFRErflREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqtRKNSIIKIIEFGQARQLKPGDNFR 31917
Cdd:cd14014      81 YVEGGSLADLLRERG-PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL--TEDGRVKLTDFGIARALGDSGLTQ 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 ---LLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFI 31994
Cdd:cd14014     158 tgsVLGT-PAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAII 236
                           250
                    ....*....|....*....
gi 1958765569 31995 DRLLVKERKSRMTASEALK 32013
Cdd:cd14014     237 LRALAKDPEERPQSAAELL 255
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
31763-32020 5.71e-39

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 151.72  E-value: 5.71e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQvlvKKEISIL-NIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14175       3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDP---SEEIEILlRYGQHPNIITLKDVYDDGKHVYLVTELMRG 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIEFGQARQLKpGDNFRLL 31919
Cdd:cd14175      80 GELLDKILRQKF-FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvdESGNPESLRICDFGFAKQLR-AENGLLM 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 ---FTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF---LAETNQQMIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd14175     158 tpcYTA-NFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDL 236
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWLKQR 32020
Cdd:cd14175     237 VSKMLHVDPHQRLTAKQVLQHPWITQK 263
Pkinase pfam00069
Protein kinase domain;
31763-32017 6.24e-39

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 148.93  E-value: 6.24e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV---KGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:pfam00069     1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKekiKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSaFELNEREVVSYVRQVCEALEflhsqnighfdirpeniiYQTRKNSIIkiiefgqarqlkpGDnfrll 31919
Cdd:pfam00069    81 EGGSLFDLLSEK-GAFSEREAKFIMKQILEGLE------------------SGSSLTTFV-------------GT----- 123
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 ftaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEaFQEISLEAMDFIDRLLV 31999
Cdd:pfam00069   124 ---PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLK 199
                           250
                    ....*....|....*...
gi 1958765569 32000 KERKSRMTASEALKHPWL 32017
Cdd:pfam00069   200 KDPSKRLTATQALQHPWF 217
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
31761-32017 6.46e-39

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 150.56  E-value: 6.46e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAK-FVKVKGTD-QVLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14088       1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkFLKRDGRKvRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR-KNSIIKIIEFGQARqLKPGdNFR 31917
Cdd:cd14088      81 ATGREVFDWILDQGY-YSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRlKNSKIVISDFHLAK-LENG-LIK 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIEN--------IMNAEYTFDEEAFQEISLE 31989
Cdd:cd14088     158 EPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYENhdknlfrkILAGDYEFDSPYWDDISQA 237
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31990 AMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14088     238 AKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
31761-32016 1.07e-38

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 149.80  E-value: 1.07e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQvLVKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14184       1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIdkaKCCGKEH-LIENEVSILRRVKHPNIIMLIEEMDTPAELYLVME 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENII---YQTRKNSiIKIIEFGQARQLKpGD 31914
Cdd:cd14184      80 LVKGGDLFDAI-TSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLvceYPDGTKS-LKLGDFGLATVVE-GP 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ--MIENIMNAEYTFDEEAFQEISLEAMD 31992
Cdd:cd14184     157 LYTVCGT-PTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQedLFDQILLGKLEFPSPYWDNITDSAKE 235
                           250       260
                    ....*....|....*....|....
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14184     236 LISHMLQVNVEARYTAEQILSHPW 259
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
31758-32018 6.63e-38

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 148.64  E-value: 6.63e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEkyMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTDQVLVKKEISILNIAR-HRNILYLHESFESMEELVMI 31835
Cdd:cd14174       1 DLYR--LTDELLGEGAYAKVQGCVSLQNGKEYAVKIIeKNAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLV 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQ-TRKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd14174      79 FEKLRGGSILAHIQKRKH-FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCEsPDKVSPVKICDFDLGSGVKLNS 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLL----FTAP----EYYAPEV-----HQHDVVSSATDMWSLGTLVYVLLSGINPFLAET---------------NQQ 31966
Cdd:cd14174     158 ACTPIttpeLTTPcgsaEYMAPEVvevftDEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCgtdcgwdrgevcrvcQNK 237
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31967 MIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd14174     238 LFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
31761-32016 1.01e-37

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 146.79  E-value: 1.01e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAED--LGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd14082       1 QLYQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKVIdklRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGlDIFERINTSAF-ELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKN-SIIKIIEFGQARQLKPG 31913
Cdd:cd14082      81 MEKLHG-DMLEMILSSEKgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfPQVKLCDFGFARIIGEK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE--TNQQmienIMNAEYTFDEEAFQEISLEAM 31991
Cdd:cd14082     160 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDedINDQ----IQNAAFMYPPNPWKEISPDAI 235
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14082     236 DLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
31763-32016 1.43e-37

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 146.66  E-value: 1.43e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMI-AEDLGRGEFGIVHRCVETSSKKTFMAKFVKvkgtDQVLVKKEISI-LNIARHRNILYLHESFESMEE----LVMIF 31836
Cdd:cd14089       2 YTIsKQVLGLGINGKVLECFHKKTGEKFALKVLR----DNPKARREVELhWRASGCPHIVRIIDVYENTYQgrkcLLVVM 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERIN---TSAFelNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR-KNSIIKIIEFGQArqlKP 31912
Cdd:cd14089      78 ECMEGGELFSRIQeraDSAF--TEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKgPNAILKLTDFGFA---KE 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 GDNFRLLFT---APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ----MIENIMNAEYTFDEEAFQE 31985
Cdd:cd14089     153 TTTKKSLQTpcyTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAispgMKKRIRNGQYEFPNPEWSN 232
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 31986 ISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14089     233 VSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
31763-32017 2.24e-37

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 145.86  E-value: 2.24e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG--TDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14081       3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKlsKESVLmkVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGdnfRL 31918
Cdd:cd14081      83 VSGGELFDYLVKKG-RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN--IKIADFGMASLQPEG---SL 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTA---PEYYAPEVHQHDVV-SSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFI 31994
Cdd:cd14081     157 LETScgsPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPH----FISPDAQDLL 232
                           250       260
                    ....*....|....*....|...
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14081     233 RRMLEVNPEKRITIEEIKKHPWF 255
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
31763-32017 3.99e-37

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 146.33  E-value: 3.99e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAED-LGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTDQVLVKKEISILNIAR-HRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14173       3 YQLQEEvLGEGAYARVQTCINLITNKEYAVKIIeKRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKM 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQ-TRKNSIIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd14173      83 RGGSILSHIHRRR-HFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEhPNQVSPVKICDFDLGSGIKLNSDCSP 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFT--------APEYYAPEV-----HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETN--------------QQMI-EN 31970
Cdd:cd14173     162 ISTpelltpcgSAEYMAPEVveafnEEASIYDKRCDLWSLGVILYIMLSGYPPFVGRCGsdcgwdrgeacpacQNMLfES 241
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 1958765569 31971 IMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14173     242 IQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
31763-32020 2.67e-36

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 144.00  E-value: 2.67e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQvlvKKEISIL-NIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14178       5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDP---SEEIEILlRYGQHPNIITLKDVYDDGKFVYLVMELMRG 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd14178      82 GELLDRILRQKC-FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYmdESGNPESIRICDFGFAKQLRAENGLLMT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 --FTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFL---AETNQQMIENIMNAEYTFDEEAFQEISLEAMDFI 31994
Cdd:cd14178     161 pcYTA-NFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDSISDAAKDIV 239
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPWLKQR 32020
Cdd:cd14178     240 SKMLHVDPHQRLTAPQVLRHPWIVNR 265
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
31769-32016 3.98e-36

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 141.98  E-value: 3.98e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGtdqvLVKK-------EISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14009       1 IGRGSFATVWKGRHKQTGEVVAIKEISRKK----LNKKlqenlesEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAG 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSaFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR-KNSIIKIIEFGQARQLKPGDNFRLLF 31920
Cdd:cd14009      77 GDLSQYIRKR-GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSgDDPVLKIADFGFARSLQPASMAETLC 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 TAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVK 32000
Cdd:cd14009     156 GSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRR 235
                           250
                    ....*....|....*.
gi 1958765569 32001 ERKSRMTASEALKHPW 32016
Cdd:cd14009     236 DPAERISFEEFFAHPF 251
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
31762-32015 4.37e-36

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 142.22  E-value: 4.37e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG---TDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd08215       1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNmseKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFE---LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENiIYQTRKNsIIKIIEFGQARQLkpGDN 31915
Cdd:cd08215      81 ADGGDLAQKIKKQKKKgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQN-IFLTKDG-VVKLGDFGISKVL--EST 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTA---PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAF-QEISleam 31991
Cdd:cd08215     157 TDLAKTVvgtPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYsSELR---- 232
                           250       260
                    ....*....|....*....|....
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd08215     233 DLVNSMLQKDPEKRPSANEILSSP 256
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
31761-32017 6.51e-36

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 141.54  E-value: 6.51e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTDQVLVKK---EISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd14099       1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVpKSSLTKPKQREKlksEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISG---LDIFERINTsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLK-P 31912
Cdd:cd14099      81 ELCSNgslMELLKRRKA----LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLD--ENMNVKIGDFGLAARLEyD 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 GDNFRLLFTAPEYYAPEV------HQHDVvssatDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfqEI 31986
Cdd:cd14099     155 GERKKTLCGTPNYIAPEVlekkkgHSFEV-----DIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHL--SI 227
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 31987 SLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14099     228 SDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31762-32016 6.71e-36

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 141.39  E-value: 6.71e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMakfVKVKGTDQVL-------VKKEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd14663       1 RYELGRTLGEGTFAKVKFARNTKTGESVA---IKIIDKEQVAregmveqIKREIAIMKLLRHPNIVELHEVMATKTKIFF 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGD 31914
Cdd:cd14663      78 VMELVTGGELFSKI-AKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGN--LKISDFGLSALSEQFR 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFT---APEYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEA 31990
Cdd:cd14663     155 QDGLLHTtcgTPNYVAPEVlARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYP----RWFSPGA 230
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14663     231 KSLIKRILDPNPSTRITVEQIMASPW 256
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
31762-32017 9.78e-36

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 140.98  E-value: 9.78e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK---------VKGTDQVLVKKEISI---LNIARHRNILYLHESFESM 31829
Cdd:cd14004       1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFkerilvdtwVRDRKLGTVPLEIHIldtLNKRSHPNIVKLLDFFEDD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 E--ELVMIfEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQA 31907
Cdd:cd14004      81 EfyYLVME-KHGSGMDLFDFIERKP-NMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILD--GNGTIKLIDFGSA 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLKPGdNFRLLFTAPEYYAPEVHQHD-VVSSATDMWSLGTLVYVLLSGINPFLAetnqqmIENIMNAEYTFDeeafQEI 31986
Cdd:cd14004     157 AYIKSG-PFDTFVGTIDYAAPEVLRGNpYGGKEQDIWALGVLLYTLVFKENPFYN------IEEILEADLRIP----YAV 225
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 31987 SLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14004     226 SEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
31769-32017 1.24e-35

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 140.45  E-value: 1.24e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISIL----NIARHRNILYLHESFESMEE--LVMIFEFIsGL 31842
Cdd:cd05118       7 IGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLkhlnDVEGHPNIVKLLDVFEHRGGnhLCLVFELM-GM 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrKNSIIKIIEFGQARQLKPGDNFRLLFTA 31922
Cdd:cd05118      86 NLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINL-ELGQLKLADFGLARSFTSPPYTPYVATR 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PeYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMnaeytfdeeafqEI--SLEAMDFIDRLLV 31999
Cdd:cd05118     165 W-YRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIV------------RLlgTPEALDLLSKMLK 231
                           250
                    ....*....|....*...
gi 1958765569 32000 KERKSRMTASEALKHPWL 32017
Cdd:cd05118     232 YDPAKRITASQALAHPYF 249
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
31760-32018 1.74e-35

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 142.10  E-value: 1.74e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVlvKKEISILNIAR-HRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14179       6 YELDLKDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANT--QREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMEL 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR-KNSIIKIIEFGQARqLKPGDNFR 31917
Cdd:cd14179      84 LKGGELLERIKKKQ-HFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDEsDNSEIKIIDFGFAR-LKPPDNQP 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 L---LFTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE-------TNQQMIENIMNAEYTFDEEAFQEIS 31987
Cdd:cd14179     162 LktpCFTL-HYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHdksltctSAEEIMKKIKQGDFSFEGEAWKNVS 240
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 31988 LEAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd14179     241 QEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQ 271
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
31747-32017 6.71e-35

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 141.31  E-value: 6.71e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31747 TMTKASHSKTKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVlvkKEISIL-NIARHRNILYLHES 31825
Cdd:cd14176       5 SIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT---EEIEILlRYGQHPNIITLKDV 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31826 FESMEELVMIFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIE 31903
Cdd:cd14176      82 YDDGKYVYVVTELMKGGELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdESGNPESIRICD 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31904 FGQARQLKPGDNFRLL--FTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFL---AETNQQMIENIMNAEYTF 31978
Cdd:cd14176     161 FGFAKQLRAENGLLMTpcYTA-NFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSL 239
                           250       260       270
                    ....*....|....*....|....*....|....*....
gi 1958765569 31979 DEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14176     240 SGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
31761-32017 1.11e-34

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 138.59  E-value: 1.11e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQvLVKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14183       6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIInksKCRGKEH-MIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPEN-IIYQTRKNS-IIKIIEFGQArQLKPGDN 31915
Cdd:cd14183      85 LVKGGDLFDAI-TSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENlLVYEHQDGSkSLKLGDFGLA-TVVDGPL 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ--MIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd14183     163 YTVCGT-PTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQevLFDQILMGQVDFPSPYWDNVSDSAKEL 241
                           250       260
                    ....*....|....*....|....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14183     242 ITMMLQVDVDQRYSALQVLEHPWV 265
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
31763-32017 1.16e-34

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 138.08  E-value: 1.16e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCveTSSKKTFMAKF-VKV----KGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd14080       2 YRLGKTIGEGSYSKVKLA--EYTKSGLKEKVaCKIidkkKAPKDFLEKflpRELEILRKLRHPNIIQVYSIFERGSKVFI 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGD 31914
Cdd:cd14080      80 FMEYAEHGDLLEYIQKRGA-LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN--VKLSDFGFARLCPDDD 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFT---APEYYAPEVHQ---HDvvSSATDMWSLGTLVYVLLSGINPFlAETN-QQMIENIMNAEYTFDEEAfQEIS 31987
Cdd:cd14080     157 GDVLSKTfcgSAAYAAPEILQgipYD--PKKYDIWSLGVILYIMLCGSMPF-DDSNiKKMLKDQQNRKVRFPSSV-KKLS 232
                           250       260       270
                    ....*....|....*....|....*....|
gi 1958765569 31988 LEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14080     233 PECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
31769-32017 3.28e-34

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 136.88  E-value: 3.28e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKtFMA-KFVKVKGTDQVLV---KKEISILNIARHRNIL-YLHesFESMEELVMIF-EFISGL 31842
Cdd:cd06606       8 LGKGSFGSVYLALNLDTGE-LMAvKEVELSGDSEEELealEREIRILSSLKHPNIVrYLG--TERTENTLNIFlEYVPGG 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTsaFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd06606      85 SLASLLKK--FGkLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDS--DGVVKLADFGCAKRLAEIATGEGTKS 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 A---PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFlAETNQQMIenIMNAeYTFDEEAFQ---EISLEAMDFID 31995
Cdd:cd06606     161 LrgtPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW-SELGNPVA--ALFK-IGSSGEPPPipeHLSEEAKDFLR 236
                           250       260
                    ....*....|....*....|..
gi 1958765569 31996 RLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06606     237 KCLQRDPKKRPTADELLQHPFL 258
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
31761-32017 3.32e-34

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 136.89  E-value: 3.32e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVEtssKKTFMAKFVKVK----GTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd14112       3 GRFSFGSEIFRGRFSVIVKAVD---STTETDAHCAVKifevSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVM 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGlDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPG--- 31913
Cdd:cd14112      80 EKLQE-DVFTRF-SSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSKLgkv 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 -DNFRLLFTAPEYYAPEVHqhdvVSSATDMWSLGTLVYVLLSGINPFLAE--TNQQMIENIMNAEYTFdEEAFQEISLEA 31990
Cdd:cd14112     158 pVDGDTDWASPEFHNPETP----ITVQSDIWGLGVLTFCLLSGFHPFTSEydDEEETKENVIFVKCRP-NLIFVEATQEA 232
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14112     233 LRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
31761-32017 4.15e-34

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 137.57  E-value: 4.15e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMA-KFVK--------VKGTDQVLVKKEISILNIARHRNILYLHESFESMEE 31831
Cdd:cd14096       1 ENYRLINKIGEGAFSNVYKAVPLRNTGKPVAiKVVRkadlssdnLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISGLDIFERI--NTSAFELNEREVVsyvRQVCEALEFLHSQNIGHFDIRPENIIYQT----------RKNS-- 31897
Cdd:cd14096      81 YYIVLELADGGEIFHQIvrLTYFSEDLSRHVI---TQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklRKADdd 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31898 -------------------IIKIIEFGQARQLKPGDNFRLLFTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINP 31958
Cdd:cd14096     158 etkvdegefipgvggggigIVKLADFGLSKQVWDSNTKTPCGTV-GYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPP 236
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31959 FLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14096     237 FYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
31760-32017 7.61e-34

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 135.82  E-value: 7.61e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14110       2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIF----ERINTSafelnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNsIIKIIEFGQARQLKPG-- 31913
Cdd:cd14110      82 SGPELLynlaERNSYS-----EAEVTDYLWQILSAVDYLHSRRILHLDLRSENMII-TEKN-LLKIVDLGNAQPFNQGkv 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 ---DNFRLLFtapEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFdEEAFQEISLEA 31990
Cdd:cd14110     155 lmtDKKGDYV---ETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQL-SRCYAGLSGGA 230
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14110     231 VNFLKSTLCAKPWGRPTASECLQNPWL 257
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
14277-14730 9.48e-34

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 143.99  E-value: 9.48e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14277 AVNVCGRATAVVEVNVLDKPGPPAAFdITDVTNESCLLTWNPPRDDGGSKITNYVVERKATDSDVWHKLSSTVKDTNfka 14356
Cdd:COG3401     121 AVGTATTATAVAGGAATAGTYALGAG-LYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGG--- 196
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14357 TKLTPNKEYIFRVAAENmyGVGEPVQATPIIAKYQFDPPGPPTRLEPSDITKDAVTLTWcepDDDGGSPITGYWVERLDP 14436
Cdd:COG3401     197 GDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW---DPVTESDATGYRVYRSNS 271
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14437 DTDKWVRCNKmpVKDTTYRVKGLTNKKKYRFRVLAENLAGpgKPSRSTEPILIKDPIDPPWPPGKPTVKDIGKTSLVLNW 14516
Cdd:COG3401     272 GDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW 347
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14517 TKPEhdgGAKIESYVIEMLKTGTDDWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKAG-ESEPSEPSDPvlcrEKLYP 14595
Cdd:COG3401     348 TASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSA----TTASA 420
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14596 PSPPRWLEVINITKNTADLKWTVPEKDGGSPITNYIVEKRDVRRKGWQTVDTTVKDtkcTVTPLTEGSLYVFRVAAENAI 14675
Cdd:COG3401     421 ASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSST---VTATTTDTTTANLSVTTGSLV 497
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 14676 GQSDYTEIGDSVLAKDTFTTPGPPYALTVVDVTKRHVDLKWEPPKNDGGRPIQRY 14730
Cdd:COG3401     498 GGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVS 552
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
31763-32017 1.58e-33

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 134.70  E-value: 1.58e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT--DQVLvkKEISILNIAR------HRNILYLHESFESMEELVM 31834
Cdd:cd14133       1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDylDQSL--DEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISG--LDIFERINTSAFELNEreVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKP 31912
Cdd:cd14133      79 VFELLSQnlYEFLKQNKFQYLSLPR--IRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIIDFGSSCFLTQ 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 GDNFrllFTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENI----------MNAEYTFDEE 31981
Cdd:cd14133     157 RLYS---YIQSRYYrAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIigtigippahMLDQGKADDE 233
                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 1958765569 31982 AFqeisleaMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14133     234 LF-------VDFLKKLLEIDPKERPTASQALSHPWL 262
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
22668-22749 1.94e-33

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 127.71  E-value: 1.94e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22668 TFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNV 22747
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22748 IV 22749
Cdd:cd05748      81 KV 82
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
31756-32013 2.10e-33

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 140.53  E-value: 2.10e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31756 TKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV----LVKKEISILNIARHRNILYLHESFESMEE 31831
Cdd:COG0515       2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPeareRFRREARALARLNHPNIVRVYDVGEEDGR 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqtRKNSIIKIIEFGQARQLK 31911
Cdd:COG0515      82 PYLVMEYVEGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL--TPDGRVKLIDFGIARALG 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFR---LLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISL 31988
Cdd:COG0515     159 GATLTQtgtVVGT-PGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPP 237
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31989 EAMDFIDRLLVKERKSR-MTASEALK 32013
Cdd:COG0515     238 ALDAIVLRALAKDPEERyQSAAELAA 263
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
31767-32017 2.38e-33

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 135.28  E-value: 2.38e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFV--KVKGTDQVLVKKEIS----ILNIAR-HRN-ILYLHESfESMEELVMIFEF 31838
Cdd:cd14171      12 QKLGTGISGPVRVCVKKSTGERFALKILldRPKARTEVRLHMMCSghpnIVQIYDvYANsVQFPGES-SPRARLLIVMEL 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQ-TRKNSIIKIIEFGQARqLKPGDNFR 31917
Cdd:cd14171      91 MEGGELFDRISQHR-HFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKdNSEDAPIKLCDFGFAK-VDQGDLMT 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTaPEYYAPEV---------HQHDVVSSAT--------DMWSLGTLVYVLLSGINPFLAETNQQMIEN-----IMNAE 31975
Cdd:cd14171     169 PQFT-PYYVAPQVleaqrrhrkERSGIPTSPTpytydkscDMWSLGVIIYIMLCGYPPFYSEHPSRTITKdmkrkIMTGS 247
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 31976 YTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14171     248 YEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
31763-32017 4.43e-33

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 133.83  E-value: 4.43e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHR--CVETSsKKTFMAKFVKVK-GTDQV-LVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14097       3 YTFGRKLGQGSFGVVIEatHKETQ-TKWAIKKINREKaGSSAVkLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQT-----RKNSIIKIIEFGQARQLKPG 31913
Cdd:cd14097      82 CEDGELKELLLRKGF-FSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSsiidnNDKLNIKVTDFGLSVQKYGL 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 --DNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAM 31991
Cdd:cd14097     161 geDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAK 240
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14097     241 NVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
31761-32020 4.70e-33

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 134.76  E-value: 4.70e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQvlvKKEISIL-NIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14177       4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDP---SEEIEILmRYGQHPNIITLKDVYDDGRYVYLVTELM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSI--IKIIEFGQARQLKpGDNFR 31917
Cdd:cd14177      81 KGGELLDRILRQKF-FSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdsIRICDFGFAKQLR-GENGL 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LL---FTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFL---AETNQQMIENIMNAEYTFDEEAFQEISLEAM 31991
Cdd:cd14177     159 LLtpcYTA-NFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVSDAAK 237
                           250       260
                    ....*....|....*....|....*....
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPWLKQR 32020
Cdd:cd14177     238 DLLSHMLHVDPHQRYTAEQVLKHSWIACR 266
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
31771-32018 5.40e-33

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 133.50  E-value: 5.40e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31771 RGEFGIVHRCVETSSKKTFMAKFVKVKG------TDQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05579       3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDmirknqVDSVLAERNI--LSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 F---ERINTsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFG------QARQLKPG-- 31913
Cdd:cd05579      81 YsllENVGA----LDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILID--ANGHLKLTDFGlskvglVRRQIKLSiq 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 ---------DNFRLLFTaPEYYAPEV---HQHdvvSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEE 31981
Cdd:cd05579     155 kksngapekEDRRIVGT-PDYLAPEIllgQGH---GKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPED 230
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|
gi 1958765569 31982 afQEISLEAMDFIDRLLVKERKSRM---TASEALKHPWLK 32018
Cdd:cd05579     231 --PEVSDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFK 268
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
31763-32017 6.16e-33

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 132.92  E-value: 6.16e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVhrcveTSSKKTFMAKFVKVKGTDQVLVK--------KEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd14074       5 YDLEETLGRGHFAVV-----KLARHVFTGEKVAVKVIDKTKLDdvskahlfQEVRCMKLVQHPNVVRLYEVIDTQTKLYL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd14074      80 ILELGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVF-FEKQGLVKLTDFGFSNKFQPGE 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPEYYAPEVHQHDVVSS-ATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDF 31993
Cdd:cd14074     159 KLETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPA----HVSPECKDL 234
                           250       260
                    ....*....|....*....|....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14074     235 IRRMLIRDPKKRASLEEIENHPWL 258
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
21297-21376 6.29e-33

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 126.55  E-value: 6.29e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21297 TLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKH--RANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVNV 21374
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 21375 RV 21376
Cdd:cd05748      81 KV 82
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
31818-32017 1.68e-32

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 132.04  E-value: 1.68e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31818 NILYLHESFESMEE----LVMIFEFISGLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQ 31892
Cdd:cd14172      58 HIVHILDVYENMHHgkrcLLIIMECMEGGELFSRIQERGDQaFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYT 137
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31893 TR-KNSIIKIIEFGQARQLKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ----M 31967
Cdd:cd14172     138 SKeKDAVLKLTDFGFAKETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAispgM 217
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31968 IENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14172     218 KRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
31767-32018 2.70e-32

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 131.18  E-value: 2.70e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFE 31846
Cdd:cd06614       6 EKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGSLTD 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31847 RINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFR--LLFTaPE 31924
Cdd:cd06614      86 IITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLS--KDGSVKLADFGFAAQLTKEKSKRnsVVGT-PY 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31925 YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFlaetnqqMIENIMNAEYTFDEEAFQEI------SLEAMDFIDRLL 31998
Cdd:cd06614     163 WMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPY-------LEEPPLRALFLITTKGIPPLknpekwSPEFKDFLNKCL 235
                           250       260
                    ....*....|....*....|
gi 1958765569 31999 VKERKSRMTASEALKHPWLK 32018
Cdd:cd06614     236 VKDPEKRPSAEELLQHPFLK 255
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
20503-20584 2.98e-32

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 124.62  E-value: 2.98e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20503 CYLAKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSI 20582
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 20583 KV 20584
Cdd:cd05748      81 KV 82
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
31762-32017 5.92e-32

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 130.02  E-value: 5.92e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG-TDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd05122       1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESkEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGdNFRLLF 31920
Cdd:cd05122      81 GGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTS--DGEVKLIDFGLSAQLSDG-KTRNTF 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 T-APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ-MIENIMNAEYTFDEEafQEISLEAMDFIDRLL 31998
Cdd:cd05122     158 VgTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKaLFLIATNGPPGLRNP--KKWSKEFKDFLKKCL 235
                           250
                    ....*....|....*....
gi 1958765569 31999 VKERKSRMTASEALKHPWL 32017
Cdd:cd05122     236 QKDPEKRPTAEQLLKHPFI 254
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
31769-32016 1.10e-31

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 129.65  E-value: 1.10e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK----VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05572       1 LGVGGFGRVELVQLKSKGRTFALKCVKkrhiVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLLFTAPE 31924
Cdd:cd05572      81 WTILRDRG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLD--SNGYVKLVDFGFAKKLGSGRKTWTFCGTPE 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31925 YYAPEV---HQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQQMIenIMNA--EYTFDEEAFQEISLEAMDFIDRLLV 31999
Cdd:cd05572     158 YVAPEIilnKGYD---FSVDYWSLGILLYELLTGRPPFGGDDEDPMK--IYNIilKGIDKIEFPKYIDKNAKNLIKQLLR 232
                           250       260
                    ....*....|....*....|..
gi 1958765569 32000 KERKSRM-----TASEALKHPW 32016
Cdd:cd05572     233 RNPEERLgylkgGIRDIKKHKW 254
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
31826-32022 2.07e-31

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 130.15  E-value: 2.07e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31826 FESMEELVMIFEFISGLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQT-RKNSIIKIIE 31903
Cdd:cd14170      68 YAGRKCLLIVMECLDGGELFSRIQDRGDQaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkRPNAILKLTD 147
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31904 FGQARQLKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE----TNQQMIENIMNAEYTFD 31979
Cdd:cd14170     148 FGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaISPGMKTRIRMGQYEFP 227
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 1958765569 31980 EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLKQRMD 32022
Cdd:cd14170     228 NPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTK 270
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
31763-32017 2.42e-31

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 128.54  E-value: 2.42e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVL-VKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14079       4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILnrqKIKSLDMEEkIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd14079      84 VSGGELFDYI-VQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMN--VKIADFGLSNIMRDGEFLKT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAPEvhqhdVVS------SATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMD 31992
Cdd:cd14079     161 SCGSPNYAAPE-----VISgklyagPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPS----HLSPGARD 231
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14079     232 LIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
31759-32017 3.33e-31

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 127.88  E-value: 3.33e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVK-GTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd14078       1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMdKKAlGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNF 31916
Cdd:cd14078      81 EYCPGGELFDYI-VAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN--LKLIDFGLCAKPKGGMDH 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFT--APEYYAPEVHQHD-VVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYtfDEEAFqeISLEAMDF 31993
Cdd:cd14078     158 HLETCcgSPAYAAPELIQGKpYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKY--EEPEW--LSPSSKLL 233
                           250       260
                    ....*....|....*....|....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14078     234 LDQMLQVDPKKRITVKELLNHPWV 257
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
31762-32017 4.99e-31

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 127.34  E-value: 4.99e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV---LVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd06627       1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSdlkSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 I---SGLDIFERINTsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKP--G 31913
Cdd:cd06627      81 VengSLASIIKKFGK----FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANIL--TTKDGLVKLADFGVATKLNEveK 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFlAETNQqmieniMNAEY---TFDEEAFQE-ISLE 31989
Cdd:cd06627     155 DENSVVGT-PYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPY-YDLQP------MAALFrivQDDHPPLPEnISPE 226
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31990 AMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06627     227 LRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
31769-32016 7.52e-31

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 128.08  E-value: 7.52e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFM------AKFVKVKGTDQVlvKKEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05580       9 LGTGSFGRVRLVKHKDSGKYYAlkilkkAKIIKLKQVEHV--LNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPGG 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTS-AFELNEREVvsYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKpgDNFRLLFT 31921
Cdd:cd05580      87 ELFSLLRRSgRFPNDVAKF--YAAEVVLALEYLHSLDIVYRDLKPENLL--LDSDGHIKITDFGFAKRVK--DRTYTLCG 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLLVKE 32001
Cdd:cd05580     161 TPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFP----SFFDPDAKDLIKRLLVVD 236
                           250       260
                    ....*....|....*....|
gi 1958765569 32002 RKSRMTA----SEALK-HPW 32016
Cdd:cd05580     237 LTKRLGNlkngVEDIKnHPW 256
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
31761-32017 7.55e-31

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 126.98  E-value: 7.55e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG---TDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14002       1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGkseKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGlDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDnfr 31917
Cdd:cd14002      81 YAQG-ELFQILEDDG-TLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG--KGGVVKLCDFGFARAMSCNT--- 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTA----PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDF 31993
Cdd:cd14002     154 LVLTSikgtPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPS----NMSPEFKSF 229
                           250       260
                    ....*....|....*....|....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14002     230 LQGLLNKDPSKRLSWPDLLEHPFV 253
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
23463-23542 8.83e-31

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 120.39  E-value: 8.83e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23463 VINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDA--AIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTV 23540
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgrVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 23541 RV 23542
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
24546-24624 1.28e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 119.62  E-value: 1.28e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24546 IVVRAGGSARIHIPFKGRPTPEITWSKEEGEF--TDKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVK 24623
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 24624 V 24624
Cdd:cd05748      82 V 82
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
31762-32017 1.33e-30

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 126.41  E-value: 1.33e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGE---FGIVHRCVETSSKKTFMAKFVKVKGTDQvLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14077      16 KVKLAKHIRTGEkcaIKIIPRASNAGLKKEREKRLEKEISRDI-RTIREAALSSLLNHPHICRLRDFLRTPNHYYMLFEY 94
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFR- 31917
Cdd:cd14077      95 VDGGQLLDYI-ISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILIS--KSGNIKIIDFGLSNLYDPRRLLRt 171
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 ----LLFTAPE------YYAPEVhqhdvvssatDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEIS 31987
Cdd:cd14077     172 fcgsLYFAAPEllqaqpYTGPEV----------DVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYP----SYLS 237
                           250       260       270
                    ....*....|....*....|....*....|
gi 1958765569 31988 LEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14077     238 SECKSLISRMLVVDPKKRATLEQVLNHPWM 267
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
28878-28957 2.04e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 119.23  E-value: 2.04e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28878 THIVRAGASIRLFIAYQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFTV 28955
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 28956 KV 28957
Cdd:cd05748      81 KV 82
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
31761-32017 2.41e-30

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 125.52  E-value: 2.41e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL---VKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14069       1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCpenIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERIntsAFE--LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDN 31915
Cdd:cd14069      81 YASGGELFDKI---EPDvgMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDN--LKISDFGLATVFRYKGK 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTA---PEYYAPEVHQHDVV-SSATDMWSLGTLVYVLLSGINPF-LAETNQQMIENIMNAEyTFDEEAFQEISLEA 31990
Cdd:cd14069     156 ERLLNKMcgtLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWdQPSDSCQEYSDWKENK-KTYLTPWKKIDTAA 234
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14069     235 LSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
31762-32017 4.75e-30

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 124.42  E-value: 4.75e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKG-TDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14073       2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIkkdKIEDeQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVME 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFR 31917
Cdd:cd14073      82 YASGGELYDYISERR-RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN--AKIADFGLSNLYSKDKLLQ 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 L-----LFTAPE------YYAPEVhqhdvvssatDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYtFDEEafqEI 31986
Cdd:cd14073     159 TfcgspLYASPEivngtpYQGPEV----------DCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDY-REPT---QP 224
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 31987 SlEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14073     225 S-DASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
31763-32017 8.38e-30

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 123.99  E-value: 8.38e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14075       4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILdktKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYA 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd14075      84 SGGELYTKISTEG-KLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYAS--NNCVKVGDFGFSTHAKRGETLNTF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYYAPEVHQHD-VVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRLL 31998
Cdd:cd14075     161 CGSPPYAAPELFKDEhYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPS----YVSEPCQELIRGIL 236
                           250
                    ....*....|....*....
gi 1958765569 31999 VKERKSRMTASEALKHPWL 32017
Cdd:cd14075     237 QPVPSDRYSIDEIKNSEWL 255
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
21587-21667 1.48e-29

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 116.92  E-value: 1.48e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITIQ 21666
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 21667 V 21667
Cdd:cd05748      82 V 82
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
31761-32017 1.79e-29

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 123.14  E-value: 1.79e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSK-----KTFMAKFVKVKGTDQVLvKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd14116       5 EDFEIGRPLGKGKFGNVYLAREKQSKfilalKVLFKAQLEKAGVEHQL-RREVEIQSHLRHPNILRLYGYFHDATRVYLI 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQlKPGDN 31915
Cdd:cd14116      84 LEYAPLGTVYRELQKLS-KFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS--AGELKIADFGWSVH-APSSR 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFID 31995
Cdd:cd14116     160 RTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPD----FVTEGARDLIS 235
                           250       260
                    ....*....|....*....|..
gi 1958765569 31996 RLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14116     236 RLLKHNPSQRPMLREVLEHPWI 257
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
31769-32020 3.76e-29

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 122.32  E-value: 3.76e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV--LVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG--L-D 31843
Cdd:cd06623       9 LGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFrkQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGgsLaD 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTsafeLNEReVVSYV-RQVCEALEFLHSQ-NIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLF- 31920
Cdd:cd06623      89 LLKKVGK----IPEP-VLAYIaRQILKGLDYLHTKrHIIHRDIKPSNLLINSKGE--VKIADFGISKVLENTLDQCNTFv 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 -TAPeYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAeTNQ----QMIENIMNAE-YTFDEEAFqeiSLEAMDFI 31994
Cdd:cd06623     162 gTVT-YMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLP-PGQpsffELMQAICDGPpPSLPAEEF---SPEFRDFI 236
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPWLKQR 32020
Cdd:cd06623     237 SACLQKDPKKRPSAAELLQHPFIKKA 262
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
13617-13962 4.16e-29

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 129.35  E-value: 4.16e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13617 EVSLAWEEPLTDGGSKIIGYVVER-RDIKRKTWVLVTDRADSCEFTVTGLQKGGVEYLFRVSARNRVGTGEPvetDSPVE 13695
Cdd:COG3401     149 GVDGANASGTTASSVAGAGVVVSPdTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP---SNEVS 225
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13696 ARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEYDGgaeITNYVIELRDKTSIRWDTAMTVRaeDLSATVTDVVEGQEYSF 13775
Cdd:COG3401     226 VTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTYYY 300
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13776 RVRAQNriGVGKPSAATPFVKVADPIERPSPPVNLSASEQTQSSVQLTWEPPLkdgGSPILGYIIERQEEGKDNWIRCNm 13855
Cdd:COG3401     301 RVTAVD--AAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIA- 374
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13856 KPVPELTYKVTGLQKGNKYLYRVSAENAAGV-SDPSEILGPLTADDASVEPTMDLSAFKDGLEVIVPNPIKILVPSTGYp 13934
Cdd:COG3401     375 ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGV- 453
                           330       340
                    ....*....|....*....|....*...
gi 1958765569 13935 rpKATWTFGDQVLEAGDRVKIKTISAYA 13962
Cdd:COG3401     454 --SAAVLADGGDTGNAVPFTTTSSTVTA 479
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
31760-32026 5.08e-29

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 123.44  E-value: 5.08e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGtdQVLVKKEISILNIAR-HRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14180       5 YELDLEEPALGEGSFSVCRKCRHRQSGQEYAVKIISRRM--EANTQREVAALRLCQsHPNIVALHEVLHDQYHTYLVMEL 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTR-KNSIIKIIEFGQARqLKPGDNFR 31917
Cdd:cd14180      83 LRGGELLDRIKKKAR-FSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADEsDGAVLKVIDFGFAR-LRPQGSRP 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 L---LFTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQ-------QMIENIMNAEYTFDEEAFQEIS 31987
Cdd:cd14180     161 LqtpCFTL-QYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEGEAWKGVS 239
                           250       260       270
                    ....*....|....*....|....*....|....*....
gi 1958765569 31988 LEAMDFIDRLLVKERKSRMTASEALKHPWLKQRMDRVST 32026
Cdd:cd14180     240 EEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSST 278
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
27793-27874 9.10e-29

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 114.61  E-value: 9.10e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27793 VIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGqPKSSTVSV 27872
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG-EKSATINV 80

                    ..
gi 1958765569 27873 KV 27874
Cdd:cd05748      81 KV 82
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
31763-32017 1.20e-28

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 120.48  E-value: 1.20e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14162       2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVsKKKAPEDYLQKflpREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQAR-QLKPGDNFR 31917
Cdd:cd14162      82 AENGDLLDYIRKNGA-LPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLD--KNNNLKITDFGFARgVMKTKDGKP 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LL---FTAPEYYA-PEVHQ---HDVVSSatDMWSLGTLVYVLLSGINPFlAETNQQMIENIMNAEYTFdeEAFQEISLEA 31990
Cdd:cd14162     159 KLsetYCGSYAYAsPEILRgipYDPFLS--DIWSMGVVLYTMVYGRLPF-DDSNLKVLLKQVQRRVVF--PKNPTVSEEC 233
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31991 MDFIDRLLVKErKSRMTASEALKHPWL 32017
Cdd:cd14162     234 KDLILRMLSPV-KKRITIEEIKRDPWF 259
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
31760-32017 1.62e-28

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 121.05  E-value: 1.62e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKymiAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV-KGTDQVLVK--KEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd07829       1 YEK---LEKLGEGTYGVVYKAKDKKTGEIVALKKIRLdNEEEGIPSTalREISLLKELKHPNIVKLLDVIHTENKLYLVF 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISgLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNsIIKIIEFGQARQlkpgdnf 31916
Cdd:cd07829      78 EYCD-QDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLI-NRDG-VLKLADFGLARA------- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 rllFTAPE-----------YYAPEV----HQHdvvSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMN-------- 31973
Cdd:cd07829     148 ---FGIPLrtythevvtlwYRAPEIllgsKHY---STAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQilgtptee 221
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31974 --------AEYTFD---------EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07829     222 swpgvtklPDYKPTfpkwpkndlEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28619-28996 2.03e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 127.43  E-value: 2.03e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28619 EAQSYTAIKLITGNEYQFRVSAVNKFGVGRPleSDPVVAQIQYTIPDAPGIPEPSNVTGNSITLTWTRPESDGgneIQHY 28698
Cdd:COG3401     190 TTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGY 264
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28699 ILERREKKSTRWVKVISkrpISETRFKVTGLVEGNEYEFHVMAENAAGVGpaSGISRLIKCREPVNPPSAPAVVKVTDTS 28778
Cdd:COG3401     265 RVYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGNE--SAPSNVVSVTTDLTPPAAPSGLTATAVG 339
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28779 KTTVSLEWArPVFDGGmeIIGYIIEMCKADLGDWHKVnTEPCVKTRYTVTDLQAGEEYKFRVSAINGAGK--GDSCEVTG 28856
Cdd:COG3401     340 SSSITLSWT-ASSDAD--VTGYNVYRSTSGGGTYTKI-AETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesAPSEEVSA 415
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28857 TIKAVDR---LSAPELDIDANFKQTHIVRAGASIR-LFIAYQGRPTPTAVWSKPDSNLSIraDIHTTDSFSTLTVENCNR 28932
Cdd:COG3401     416 TTASAASgesLTASVDAVPLTDVAGATAAASAASNpGVSAAVLADGGDTGNAVPFTTTSS--TVTATTTDTTTANLSVTT 493
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 28933 NDAGKYTLTVENNSGRKSITFT---VKVLDSPGPPGPITFKDVTRGSATLMWDAPLLDGGARIHHYV 28996
Cdd:COG3401     494 GSLVGGSGASSVTNSVSVIGASaaaAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
31771-32018 2.63e-28

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 119.89  E-value: 2.63e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31771 RGEFGIVHRCVETSSKKTFMAKFVKVKGTD---QVL-VKKEISILNIARHR-NILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd05611       6 KGAFGSVYLAKKRSTGDYFAIKVLKKSDMIaknQVTnVKAERAIMMIQGESpYVAKLYYSFQSKDYLYLVMEYLNGGDCA 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFTAPEY 31925
Cdd:cd05611      86 SLIKTLGG-LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGH--LKLTDFGLSRNGLEKRHNKKFVGTPDY 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31926 YAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSR 32005
Cdd:cd05611     163 LAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLCMDPAKR 242
                           250
                    ....*....|....*.
gi 1958765569 32006 MTAS---EALKHPWLK 32018
Cdd:cd05611     243 LGANgyqEIKSHPFFK 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
31769-32017 6.45e-28

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 118.51  E-value: 6.45e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL-----VKKEISILNIARHRNILYLHESF--ESMEELVMIFEF-IS 31840
Cdd:cd14119       1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPngeanVKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEYcVG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDifERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd14119      81 GLQ--EMLDSAPDKrLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTT--DGTLKISDFGVAEALDLFAEDDTC 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTA---PEYYAPEVHQHDVVSS--ATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFI 31994
Cdd:cd14119     157 TTSqgsPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPD----DVDPDLQDLL 232
                           250       260
                    ....*....|....*....|...
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14119     233 RGMLEKDPEKRFTIEQIRQHPWF 255
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
13874-14373 6.52e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.89  E-value: 6.52e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13874 YLYRVSAENAAGVSDPSEILGPLTADDASVEPTMDLSAFKDGLEVIVPNPIKILVPSTGYPRPKATWTFGDQVLEAGDRV 13953
Cdd:COG3401     101 GSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAV 180
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13954 KIKTISAYAELIISPSERPDKGI-YTLTL----ENPVKSISGEIDVNVIAR-PSAPKELKFSDVTKDSVHLTWEPPDDDG 14027
Cdd:COG3401     181 ATTSLTVTSTTLVDGGGDIEPGTtYYYRVaatdTGGESAPSNEVSVTTPTTpPSAPTGLTATADTPGSVTLSWDPVTESD 260
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14028 gspLTGYVVEKRDMSRKTWTKVmDFVTDLEFTVPDLVQGKEYLFKVCARNKCGpGEPAYTDEpVNMSAPATVPDPPENVK 14107
Cdd:COG3401     261 ---ATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYYRVTAVDAAG-NESAPSNV-VSVTTDLTPPAAPSGLT 334
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14108 WRDRTANSIFLTWDPPKNDGgsrIKGYIVEKCPRGSDKWVACGEPVPDTKMEVTGLEEGKWYAYRVKALNRQGASkpSKP 14187
Cdd:COG3401     335 ATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAP 409
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14188 TEEIQAVDTQEAPEIFLD-----VKLLAGLTVKAGTKIELPATVTGK---PEPKITWTKADTLLRPDQRITIENVP--KK 14257
Cdd:COG3401     410 SEEVSATTASAASGESLTasvdaVPLTDVAGATAAASAASNPGVSAAvlaDGGDTGNAVPFTTTSSTVTATTTDTTtaNL 489
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14258 STVTITDSKRSDTGTYIIEAVNVCGRATAVVeVNVLDKPGPPAAFDITDVTNESCLLTWNPPRDDGGSKITNYvverkat 14337
Cdd:COG3401     490 SVTTGSLVGGSGASSVTNSVSVIGASAAAAV-GGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSV------- 561
                           490       500       510
                    ....*....|....*....|....*....|....*.
gi 1958765569 14338 dSDVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAEN 14373
Cdd:COG3401     562 -SGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVH 596
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29967-30046 6.74e-28

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 111.91  E-value: 6.74e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29967 TVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLAN--RAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLV 30044
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 30045 KV 30046
Cdd:cd05748      81 KV 82
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
31770-32017 8.14e-28

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 118.13  E-value: 8.14e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31770 GRGEFGIVHRCVETSSKKTFMAKF---VKVKGTDQV-LVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI- 31844
Cdd:cd05578       9 GKGSFGKVCIVQKKDTKKMFAMKYmnkQKCIEKDSVrNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDLr 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAFelNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLLFTAPE 31924
Cdd:cd05578      89 YHLQQKVKF--SEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLD--EQGHVHITDFNIATKLTDGTLATSTSGTKP 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31925 YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNqQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKS 32004
Cdd:cd05578     165 YMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSR-TSIEEIRAKFETASVLYPAGWSEEAIDLINKLLERDPQK 243
                           250
                    ....*....|....
gi 1958765569 32005 RMTASEALK-HPWL 32017
Cdd:cd05578     244 RLGDLSDLKnHPYF 257
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
13690-14120 8.59e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.50  E-value: 8.59e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13690 TDSPVEARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEYDGGAEITNYVIELRDKTSIRWDTAMTVRAEDLSATVTDVVE 13769
Cdd:COG3401     122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEP 201
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13770 GQEYSFRVRAQNRIGVGKPSAAtpfVKVADPIERPSPPVNLSASEQTQSSVQLTWEPPLKDGgspILGYIIERQEEGKDN 13849
Cdd:COG3401     202 GTTYYYRVAATDTGGESAPSNE---VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGP 275
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13850 WIRcnMKPVPELTYKVTGLQKGNKYLYRVSAENAAGV-SDPSEIlgpltaddasVEPTMDLSAfkdglevivpnpikilv 13928
Cdd:COG3401     276 FTK--VATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNV----------VSVTTDLTP----------------- 326
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13929 pstgyprpkatwtfgdqvleagdrvkiktisayaeliispserpdkgiytltlenpvksisgeidvnviarPSAPKELKF 14008
Cdd:COG3401     327 -----------------------------------------------------------------------PAAPSGLTA 335
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14009 SDVTKDSVHLTWEPPDDdggSPLTGYVVEKRDMSRKTWTKVMDFVTDLEFTVPDLVQGKEYLFKVCARNKCGPgEPAYTD 14088
Cdd:COG3401     336 TAVGSSSITLSWTASSD---ADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAPSE 411
                           410       420       430
                    ....*....|....*....|....*....|..
gi 1958765569 14089 EPVNMSAPATVPDPPENVKWRDRTANSIFLTW 14120
Cdd:COG3401     412 EVSATTASAASGESLTASVDAVPLTDVAGATA 443
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
31763-32016 9.65e-28

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 118.17  E-value: 9.65e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRcveTSSKKTFmaKFVKVKGTDQvlvKKEISILNIAR------HRNILYLHESFESMEELVMIF 31836
Cdd:cd14010       2 YVLYDEIGRGKHSVVYK---GRRKGTI--EFVAIKCVDK---SKRPEVLNEVRlthelkHPNVLKFYEWYETSNHLWLVV 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQL------ 31910
Cdd:cd14010      74 EYCTGGDLETLLRQDGN-LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLD--GNGTLKLSDFGLARREgeilke 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 -----------KPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTF- 31978
Cdd:cd14010     151 lfgqfsdegnvNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPp 230
                           250       260       270
                    ....*....|....*....|....*....|....*....
gi 1958765569 31979 DEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHP-W 32016
Cdd:cd14010     231 PPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27520-27928 9.72e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.11  E-value: 9.72e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27520 TSRVVWSMVAENLEECIITTTKIIKGNEYIFRVRAVNKYGIGEPleSEPVVAKNSFVTPGPPSIPEVTKITKNSMTVVWN 27599
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27600 RPTVDGgseINGYFLEKRDKKSLAWLKVlkETIRDTRQKVTGLTENSDYQYRVCAVNAAGMGpfSEPSDFYKAADPIDPP 27679
Cdd:COG3401     255 PVTESD---ATGYRVYRSNSGDGPFTKV--ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE--SAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27680 GPPAKIRIADSTKSSITLGWSKPvydGGSDVTGYVVEMRQGEEEEWTIVSTkgEARTTEYVVSNLKPGVNYYFQVSAVNC 27759
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAE--TVTTTSYTDTGLTPGTTYYYKVTAVDA 402
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27760 AGQGEPitMTEPVQAKDILEEPEIDLDvalrTSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSiqNTDSSS 27839
Cdd:COG3401     403 AGNESA--PSEEVSATTASAASGESLT----ASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAV--PFTTTS 474
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27840 LLVIPQVTRNDTGKYILTIENGVGQPKSSTVSVKVLDTPAACQKLQVKHVSLGTVTLLWDPPlidggSPIINYVIEKRDA 27919
Cdd:COG3401     475 STVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPV-----TVGASTGDVLITD 549

                    ....*....
gi 1958765569 27920 TKRTWSIVS 27928
Cdd:COG3401     550 LVSLTTSAS 558
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
31767-32016 1.08e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 117.77  E-value: 1.08e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMA-KFVKVK-----GTDQVLVkkEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd14121       1 EKLGSGTYATVYKAYRKSGAREVVAvKCVSKSslnkaSTENLLT--EIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCS 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLF 31920
Cdd:cd14121      79 GGDLSRFIRSRR-TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHSLR 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 TAPEYYAPEV---HQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEyTFDEEAFQEISLEAMDFIDRL 31997
Cdd:cd14121     158 GSPLYMAPEMilkKKYD---ARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSK-PIEIPTRPELSADCRDLLLRL 233
                           250
                    ....*....|....*....
gi 1958765569 31998 LVKERKSRMTASEALKHPW 32016
Cdd:cd14121     234 LQRDPDRRISFEEFFAHPF 252
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
24832-24913 1.10e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 111.53  E-value: 1.10e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24832 TYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSV 24911
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 24912 IV 24913
Cdd:cd05748      81 KV 82
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
31770-32017 1.12e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 118.17  E-value: 1.12e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31770 GRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK---EISILNIARHRNILylheSFESME---ELVMIF-EFISGL 31842
Cdd:cd06626       9 GEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEiadEMKVLEGLDHPNLV----RYYGVEvhrEEVYIFmEYCQEG 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFE-----RIntsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGD--- 31914
Cdd:cd06626      85 TLEEllrhgRI------LDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLD--SNGLIKLGDFGSAVKLKNNTttm 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 ---NFRLLFTAPEYYAPEVHQHDVVSS---ATDMWSLGTLVYVLLSGINP--FLAETNQQMIENIMNAEYTFDEEafQEI 31986
Cdd:cd06626     157 apgEVNSLVGTPAYMAPEVITGNKGEGhgrAADIWSLGCVVLEMATGKRPwsELDNEWAIMYHVGMGHKPPIPDS--LQL 234
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 31987 SLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06626     235 SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30301-30640 1.25e-27

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.11  E-value: 1.25e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30301 THTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKVVILDKPGPPIGPIKIDEVDATSVTISWEPP-ELDGGAPLSGY 30379
Cdd:COG3401      90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGtTASSVAGAGVV 169
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30380 VVEQRDAHRPGWLPVSESVTRPTFKFT-RLTEGNEYVFRVAATNRFGIGSYlqSEVIECRSSISIPGPPETLQIFDISRD 30458
Cdd:COG3401     170 VSPDTSATAAVATTSLTVTSTTLVDGGgDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPG 247
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30459 GMTLTWYPPEDDGgsqVTGYIIERKEVRADRWVRVNKVpvTMTRYRSTGLIEGLEYEHRVTAINARGTgkPSRPSKP-TV 30537
Cdd:COG3401     248 SVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVvSV 320
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30538 AMDPIaPPGKPQNPRVTDTTRTSVSLAWSVPEDEGgskVTGYLIEMQKVDQREWTKCNTTPTKIrEYTLTHLPQGAEYRF 30617
Cdd:COG3401     321 TTDLT-PPAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTT-SYTDTGLTPGTTYYY 395
                           330       340
                    ....*....|....*....|....
gi 1958765569 30618 RVLACNAGGP-GEPAEVPGTVKVT 30640
Cdd:COG3401     396 KVTAVDAAGNeSAPSEEVSATTAS 419
I-set pfam07679
Immunoglobulin I-set domain;
7107-7196 1.49e-27

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 111.20  E-value: 1.49e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVG 7186
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7187 KDMCSAQLSV 7196
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
20532-21039 1.70e-27

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 124.34  E-value: 1.70e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20532 EDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKVVGKPGIPTGPIKFDEVTAEAMTLKWGP 20611
Cdd:COG3401      91 ATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVV 170
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20612 PKDDGGSEITNYVLEKRDSVNNKWVTcasavqkttfrvTRLHEGIEYTFRVSAENKygVGEGLKSEPIVAKHPFDVPDAP 20691
Cdd:COG3401     171 SPDTSATAAVATTSLTVTSTTLVDGG------------GDIEPGTTYYYRVAATDT--GGESAPSNEVSVTTPTTPPSAP 236
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20692 PPPNIVDVRHDSVSLTWTDPKKTGgspITGYHIEFKERNSLLWKRANKTpiRMKDFKVTGLTEGLEYEFRVMAINLAGVg 20771
Cdd:COG3401     237 TGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGN- 310
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20772 kPSLPSEPVVALDPIDPPGKPEVISVTR---NSVTLIWTEPKYDGghkLTGYIVEKRDLPSKSWMKANHVnVPDCAFTVT 20848
Cdd:COG3401     311 -ESAPSNVVSVTTDLTPPAAPSGLTATAvgsSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAET-VTTTSYTDT 385
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20849 DLVEGGKYEFRIRAKNTAGAISAPSE----STGTIICKDEYEAPTIVLDPTIKDGLTVKAGDSIVLSAISILGKPLPKSS 20924
Cdd:COG3401     386 GLTPGTTYYYKVTAVDAAGNESAPSEevsaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20925 WSKAGKDIRPSDIAQITSTPTSSMLTVKYAT--RKDAGEYTITATNPFGTKEEhVKVSVLDVPGPPGPIEISNVSAEKAT 21002
Cdd:COG3401     466 NAVPFTTTSSTVTATTTDTTTANLSVTTGSLvgGSGASSVTNSVSVIGASAAA-AVGGAPDGTPNVTGASPVTVGASTGD 544
                           490       500       510
                    ....*....|....*....|....*....|....*..
gi 1958765569 21003 LTWTPPLEDGGSPIKAYVLEKRETSRLLWTVVSEDIQ 21039
Cdd:COG3401     545 VLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSL 581
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
17045-17124 2.04e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 110.76  E-value: 2.04e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17045 RIVVHAGGVIRIIAYVSGKPPPTVTWNMNERAL--PQEATIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIV 17122
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 17123 DV 17124
Cdd:cd05748      81 KV 82
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
31761-32017 2.11e-27

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 116.98  E-value: 2.11e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLvKKEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd06612       3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEI-IKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCG 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 G---LDIFERINTSafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLkpGDNFR 31917
Cdd:cd06612      82 AgsvSDIMKITNKT---LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQ--AKLADFGVSGQL--TDTMA 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFT---APEYYAPEVHQHDVVSSATDMWSLGTLVYVL------LSGINPFLAetnQQMIENimNAEYTFDEEafQEISL 31988
Cdd:cd06612     155 KRNTvigTPFWMAPEVIQEIGYNNKADIWSLGITAIEMaegkppYSDIHPMRA---IFMIPN--KPPPTLSDP--EKWSP 227
                           250       260
                    ....*....|....*....|....*....
gi 1958765569 31989 EAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06612     228 EFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25356-25768 2.58e-27

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 123.96  E-value: 2.58e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25356 TSRLSWTQVSTEVQALNYKVTKLLPGNEYIFRVMAVNKYGVGEPleSEPVIACNPYKLPGPPSTPEASAITKDSMVLTWT 25435
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25436 rPVDDGGAeiEGYILEKRDKEGIRWTKCNkkTLTDLRFRVTGLTEGHSYEFRVAAENAAgvGEPSEPSVFYRACDALYPP 25515
Cdd:COG3401     255 -PVTESDA--TGYRVYRSNSGDGPFTKVA--TVTTTSYTDTGLTNGTTYYYRVTAVDAA--GNESAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25516 GPPSNPKVTDTSRSSVSLAWNKPiydGGAPVRGYVIELKEAAADEWTTCTppSGLQGKQFTVTKLKENTEYNFRICAFNT 25595
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ETVTTTSYTDTGLTPGTTYYYKVTAVDA 402
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25596 EGVGEPATIPGSVVAQermEAPEIELDADLRKVVTLRASATLRLFVTIKGRPEPEVKWEKAEGILTERAQIEVTSSYTML 25675
Cdd:COG3401     403 AGNESAPSEEVSATTA---SAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA 479
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25676 VIDNVTRFDSGRYNLTLENNSGSKTAFVNVRVLDSPSAPVNLTVREvkKDSVTLSWEPPLIDGGAKVTNYIVEKRETTRK 25755
Cdd:COG3401     480 TTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPD--GTPNVTGASPVTVGASTGDVLITDLVSLTTSA 557
                           410
                    ....*....|...
gi 1958765569 25756 AYATITNNCTKTT 25768
Cdd:COG3401     558 SSSVSGAGLGSGN 570
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26707-26786 2.60e-27

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 110.37  E-value: 2.60e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26707 TLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDL--RTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTFVV 26784
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 26785 KV 26786
Cdd:cd05748      81 KV 82
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
31759-32017 4.66e-27

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 115.82  E-value: 4.66e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQ---VLVKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd14161       1 LKHRYEFLETLGKGTYGRVKKARDSSGRLVAIKSIRKDRIKDEqdlLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDN 31915
Cdd:cd14161      81 MEYASRGDLYDYISERQ-RLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN--IKIADFGLSNLYNQDKF 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPE-VHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFqeislEAMDFI 31994
Cdd:cd14161     158 LQTYCGSPLYASPEiVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-----DACGLI 232
                           250       260
                    ....*....|....*....|...
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14161     233 RWLLMVNPERRATLEDVASHWWV 255
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
31761-32017 5.82e-27

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 115.73  E-value: 5.82e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV----LVKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd14186       1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAgmvqRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK-PGDN 31915
Cdd:cd14186      81 EMCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN--IKIADFGLATQLKmPHEK 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYtfdeEAFQEISLEAMDFID 31995
Cdd:cd14186     159 HFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADY----EMPAFLSREAQDLIH 234
                           250       260
                    ....*....|....*....|..
gi 1958765569 31996 RLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14186     235 QLLRKNPADRLSLSSVLDHPFM 256
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26437-26819 6.68e-27

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 122.80  E-value: 6.68e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26437 TSRLAWTICEAELRTTSCKVTKLLKGNEYIFRVTGVNKYGVGEPleSVAVKALDPFTTPSPPTSLEITSVTKDSMTLCWS 26516
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26517 RPEtdgGSDISGYIIERREKNSLRWMRVNKkpVYDLRVKSTGLREGCEYEYRVFAENAAGLslPSDTSPLVRAEDPVFLP 26596
Cdd:COG3401     255 PVT---ESDATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPP 327
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26597 SPPSKPKIVDSGKTTITIGWVKPLfdgGAPITGYTVEYKKSEETDWKVAIQSFRGTEYTMSGLTTGAEYVFRVRSLNKVG 26676
Cdd:COG3401     328 AAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26677 -ASDPSDITDPQVAkereeePAFDVDSEMRKTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRTSLT 26755
Cdd:COG3401     405 nESAPSEEVSATTA------SAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT 478
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 26756 IENANRNDSGKYTLTIQNVLSAASMTFVVKVLDSPGPPANITVREVTKETAVLSWDVPENDGGA 26819
Cdd:COG3401     479 ATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAST 542
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26997-27078 1.07e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 108.45  E-value: 1.07e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26997 TVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTFINI 27076
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 27077 IV 27078
Cdd:cd05748      81 KV 82
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
31762-32005 1.22e-26

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 115.12  E-value: 1.22e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV-LVKKEISIL-NIARHRNIL-YLHESFESME---ELVMI 31835
Cdd:cd13985       1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLrVAIKEIEIMkRLCGHPNIVqYYDSAILSSEgrkEVLLL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGlDIFERINTSA-FELNEREVVSYVRQVCEALEFLHSQN--IGHFDIRPENIIYQTRKNsiIKIIEFG----QAR 31908
Cdd:cd13985      81 MEYCPG-SLVDILEKSPpSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR--FKLCDFGsattEHY 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31909 QLKPGDNFRLL------FTAPEYYAPE---VHQHDVVSSATDMWSLGTLVYVLLSGINPFlaETNQQMieNIMNAEYTFD 31979
Cdd:cd13985     158 PLERAEEVNIIeeeiqkNTTPMYRAPEmidLYSKKPIGEKADIWALGCLLYKLCFFKLPF--DESSKL--AIVAGKYSIP 233
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31980 EEAFQeiSLEAMDFIDRLLVKERKSR 32005
Cdd:cd13985     234 EQPRY--SPELHDLIRHMLTPDPAER 257
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
31762-32015 1.42e-26

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 115.68  E-value: 1.42e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTfmakfVKVKgtdQVLVKK-----EISILNIARHRNILYLHESFESMEE----- 31831
Cdd:cd14137       5 SYTIEKVIGSGSFGVVYQAKLLETGEV-----VAIK---KVLQDKryknrELQIMRRLKHPNIVKLKYFFYSSGEkkdev 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 -LVMIFEFISgLDIFERI-----NTSAFELNEREVVSYvrQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsIIKIIEFG 31905
Cdd:cd14137      77 yLNLVMEYMP-ETLYRVIrhyskNKQTIPIIYVKLYSY--QLFRGLAYLHSLGICHRDIKPQNLLVDPETG-VLKLCDFG 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31906 QARQLKPGD---------NFR---LLFTAPEYyapevhqhdvvSSATDMWSLGTLVYVLLSGINPFLAETNQ-QMIENI- 31971
Cdd:cd14137     153 SAKRLVPGEpnvsyicsrYYRapeLIFGATDY-----------TTAIDIWSAGCVLAELLLGQPLFPGESSVdQLVEIIk 221
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31972 ------------MNAEYTFD----------EEAFQE-ISLEAMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd14137     222 vlgtptreqikaMNPNYTEFkfpqikphpwEKVFPKrTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
I-set pfam07679
Immunoglobulin I-set domain;
8989-9078 1.69e-26

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 108.50  E-value: 1.69e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVG 9068
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  9069 KDSCTAQLNI 9078
Cdd:pfam07679    81 EAEASAELTV 90
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
31761-31978 1.79e-26

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 115.19  E-value: 1.79e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKF------VKVKGTDQVLVKKEIsiLNIARHRNILYLHESFESMEELVM 31834
Cdd:cd14209       1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKIldkqkvVKLKQVEHTLNEKRI--LQAINFPFLVKLEYSFKDNSNLYM 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKpGD 31914
Cdd:cd14209      79 VMEYVPGGEMFSHLRRIG-RFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLID--QQGYIKVTDFGFAKRVK-GR 154
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31915 NFRLLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTF 31978
Cdd:cd14209     155 TWTLCGT-PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF 217
I-set pfam07679
Immunoglobulin I-set domain;
8797-8886 2.09e-26

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 108.11  E-value: 2.09e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVG 8876
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8877 EVSSSTFLTV 8886
Cdd:pfam07679    81 EAEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3199-3289 3.64e-26

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 107.51  E-value: 3.64e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLL---STGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKN 3275
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  3276 DYGVATTSASLSVE 3289
Cdd:cd20951      81 IHGEASSSASVVVE 94
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
31763-32017 3.93e-26

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 113.26  E-value: 3.93e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK---EISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14071       2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKiyrEVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd14071      82 SNGEIFDYL-AQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMN--IKIADFGFSNFFKPGELLKTW 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYYAPEVHQ-HDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYT---FdeeafqeISLEAMDFID 31995
Cdd:cd14071     159 CGSPPYAAPEVFEgKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRipfF-------MSTDCEHLIR 231
                           250       260
                    ....*....|....*....|..
gi 1958765569 31996 RLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14071     232 RMLVLDPSKRLTIEQIKKHKWM 253
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
31769-32018 3.99e-26

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 114.45  E-value: 3.99e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTF------MAKFVKVKGTDQVlvKKEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05612       9 IGTGTFGRVHLVRDRISEHYYalkvmaIPEVIRLKQEQHV--HNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGG 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKpgDNFRLLFTA 31922
Cdd:cd05612      87 ELFSYLRNSG-RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLD--KEGHIKLTDFGFAKKLR--DRTWTLCGT 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLLVKER 32002
Cdd:cd05612     162 PEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFP----RHLDLYAKDLIKKLLVVDR 237
                           250       260
                    ....*....|....*....|.
gi 1958765569 32003 KSRM-----TASEALKHPWLK 32018
Cdd:cd05612     238 TRRLgnmknGADDVKNHRWFK 258
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
16331-16420 4.86e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.91  E-value: 4.86e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16331 CLICKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKamkdgihdIPEDAQLETAENSSVIVIPECTRAHSGKYSITAKNKAG 16410
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLK--------ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG 72
                            90
                    ....*....|
gi 1958765569 16411 QKTANCRVKV 16420
Cdd:cd05748      73 EKSATINVKV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
25628-25707 5.68e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.52  E-value: 5.68e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25628 VVTLRASATLRLFVTIKGRPEPEVKWEKAEGIL--TERAQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVNV 25705
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 25706 RV 25707
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
19128-19207 6.13e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.52  E-value: 6.13e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVR-KGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVK 19206
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19207 V 19207
Cdd:cd05748      82 V 82
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
31769-32015 6.81e-26

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 112.46  E-value: 6.81e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIV----HRcvetssKKTFMAKFVKV-----KGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14120       1 IGHGAFAVVfkgrHR------KKPDLPVAIKCitkknLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYC 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENII--YQTRKNS-----IIKIIEFGQARQLKP 31912
Cdd:cd14120      75 NGGDLADYLQAKG-TLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILlsHNSGRKPspndiRLKIADFGFARFLQD 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 GDNFRLLFTAPEYYAPEV---HQHDVVSsatDMWSLGTLVYVLLSGINPFLAETNQQMiENIMNAEYTFDEEAFQEISLE 31989
Cdd:cd14120     154 GMMAATLCGSPMYMAPEVimsLQYDAKA---DLWSIGTIVYQCLTGKAPFQAQTPQEL-KAFYEKNANLRPNIPSGTSPA 229
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31990 AMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd14120     230 LKDLLLGLLKRNPKDRIDFEDFFSHP 255
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
22381-22460 6.89e-26

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 106.13  E-value: 6.89e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22381 VVTIRACCTLRLFVPIKGRPAPEVKWAREHGESLD--KASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFVNV 22458
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtgRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22459 RV 22460
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
7294-7382 7.92e-26

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 106.57  E-value: 7.92e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVG 7373
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  7374 SDTCACTVK 7382
Cdd:pfam07679    81 EAEASAELT 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22109-22355 9.09e-26

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 118.95  E-value: 9.09e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22109 TSRLAWTNVATEVQVTKLKVTKLLKGNEYIFRVMAVNKYGVGEPleSEPVLAVDPYGPPDPPKNPEVTTITKDSMVVCWg 22188
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW- 253
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22189 hpDSDGGSEIINYIVERRDKAGQRWVKCNkkALTDLRFKVSGLTEGHEYEFRIMAENAAGV-SAPSATSPFYKacdSVFK 22267
Cdd:COG3401     254 --DPVTESDATGYRVYRSNSGDGPFTKVA--TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTT---DLTP 326
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22268 PGPPGNPRVLDTSRSSISIAWNKPiydGGSEITGYMVEIALPEEDEWQVVTPPagLKATSYTITNLIENQEYKIRIYAMN 22347
Cdd:COG3401     327 PAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET--VTTTSYTDTGLTPGTTYYYKVTAVD 401

                    ....*...
gi 1958765569 22348 SEGLGEPA 22355
Cdd:COG3401     402 AAGNESAP 409
I-set pfam07679
Immunoglobulin I-set domain;
6-97 1.26e-25

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 105.80  E-value: 1.26e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTStlPGVQISFSDGRARLMIPAVTKANSGRYSLRATNG 85
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS--DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                            90
                    ....*....|..
gi 1958765569    86 SGQATSTAELLV 97
Cdd:pfam07679    79 AGEAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
30658-30736 1.58e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 105.36  E-value: 1.58e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30658 VFVRQGGVIRLTIPIKGKPFPICKWTKEGQDV--SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVK 30735
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 30736 V 30736
Cdd:cd05748      82 V 82
I-set pfam07679
Immunoglobulin I-set domain;
33074-33162 1.63e-25

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 105.42  E-value: 1.63e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33074 RILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGK 33153
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569 33154 QEAQFTLTV 33162
Cdd:pfam07679    82 AEASAELTV 90
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
31765-32032 1.84e-25

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 112.14  E-value: 1.84e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV---LVkkEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd06611       9 IIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELedfMV--EIDILSECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 ------LDIFERIntsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSIiKIIEFGQARQLKPGDN 31915
Cdd:cd06611      87 galdsiMLELERG------LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILL-TLDGDV-KLADFGVSAKNKSTLQ 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFT------APEYYAPEVHQHDVVSSATDMWSLG-TLVYvlLSGINPFLAETN-QQMIENIMNAEY-TFDEEafQEI 31986
Cdd:cd06611     159 KRDTFIgtpywmAPEVVACETFKDNPYDYKADIWSLGiTLIE--LAQMEPPHHELNpMRVLLKILKSEPpTLDQP--SKW 234
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569 31987 SLEAMDFIDRLLVKERKSRMTASEALKHPWLKQRMDRvstKVIRTL 32032
Cdd:cd06611     235 SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDN---KAIKDL 277
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
21651-21963 2.12e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.80  E-value: 2.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21651 TAKNTVGEVGDVITIQVHDIPGPPTGPIKFDEVSSDFVTFSWEPPENDGGVPISNYVVEMR--QTDSTTWVELATTVIRT 21728
Cdd:COG3401     113 SSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDtsATAAVATTSLTVTSTTL 192
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21729 TYKATRLTTGVEYQFRVKAQNryGVGPGITSASVVANYPFKVPGPPGTPQVTAVTKDSMTISWHEPLSDGgspILGYHIE 21808
Cdd:COG3401     193 VDGGGDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVY 267
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21809 RKERNGILWQTVSKalVPGNIFKSTGLTDGIAYEFRVIAENMAGKskPSKPSEPTFALDPIDPPGKPVPLNITRHT---V 21885
Cdd:COG3401     268 RSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGsssI 343
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 21886 ALKWAKPEYTGgfkITSYVVEKRDLPNGRWLKANfSNILENEFTVSGLTEDAAYEFRVIAKNAAGAISPPSEPSDAIT 21963
Cdd:COG3401     344 TLSWTASSDAD---VTGYNVYRSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATT 417
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29708-30085 2.89e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.41  E-value: 2.89e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29708 TLSYVVTRLIKNNEYTFRVRAVNKYGLGVPieSEPIVARNSFTIPSQPGIPEGVGAGKEHIIIQWTKPESDGgneISNYL 29787
Cdd:COG3401     191 TLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYR 265
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29788 VDKREKKSLRWTRVNKdyvVYDTRLKVTSLMEGCDYQFRVTAVNSAGNsePSEASNFISCREPSYTPGPPSAPRVVDTTK 29867
Cdd:COG3401     266 VYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGS 340
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29868 SSISLAWTKPMydgGTDIIGYVLEMQEKDTDQWCRVHTntTIRNNEFTVPDLKMGQKYSFRVAAVNAKGmsDYSETTAEI 29947
Cdd:COG3401     341 SSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAE--TVTTTSYTDTGLTPGTTYYYKVTAVDAAG--NESAPSEEV 413
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29948 EpVERLEIPDLELADDLKKTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDKVNRYDAGKY 30027
Cdd:COG3401     414 S-ATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVT 492
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 30028 TIEAENQSGKKSATVLVKVYDTPGPCPSVNVKEVSRDSVTITWEIPTIDGGAPVNNYI 30085
Cdd:COG3401     493 TGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDL 550
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
23064-23145 3.08e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 104.59  E-value: 3.08e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23064 TVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNV 23143
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 23144 KV 23145
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24957-25592 3.51e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.41  E-value: 3.51e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24957 RDTTTTNWQMVSATVARTTIKVSKLKTGTEYQFRIFAENRYGKSTPLDSKPVVVQYPFKEPGPPGTPFVTS--VSKDQML 25034
Cdd:COG3401      73 AGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALgaGLYGVDG 152
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25035 VQWHEPVNDGGSKVIGYHLEQKEKNSILWVKLNKIPIQDTKFKTTGLDEGLEYEFRVSAENIVGIGKPSKVSECYVARDP 25114
Cdd:COG3401     153 ANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP 232
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25115 CDPPGRPEAIIITRNSVTLKWKKPTYDGgskITGYIVEKKDLPDGRWMKASFTNvvETEFTVTGLVEDQRYEFRVIARNA 25194
Cdd:COG3401     233 PSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTYYYRVTAVDA 307
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25195 ADNFSEPSEssgaitardeidapnasldpkyrdviivragetfvleadirgkpipdivwskdgneleetaarmeikstlq 25274
Cdd:COG3401     308 AGNESAPSN----------------------------------------------------------------------- 316
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25275 ktTLTVKdcirtdggqytlklsnvggTKTIPitvkvldrPGPPEGpLKVTGVTAEKCYLAWNPPLqdgGASISHYIIEKR 25354
Cdd:COG3401     317 --VVSVT-------------------TDLTP--------PAAPSG-LTATAVGSSSITLSWTASS---DADVTGYNVYRS 363
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25355 ETSRLSWTQVSTEVQALNYKVTKLLPGNEYIFRVMAVNKYGVG----EPLESEPVIACNPYKLPGPPSTPEASAITKDSM 25430
Cdd:COG3401     364 TSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNEsapsEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25431 VLTWTRPVDDGGAEIEGYILEKRDKEGIRWTKCNKKTLTDLRFRVTGLTEGHSYEFRVAAENaagVGEPSEPSVFYRACD 25510
Cdd:COG3401     444 AASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSV---TNSVSVIGASAAAAV 520
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25511 ALYPPGPPSnpkVTDTSRSSVSLAWNKPIYDGGAPVRGYVIElkeaaaDEWTTCTPPSGLQGKQFTVTKLKENTEYNFRI 25590
Cdd:COG3401     521 GGAPDGTPN---VTGASPVTVGASTGDVLITDLVSLTTSASS------SVSGAGLGSGNLYLITTLGGSLLTTTSTNTND 591

                    ..
gi 1958765569 25591 CA 25592
Cdd:COG3401     592 VA 593
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
31763-32017 3.55e-25

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 111.09  E-value: 3.55e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSK-----KTFMAKFvkvKGTDQVLVKKEI-SILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd07830       1 YKVIKQLGDGTFGSVYLARNKETGelvaiKKMKKKF---YSWEECMNLREVkSLRKLNEHPNIVKLKEVFRENDELYFVF 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGlDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPgdn 31915
Cdd:cd07830      78 EYMEG-NLYQLMKDRKGKpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLL--VSGPEVVKIADFGLAREIRS--- 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 fRLLFTapEY-----Y-APEVH-QHDVVSSATDMWSLGTL---VYV---LLSGINpflaETNQ--QMIE----------- 31969
Cdd:cd07830     152 -RPPYT--DYvstrwYrAPEILlRSTSYSSPVDIWALGCImaeLYTlrpLFPGSS----EIDQlyKICSvlgtptkqdwp 224
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31970 ------NIMNaeYTFDEEA-------FQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07830     225 egyklaSKLG--FRFPQFAptslhqlIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
14495-15023 4.26e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.03  E-value: 4.26e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14495 PPWPPGKPTVKDIGKTSLVLNWTKPEHDGGAKIESYVIEMLKTGTDDWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNK 14574
Cdd:COG3401      32 SGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGL 111
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14575 AGESEPSEPSDPVLCREKLYPPSPP------RWLEVINITKNTADLKWTVPEKDGGSPITNYIVEKRDVRRKGWQTVDTT 14648
Cdd:COG3401     112 TSSDEVPSPAVGTATTATAVAGGAAtagtyaLGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTT 191
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14649 VKDTKCTVTPlteGSLYVFRVAAENAIGQSDYteiGDSVLAKDTFTTPGPPYALTVVDVTKRHVDLKWEPPKNDGgrpIQ 14728
Cdd:COG3401     192 LVDGGGDIEP---GTTYYYRVAATDTGGESAP---SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---AT 262
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14729 RYIIEKKEKLGTRWVKAGKTSGPdcNFRVTDVIEGTEVQFQVRAENEAGVghPSEPTEILSIEDPVGPPSPPLDLHVTDA 14808
Cdd:COG3401     263 GYRVYRSNSGDGPFTKVATVTTT--SYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAV 338
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14809 GRKHIAIAWKPPEkngGSPIIGYHVEMCPVGTEKWMRVNSrPIKDLKFKVeEGVVPDKEYVLRVRAVNAVG----VSDPS 14884
Cdd:COG3401     339 GSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAE-TVTTTSYTD-TGLTPGTTYYYKVTAVDAAGnesaPSEEV 413
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14885 EISENVVAKDPDCKPTIDLETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHA 14964
Cdd:COG3401     414 SATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTT 493
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 14965 DAGVYTITLE------NKLGSATASINVKVIGLPGPCKDIKASDITKSSCKLTWEPPEFDGGSPI 15023
Cdd:COG3401     494 GSLVGGSGASsvtnsvSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSAS 558
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
31767-31973 4.29e-25

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 110.31  E-value: 4.29e-25
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31767 EDLGRGEFGIVHRCVetsskktfmAKFVKVKGTDQVLVK---------------KEISILNIARHRNILYLHESFESMEE 31831
Cdd:smart00219     5 KKLGEGAFGEVYKGK---------LKGKGGKKKVEVAVKtlkedaseqqieeflREARIMRKLDHPNVVKLLGVCTEEEP 75
                             90       100       110       120       130       140       150       160
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31832 LVMIFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLK 31911
Cdd:smart00219    76 LYIVMEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG--ENLVVKISDFGLSRDLY 153
                            170       180       190       200       210       220
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  31912 PGDNFRLLFT-AP-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIMN 31973
Cdd:smart00219   154 DDDYYRKRGGkLPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKN 218
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27044-27758 4.74e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 117.03  E-value: 4.74e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27044 LTINLKESVTADAGKYEITAANSSGTTKTFINIIVLDRPGPPTGPVAISDITEESVTLKWEPPKYDGGSHVTNYIVLkre 27123
Cdd:COG3401       9 LDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVA--- 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27124 tsTAVWTEVSATvARTMIKVMKLTTGEEYQFRIKAENRFGISDHIDSACVVVKLPYTTPGPPSTPWVSNVTRESITVGW- 27202
Cdd:COG3401      86 --AAPPTATGLT-TLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASs 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27203 HEPVSNGGSAVIGYHLEMKDRNSILWQKANKMIirtthfkVTTISAGLIYEFRVYAENAAGIGKPSHSSEPVLAIDACEP 27282
Cdd:COG3401     163 VAGAGVVVSPDTSATAAVATTSLTVTSTTLVDG-------GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSA 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27283 PRNVRITDISKNSVNLSWQQPAFDGgskITGYIVERRDLPDGRWTKASFTNviETQFTVSGLTQNSQYEFRVFARNAVGS 27362
Cdd:COG3401     236 PTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGN 310
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27363 VSNPSEVVgpitcidsyggpvidlpleytevvkyragtsvklragiSGKPEPTiewykddkelqtnalvcvenstdlasi 27442
Cdd:COG3401     311 ESAPSNVV--------------------------------------SVTTDLT--------------------------- 325
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27443 likdanrlnsgsyelklrnamgsasatirvqildKPGPPGGpIEFKTVTAEKITLLWRPPADdggAKITHYIVEKRETSR 27522
Cdd:COG3401     326 ----------------------------------PPAAPSG-LTATAVGSSSITLSWTASSD---ADVTGYNVYRSTSGG 367
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27523 VVWSMVAENLEECIITTTKIIKGNEYIFRVRAVNKYGIgEPLESEPVVAKNSFVTPGPPSI------PEVTKITKNSMTV 27596
Cdd:COG3401     368 GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAPSEEVSATTASAASGESLTasvdavPLTDVAGATAAAS 446
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27597 VWNRPTVDGGSEINGYFLEKRDKkslawlkvlkeTIRDTRQKVTGLTENSDYQYRVCAVNAAGMGPFSEPSDFYKAADPI 27676
Cdd:COG3401     447 AASNPGVSAAVLADGGDTGNAVP-----------FTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGAS 515
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27677 DPPGPPAKIRIADSTKSSITLGWSKPVYDGGSDVTGYVVEMrQGEEEEWTIVSTKGEARTTEYVVSNLKPGVNYYFQVSA 27756
Cdd:COG3401     516 AAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTS-ASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAG 594

                    ..
gi 1958765569 27757 VN 27758
Cdd:COG3401     595 VH 596
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
31769-32018 4.75e-25

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 112.11  E-value: 4.75e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSK---KTFMAKFVKvKGT------DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05584       4 LGKGGYGKVFQVRKTTGSdkgKIFAMKVLK-KASivrnqkDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEYL 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAFELnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd05584      83 SGGELFMHLEREGIFM-EDTACFYLAEITLALGHLHSLGIIYRDLKPENILLD--AQGHVKLTDFGLCKESIHDGTVTHT 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAP-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLL 31998
Cdd:cd05584     160 FCGTiEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLP----PYLTNEARDLLKKLL 235
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31999 VKERKSRMTA----SEALK-HPWLK 32018
Cdd:cd05584     236 KRNVSSRLGSgpgdAEEIKaHPFFR 260
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
31769-32017 6.08e-25

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 110.10  E-value: 6.08e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIV----HR-------CVETSSKKTfMAKfvkvkgtDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14202      10 IGHGAFAVVfkgrHKekhdlevAVKCINKKN-LAK-------SQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVME 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY------QTRKNSI-IKIIEFGQARQL 31910
Cdd:cd14202      82 YCNGGDLADYLHTMR-TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysggrKSNPNNIrIKIADFGFARYL 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMiENIMNAEYTFDEEAFQEISLEA 31990
Cdd:cd14202     161 QNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDL-RLFYEKNKSLSPNIPRETSSHL 239
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14202     240 RQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
31769-32018 6.13e-25

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 111.54  E-value: 6.13e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGivhrcvetsskKTFMAKFvkvKGTDQV----LVKKEI--------------SILNIARHRNIL-YLHESFESM 31829
Cdd:cd05570       3 LGKGSFG-----------KVMLAER---KKTDELyaikVLKKEViiedddvectmtekRVLALANRHPFLtGLHACFQTE 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ 31909
Cdd:cd05570      69 DRLYFVMEYVNGGDLMFHIQRAR-RFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGH--IKIADFGMCKE 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 -LKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISL 31988
Cdd:cd05570     146 gIWGGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYP----RWLSR 221
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 31989 EAMDFIDRLLVKERKSRM-----TASEALKHPWLK 32018
Cdd:cd05570     222 EAVSILKGLLTKDPARRLgcgpkGEADIKAHPFFR 256
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
31769-32018 6.43e-25

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 109.84  E-value: 6.43e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKV-KGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG---LDI 31844
Cdd:cd06648      15 IGEGSTGIVCIATDKSTGRQVAVKKMDLrKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGgalTDI 94
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 ferinTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQL-KPGDNFRLLFTAP 31923
Cdd:cd06648      95 -----VTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLT--SDGRVKLSDFGFCAQVsKEVPRRKSLVGTP 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31924 EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQeISLEAMDFIDRLLVKERK 32003
Cdd:cd06648     168 YWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHK-VSPRLRSFLDRMLVRDPA 246
                           250
                    ....*....|....*
gi 1958765569 32004 SRMTASEALKHPWLK 32018
Cdd:cd06648     247 QRATAAELLNHPFLA 261
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
27393-27474 6.51e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 103.44  E-value: 6.51e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27393 VVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRV 27472
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 27473 QI 27474
Cdd:cd05748      81 KV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
30259-30340 6.64e-25

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 103.44  E-value: 6.64e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30259 TIHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKV 30338
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 30339 VI 30340
Cdd:cd05748      81 KV 82
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
31761-32017 7.07e-25

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 110.48  E-value: 7.07e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVEtssKKTFM----AKFVKVKGTDQV--LVKKEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd07833       1 NKYEVLGVVGEGAYGVVLKCRN---KATGEivaiKKFKESEDDEDVkkTALREVKVLRQLRHENIVNLKEAFRRKGRLYL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFIsGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd07833      78 VFEYV-ERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENIL--VSESGVLKLCDFGFARALTARP 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLL-FTAPEYY-APEVHQHDV-VSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNA--------EYTFDE--- 31980
Cdd:cd07833     155 ASPLTdYVATRWYrAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKClgplppshQELFSSnpr 234
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31981 ---EAF----QEISLE----------AMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07833     235 fagVAFpepsQPESLErrypgkvsspALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
31769-32017 7.70e-25

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 109.80  E-value: 7.70e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL------VKKEISILNIARHRNILYLHESfESMEELVMIF-EFISG 31841
Cdd:cd06632       8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSresvkqLEQEIALLSKLRHPNIVQYYGT-EREEDNLYIFlEYVPG 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINT-SAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFRLLF 31920
Cdd:cd06632      87 GSIHKLLQRyGAFE--EPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDT--NGVVKLADFGMAKHVEAFSFAKSFK 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 TAPEYYAPEV--HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTfdEEAFQEISLEAMDFIDRLL 31998
Cdd:cd06632     163 GSPYWMAPEVimQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGEL--PPIPDHLSPDAKDFIRLCL 240
                           250
                    ....*....|....*....
gi 1958765569 31999 VKERKSRMTASEALKHPWL 32017
Cdd:cd06632     241 QRDPEDRPTASQLLEHPFV 259
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22729-23136 8.55e-25

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 8.55e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22729 HYTVKLTNSAGEATETLNVIVLDK---PGPPTGpVKMDEVTADSVTLSWEPPKydgGSSINNYIVEKRDTSTTAWQIVsA 22805
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVTTPttpPSAPTG-LTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKV-A 280
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22806 TVARTTIKASRLKTGCEYQFRIAAENRYG-KSTYlnSEPVIAQYPFKVPGPPGTPFVTLASKDSMEVQWhEPVSDGGsrV 22884
Cdd:COG3401     281 TVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP--SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--V 355
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22885 IGYHLERKERNSILWVKLNKTpIPQTKFKTTGLEEGIEYEFRVSAENIVGIGkpSKPSECYAAH--DPCDPPGRPEAIIV 22962
Cdd:COG3401     356 TGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATtaSAASGESLTASVDA 432
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22963 TRNSVTLQWKKPTYDGGSKITGYVVEKKELPDGRWmkasfTNIIDTQFEVTGLIEDHRYEFRVIARNAAGVFSEPSESTG 23042
Cdd:COG3401     433 VPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA-----VPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23043 AITARDEVEPPrISMDPKYKDTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVD 23122
Cdd:COG3401     508 SVSVIGASAAA-AVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTS 586
                           410
                    ....*....|....
gi 1958765569 23123 SGNYILKAKNVAGE 23136
Cdd:COG3401     587 TNTNDVAGVHGGTL 600
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17444-17715 1.00e-24

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 1.00e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17444 SWKPPLDDGGSEITNYIIEKKELGKDIWMPVTSASAKTTCKV---------PKLLEGKDYIFRIHAENLYGISDPlvSDS 17514
Cdd:COG3401     146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVtsttlvdggGDIEPGTTYYYRVAATDTGGESAP--SNE 223
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17515 MKARDRFRVPDAPEQPVVTEVTKDSALVTWNKPNDGGkpITNYILEKRETMSKRWVRVTKEPihpYTKYRVPDLLEGCQY 17594
Cdd:COG3401     224 VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSGDGPFTKVATVT---TTSYTDTGLTNGTTY 298
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17595 EFRVSAENEIGIgdPSPPSKPVFARDPIAKPSPPINPEAIDTTCNSVDLTWQPPrhdGGSKILGYIVEYQKVGDEEWRRA 17674
Cdd:COG3401     299 YYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKI 373
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 17675 NHTPEscpETKYKVTGLRDGQTYKFRVLAVNEAG-ESDPAHV 17715
Cdd:COG3401     374 AETVT---TTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEE 412
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24787-25210 1.03e-24

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 115.87  E-value: 1.03e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24787 LSSGQEYQFRVKAYNEKGKSDPRVLGVPVIAKDLTIQPSFKLPFNTYSVQAGeDLKIEIPVIGRPRPKISWVKDGEPLRQ 24866
Cdd:COG3401       6 LTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLV-AAGLSSGGGLGTGGRAGTTSGVAAVAV 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24867 TTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVIVLEKPGPPVGPVKFDEVSADFVVISWEPPAYTGG 24946
Cdd:COG3401      85 AAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVA 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24947 C-QISNYIVEKRDTTTTNWQMVSATVArTTIKVSKLKTGTEYQFRIFAENRYGKSTPldSKPVVVQYPFKEPGPPGTPFV 25025
Cdd:COG3401     165 GaGVVVSPDTSATAAVATTSLTVTSTT-LVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTA 241
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25026 TSVSKDQMLVQWhEPVNDGGskVIGYHLEQKEKNSILWVKLNKIpiQDTKFKTTGLDEGLEYEFRVSAENIVGI-GKPSK 25104
Cdd:COG3401     242 TADTPGSVTLSW-DPVTESD--ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSN 316
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25105 VSECYVARDPCDPPGRPEAIIITRNSVTLKWKKPTydgGSKITGYIVEKKDLPDGRWMKASFTnVVETEFTVTGLVEDQR 25184
Cdd:COG3401     317 VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTT 392
                           410       420
                    ....*....|....*....|....*.
gi 1958765569 25185 YEFRVIARNAADNFSEPSESSGAITA 25210
Cdd:COG3401     393 YYYKVTAVDAAGNESAPSEEVSATTA 418
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
31769-32018 1.08e-24

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 110.79  E-value: 1.08e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTF---------MAKFVKVKgtdQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05574       9 LGKGDVGRVYLVRLKGTGKLFamkvldkeeMIKRNKVK---RVLTEREI--LATLDHPFLPTLYASFQTSTHLCFVMDYC 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIF---ERINTSAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQ-----------------TRKNSII 31899
Cdd:cd05574      84 PGGELFrllQKQPGKRLP--EEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHesghimltdfdlskqssVTPPPVR 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31900 KIIEFGQAR-QLKPGDNFRLLFTAP----------EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMI 31968
Cdd:cd05574     162 KSLRKGSRRsSVKSIEKETFVAEPSarsnsfvgteEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETF 241
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31969 ENIMNAEYTFDEEAfqEISLEAMDFIDRLLVKERKSRM----TASEALKHPWLK 32018
Cdd:cd05574     242 SNILKKELTFPESP--PVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFR 293
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
31769-32015 1.22e-24

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 109.02  E-value: 1.22e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd08530       8 LGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREdsvNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPFGDLS 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSAFE---LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGdnfrLLFT- 31921
Cdd:cd08530      88 KLISKRKKKrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLS--AGDLVKIGDLGISKVLKKN----LAKTq 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 --APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFqeiSLEAMDFIDRLLV 31999
Cdd:cd08530     162 igTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVY---SQDLQQIIRSLLQ 238
                           250
                    ....*....|....*.
gi 1958765569 32000 KERKSRMTASEALKHP 32015
Cdd:cd08530     239 VNPKKRPSCDKLLQSP 254
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
31762-32013 1.36e-24

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 108.98  E-value: 1.36e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK--------KEISI-LNIARHRNILYLHESFESMEEL 31832
Cdd:cd13993       1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNdfqklpqlREIDLhRRVSRHPNIITLHDVFETEVAI 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31833 VMIFEFISGLDIFERINTSAFELNEREVVSYV-RQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiIKIIEFGQARQLK 31911
Cdd:cd13993      81 YIVLEYCPNGDLFEAITENRIYVGKTELIKNVfLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT-VKLCDFGLATTEK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFRllfTAPEYY-APEVHQHDVVSSAT------DMWSLGTLVYVLLSGINPFLAETNQqmiENIMNAEYTFDEEAFQ 31984
Cdd:cd13993     160 ISMDFG---VGSEFYmAPECFDEVGRSLKGypcaagDIWSLGIILLNLTFGRNPWKIASES---DPIFYDYYLNSPNLFD 233
                           250       260       270
                    ....*....|....*....|....*....|..
gi 1958765569 31985 EI---SLEAMDFIDRLLVKERKSRMTASEALK 32013
Cdd:cd13993     234 VIlpmSDDFYNLLRQIFTVNPNNRILLPELQL 265
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
31767-31976 1.44e-24

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 108.79  E-value: 1.44e-24
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31767 EDLGRGEFGIVHRCVetsskktfmAKFVKVKGTDQVLVK---------------KEISILNIARHRNILYLHESFESMEE 31831
Cdd:smart00221     5 KKLGEGAFGEVYKGT---------LKGKGDGKEVEVAVKtlkedaseqqieeflREARIMRKLDHPNIVKLLGVCTEEEP 75
                             90       100       110       120       130       140       150       160
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31832 LVMIFEFISG--LDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKnsIIKIIEFGQARQ 31909
Cdd:smart00221    76 LMIVMEYMPGgdLLDYLRKNRPKE-LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENL--VVKISDFGLSRD 152
                            170       180       190       200       210       220       230
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31910 LKPGDNFRLLFT-AP-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIMNAEY 31976
Cdd:smart00221   153 LYDDDYYKVKGGkLPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYR 222
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
26310-26391 1.84e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 102.28  E-value: 1.84e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26310 VIVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNC 26389
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 26390 KV 26391
Cdd:cd05748      81 KV 82
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
31780-32018 1.91e-24

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 108.79  E-value: 1.91e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31780 CVETSSKKTFMAKFVKV-----KGTDQVLVKKEISILN-----------IARHRNILYLHESFESMEELVMIFEFISGLD 31843
Cdd:PHA03390     16 CEIVKKLKLIDGKFGKVsvlkhKPTQKLFVQKIIKAKNfnaiepmvhqlMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGD 95
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSIIKIIEFGQARQLKpgdnfrllftAP 31923
Cdd:PHA03390     96 LFDLLKKEGK-LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY-DRAKDRIYLCDYGLCKIIG----------TP 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31924 -------EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFlAETNQQMIE-NIMNAEYTFDEEAFQEISLEAMDFID 31995
Cdd:PHA03390    164 scydgtlDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPF-KEDEDEELDlESLLKRQQKKLPFIKNVSKNANDFVQ 242
                           250       260
                    ....*....|....*....|....
gi 1958765569 31996 RLLVKERKSRMTA-SEALKHPWLK 32018
Cdd:PHA03390    243 SMLKYNINYRLTNyNEIIKHPFLK 266
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25414-25506 2.29e-24

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 102.57  E-value: 2.29e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25414 PGPPSTPEASAITKDSMVLTWTRPVDDGGaEIEGYILEKRDKEGIRWTKCNKKTLTDLRFRVTGLTEGHSYEFRVAAENA 25493
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 25494 AGVGEPSEPSVFY 25506
Cdd:cd00063      80 GGESPPSESVTVT 92
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
31768-32016 3.58e-24

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 108.22  E-value: 3.58e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31768 DLGRGEFGIV----------HRCVETSSKKTFMAKF--------------VKVKGTDQVLVKKEISILNIARHRNILYLH 31823
Cdd:cd14118       1 EIGKGSYGIVklayneedntLYAMKILSKKKLLKQAgffrrppprrkpgaLGKPLDPLDRVYREIAILKKLDHPNVVKLV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31824 ESFESMEE--LVMIFEFISGLDIFERINTSAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKI 31901
Cdd:cd14118      81 EVLDDPNEdnLYMVFELVDKGAVMEVPTDNPLS--EETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLG--DDGHVKI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31902 IEFGQARQLKPGDNFrLLFTA--PEYYAPEV---HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEY 31976
Cdd:cd14118     157 ADFGVSNEFEGDDAL-LSSTAgtPAFMAPEAlseSRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPV 235
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|
gi 1958765569 31977 TFDEEAfqEISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14118     236 VFPDDP--VVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
25915-25996 4.74e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 101.13  E-value: 4.74e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25915 TFNVKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITV 25994
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 25995 IV 25996
Cdd:cd05748      81 KV 82
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
31769-32018 5.47e-24

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 107.40  E-value: 5.47e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIV----HR-------CVETSSKKTFmakfvkvkGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14201      14 VGHGAFAVVfkgrHRkktdwevAIKSINKKNL--------SKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENII--YQTRKNSI-----IKIIEFGQARQL 31910
Cdd:cd14201      86 YCNGGDLADYLQAKG-TLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILlsYASRKKSSvsgirIKIADFGFARYL 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMiENIMNAEYTFDEEAFQEISLEA 31990
Cdd:cd14201     165 QSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDL-RMFYEKNKNLQPSIPRETSPYL 243
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd14201     244 ADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
I-set pfam07679
Immunoglobulin I-set domain;
6915-6996 5.54e-24

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 101.18  E-value: 5.54e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIG 6994
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ..
gi 1958765569  6995 TA 6996
Cdd:pfam07679    81 EA 82
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
31762-31976 9.37e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 106.43  E-value: 9.37e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd08218       1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEInisKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTS-AFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLK-PGDNF 31916
Cdd:cd08218      81 CDGGDLYKRINAQrGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT--KDGIIKLGDFGIARVLNsTVELA 158
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEY 31976
Cdd:cd08218     159 RTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSY 218
I-set pfam07679
Immunoglobulin I-set domain;
900-989 1.04e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 100.41  E-value: 1.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAG 979
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569   980 TVSTSCYLAV 989
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26998-27452 1.20e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 112.40  E-value: 1.20e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26998 VYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGT---TKTFI 27074
Cdd:COG3401     146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGEsapSNEVS 225
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27075 NIIVLDRPGPPTGpVAISDITEESVTLKWEPPKydgGSHVTNYIVLKRETSTAVWTEVsATVARTMIKVMKLTTGEEYQF 27154
Cdd:COG3401     226 VTTPTTPPSAPTG-LTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYY 300
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27155 RIKAENRFGI-SDhiDSACVVVKLPYTTPGPPSTPWVSNVTRESITVGWhEPVSNGGsaVIGYHLEMKDRNSILWQKANK 27233
Cdd:COG3401     301 RVTAVDAAGNeSA--PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAE 375
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27234 MIiRTTHFKVTTISAGLIYEFRVYAENAAGIGkpSHSSEPVLAIDAcePPRNVRITDISKNSVNLSWQQPAFDGGSKITG 27313
Cdd:COG3401     376 TV-TTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTA--SAASGESLTASVDAVPLTDVAGATAAASAASN 450
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27314 YIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAVGSVSNpSEVVGPITCIDSYGGPVIDLPLEYTEV 27393
Cdd:COG3401     451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGA-SSVTNSVSVIGASAAAAVGGAPDGTPN 529
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 27394 VKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNS 27452
Cdd:COG3401     530 VTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTN 588
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
31758-32037 1.32e-23

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 106.56  E-value: 1.32e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEKYmiaEDLGRGEFGIVHRCVETSSKKTFMAKFVKV-KGTDQV-LVKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd06609       1 ELFTLL---ERIGKGSFGEVYKGIDKRTNQVVAIKVIDLeEAEDEIeDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWII 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPGDN 31915
Cdd:cd06609      78 MEYCGGGSVLDLLKPGPLD--ETYIAFILREVLLGLEYLHSEGKIHRDIKAANIL--LSEEGDVKLADFGVSGQLTSTMS 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTA-PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPfLAETNQQ--MIENIMNAEYTFDEEAFqeiSLEAMD 31992
Cdd:cd06609     154 KRNTFVGtPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPP-LSDLHPMrvLFLIPKNNPPSLEGNKF---SKPFKD 229
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWLKqrmdRVSTKVIRTLRHRRY 32037
Cdd:cd06609     230 FVELCLNKDPKERPSAKELLKHKFIK----KAKKTSYLTLLIERI 270
I-set pfam07679
Immunoglobulin I-set domain;
5697-5787 1.37e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 100.02  E-value: 1.37e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDA 5776
Cdd:pfam07679     1 PKFTQKPKDVEV-QEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  5777 GTASCSIELKV 5787
Cdd:pfam07679    80 GEAEASAELTV 90
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31762-32016 1.44e-23

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 105.84  E-value: 1.44e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14665       1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14665      81 GELFERI-CNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVG 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEV---HQHDvvSSATDMWSLGTLVYVLLSGINPFLAETN----QQMIENIMNAEYTFDEeaFQEISLEAMDFI 31994
Cdd:cd14665     160 TPAYIAPEVllkKEYD--GKIADVWSCGVTLYVMLVGAYPFEDPEEprnfRKTIQRILSVQYSIPD--YVHISPECRHLI 235
                           250       260
                    ....*....|....*....|..
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14665     236 SRIFVADPATRITIPEIRNHEW 257
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
31769-32017 1.56e-23

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 105.85  E-value: 1.56e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFG---IVHRcVETSSKKTFMAKFVKVKGTDQVL------VKKEISILNIARHRNI---LYLHESFESmeELVMIF 31836
Cdd:cd13994       1 IGKGATSvvrIVTK-KNPRSGVLYAVKEYRRRDDESKRkdyvkrLTSEYIISSKLHHPNIvkvLDLCQDLHG--KWCLVM 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTS-AFELNEREVvsYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK-PGD 31914
Cdd:cd13994      78 EYCPGGDLFTLIEKAdSLSLEEKDC--FFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV--LKLTDFGTAEVFGmPAE 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 N----FRLLFTAPEYYAPEVH-QHDVVSSATDMWSLGTLVYVLLSGINPF-LAETNQQMIENIMNaEYTFDEEAFQEISL 31988
Cdd:cd13994     154 KespmSAGLCGSEPYMAPEVFtSGSYDGRAVDVWSCGIVLFALFTGRFPWrSAKKSDSAYKAYEK-SGDFTNGPYEPIEN 232
                           250       260       270
                    ....*....|....*....|....*....|...
gi 1958765569 31989 ----EAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd13994     233 llpsECRRLIYRMLHPDPEKRITIDEALNDPWV 265
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19211-19297 1.70e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 99.88  E-value: 1.70e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19211 PGPVSDLKVSDVTKTSCHVSWAPPENDGGsPVTHYIVEKREAERKTWSTV-TPEVKKTSFNVTNLVPGNEYFFRVTAVNE 19289
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 19290 YGPGVPTD 19297
Cdd:cd00063      80 GGESPPSE 87
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
31762-32017 1.83e-23

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 105.29  E-value: 1.83e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTDQVLVK--KEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14072       1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIdKTQLNPSSLQKlfREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd14072      81 ASGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMN--IKIADFGFSNEFTPGNKLDT 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAPEVHQ---HDvvSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFdeeAFQeISLEAMDFID 31995
Cdd:cd14072     158 FCGSPPYAAPELFQgkkYD--GPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI---PFY-MSTDCENLLK 231
                           250       260
                    ....*....|....*....|..
gi 1958765569 31996 RLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14072     232 KFLVLNPSKRGTLEQIMKDRWM 253
I-set pfam07679
Immunoglobulin I-set domain;
8048-8137 1.92e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 99.64  E-value: 1.92e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAG 8127
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8128 KDSCSAQLGV 8137
Cdd:pfam07679    81 EAEASAELTV 90
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
31763-32017 2.06e-23

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 105.19  E-value: 2.06e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK---EISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd08529       2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEaidEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNF-R 31917
Cdd:cd08529      82 ENGDLHSLIKSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN--VKIGDLGVAKILSDTTNFaQ 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYtfdEEAFQEISLEAMDFIDRL 31997
Cdd:cd08529     160 TIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKY---PPISASYSQDLSQLIDSC 236
                           250       260
                    ....*....|....*....|
gi 1958765569 31998 LVKERKSRMTASEALKHPWL 32017
Cdd:cd08529     237 LTKDYRQRPDTTELLRNPSL 256
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
31769-32018 2.08e-23

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 107.76  E-value: 2.08e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTF----MAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05573       9 IGRGAFGEVWLVRDKDTGQVYamkiLRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEYMPGGDL 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 ---FERINTsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd05573      89 mnlLIKYDV----FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLD--ADGHIKLADFGLCTKMNKSGDRESYLN 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 A------------------------------PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENI 31971
Cdd:cd05573     163 DsvntlfqdnvlarrrphkqrrvraysavgtPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKI 242
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 1958765569 31972 MNAEYTFDEEAFQEISLEAMDFIDRLLvKERKSRMTASEALK-HPWLK 32018
Cdd:cd05573     243 MNWKESLVFPDDPDVSPEAIDLIRRLL-CDPEDRLGSAEEIKaHPFFK 289
I-set pfam07679
Immunoglobulin I-set domain;
3305-3391 2.10e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 99.64  E-value: 2.10e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3305 PAIVTPLQDAVTSEGRPARFQCQVSGT-DLKVSWYCRDKKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAVG 3383
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*...
gi 1958765569  3384 QVSSTATL 3391
Cdd:pfam07679    81 EAEASAEL 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29169-29249 2.55e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.82  E-value: 2.55e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29169 ITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLKETDRMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITVV 29248
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 29249 V 29249
Cdd:cd05748      82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25290-25610 2.76e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 111.25  E-value: 2.76e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25290 QYTLKLSNVGGTKTIPITVKVLDRPGPPEGP--LKVTGVTAEKCYLAWNPPlqdGGASISHYIIEKRETSRLSWTQVSTe 25367
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVAT- 281
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25368 VQALNYKVTKLLPGNEYIFRVMAVNKYGVgeplESEP--VIACNPYK-LPGPPSTPEASAITKDSMVLTWTrPVDDGGAe 25444
Cdd:COG3401     282 VTTTSYTDTGLTNGTTYYYRVTAVDAAGN----ESAPsnVVSVTTDLtPPAAPSGLTATAVGSSSITLSWT-ASSDADV- 355
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25445 iEGYILEKRDKEGIRWTKCNkKTLTDLRFRVTGLTEGHSYEFRVAAENAAGV-GEPSEPSVF--YRACDALYPPGPPSNP 25521
Cdd:COG3401     356 -TGYNVYRSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSAttASAASGESLTASVDAV 433
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25522 KVTDTSRSSVSLAWNKPiYDGGAPVRGYVIELKEAAADEWTTCTPPSGLQGKQFTVTKLKENTEYNFRICAFNTEGVGEP 25601
Cdd:COG3401     434 PLTDVAGATAAASAASN-PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVI 512

                    ....*....
gi 1958765569 25602 ATIPGSVVA 25610
Cdd:COG3401     513 GASAAAAVG 521
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
31763-32017 3.12e-23

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 106.47  E-value: 3.12e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK--VKGTDQVLVkkEISILNIARHR------NILYLHESFESMEELVM 31834
Cdd:cd14210      15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRnkKRFHQQALV--EVKILKHLNDNdpddkhNIVRYKDSFIFRGHLCI 92
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISgLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFG-------- 31905
Cdd:cd14210      93 VFELLS-INLYELLKSNNFQgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVIDFGsscfegek 171
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31906 -----QARqlkpgdnFrllftapeYYAPEV---HQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQ------------ 31965
Cdd:cd14210     172 vytyiQSR-------F--------YRAPEVilgLPYD---TAIDMWSLGCILAELYTGYPLFPGENEEeqlacimevlgv 233
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31966 ---QMIENIMNAEYTFDEEAF--------------QEISLEAM---------DFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14210     234 ppkSLIDKASRRKKFFDSNGKprpttnskgkkrrpGSKSLAQVlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
31761-32018 3.17e-23

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 105.01  E-value: 3.17e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT-DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd06647       7 KKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFR-L 31918
Cdd:cd06647      87 AGGSLTDVVTETC--MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM--DGSVKLTDFGFCAQITPEQSKRsT 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAetnqqmiENIMNAEY------TFDEEAFQEISLEAMD 31992
Cdd:cd06647     163 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-------ENPLRALYliatngTPELQNPEKLSAIFRD 235
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd06647     236 FLNRCLEMDVEKRGSAKELLQHPFLK 261
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22167-22259 3.42e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 99.11  E-value: 3.42e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22167 PDPPKNPEVTTITKDSMVVCWGHPDSDGGsEIINYIVERRDKAGQRWVKCNKKALTDLRFKVSGLTEGHEYEFRIMAENA 22246
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 22247 AGVSAPSATSPFY 22259
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18046-18507 3.62e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.86  E-value: 3.62e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18046 IRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLTVLDVPGPPTGPINi 18125
Cdd:COG3401      80 AAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGT- 158
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18126 ldvtpeymTISWQPPKDDGGSPVINYIVEKQDTrkgtwgVVSAGSSKLKLKVPHLQKGCEYVFRVKAENKMGVGPPLDSI 18205
Cdd:COG3401     159 --------TASSVAGAGVVVSPDTSATAAVATT------SLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEV 224
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18206 PTVAKHkfSPPSPPGKPVVTDITENAATVSWTLPKSDGgspITGYYVERREIT-GKWVRVNKTpiADLKFRVTGLYEGNT 18284
Cdd:COG3401     225 SVTTPT--TPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGdGPFTKVATV--TTTSYTDTGLTNGTT 297
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18285 YEFRVFAENLAGlsNPSPSSDPIKACRPIKPPGPPINPKLKDKTKESADLVWTKPLSdggSPILGYVVECQKPGTTQWDR 18364
Cdd:COG3401     298 YYYRVTAVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD---ADVTGYNVYRSTSGGGTYTK 372
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18365 INkdELIRQCAFRVPGLIEGNEYRFRIRAANIVGEgEPRELAESVIAKDILHPPEVELDVTCRDVITVRVGQTIRILARv 18444
Cdd:COG3401     373 IA--ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAA- 448
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 18445 kgrpEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:COG3401     449 ----SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
31769-32014 3.64e-23

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 106.63  E-value: 3.64e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVhrcVETSSKKTFMAKFVKVKGTDQVLVKKEIS-------ILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd05595       3 LGKGTFGKV---ILVREKATGRYYAMKILRKEVIIAKDEVAhtvtesrVLQNTRHPFLTALKYAFQTHDRLCFVMEYANG 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFerintsaFELNEREVVS------YVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQ-LKPGD 31914
Cdd:cd05595      80 GELF-------FHLSRERVFTedrarfYGAEIVSALEYLHSRDVVYRDIKLENLMLD--KDGHIKITDFGLCKEgITDGA 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFI 31994
Cdd:cd05595     151 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFP----RTLSPEAKSLL 226
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31995 DRLLVKERKSRM-----TASEALKH 32014
Cdd:cd05595     227 AGLLKKDPKQRLgggpsDAKEVMEH 251
I-set pfam07679
Immunoglobulin I-set domain;
3461-3550 3.65e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 98.87  E-value: 3.65e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYG 3540
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  3541 RAVCSAHLKV 3550
Cdd:pfam07679    81 EAEASAELTV 90
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
31762-32017 3.79e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 104.65  E-value: 3.79e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAK---FVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd08225       1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKeidLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTS-AFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIiYQTRKNSIIKIIEFGQARQLKpgDNFR 31917
Cdd:cd08225      81 CDGGDLMKRINRQrGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNI-FLSKNGMVAKLGDFGIARQLN--DSME 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFT---APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFqeiSLEAMDFI 31994
Cdd:cd08225     158 LAYTcvgTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNF---SRDLRSLI 234
                           250       260
                    ....*....|....*....|...
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd08225     235 SQLFKVSPRDRPSITSILKRPFL 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
31767-31973 4.12e-23

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 104.50  E-value: 4.12e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVetsskktfmAKFVKVKGTDQVLVK---------------KEISILNIARHRNILYLHESFESMEE 31831
Cdd:pfam07714     5 EKLGEGAFGEVYKGT---------LKGEGENTKIKVAVKtlkegadeeeredflEEASIMKKLDHPNIVKLLGVCTQGEP 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISG--LDIFERINTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQ 31909
Cdd:pfam07714    76 LYIVTEYMPGgdLLDFLRKHKRK--LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVS--ENLVVKISDFGLSRD 151
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31910 LKPGDNFRLLFTAPE---YYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIMN 31973
Cdd:pfam07714   152 IYDDDYYRKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLED 219
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
31549-31630 4.14e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.43  E-value: 4.14e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31549 VHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFGIDQKTVEL 31628
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKN-AKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 31629 DV 31630
Cdd:cd05748      81 KV 82
I-set pfam07679
Immunoglobulin I-set domain;
104-193 4.48e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 98.48  E-value: 4.48e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVG 183
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569   184 RATSTADLLV 193
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16015-16314 4.75e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.48  E-value: 4.75e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16015 NLAVTDIKAESCYLTWDAPLDNGGSEITHYIIDKRDASRKKSEWEEVTNTAVerrygiwkLIPNGQYEFRVRAVNKYGTS 16094
Cdd:COG3401     147 LYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGD--------IEPGTTYYYRVAATDTGGES 218
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16095 DEckSDKVVIQDPYRLPGPPGKPKVLERTKGSMLVSWTPPLDNGgspITGYWLEKREEGGAYWSRVSRapitkvgLKGVE 16174
Cdd:COG3401     219 AP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT-------VTTTS 286
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16175 FSVPRLIEGVKYQFRAMAINAAGIgpPSEPSDPAVAGDPIYPPGPPSCPEVKDKTKSSISLAWKPPAkdgGSPIKGYIVE 16254
Cdd:COG3401     287 YTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVY 361
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 16255 MQEEGTTDWKKVNEpdkLLTACECVVPNLKELRKYRFRVKAVNEAG-ESEPSDTTGEIPAT 16314
Cdd:COG3401     362 RSTSGGGTYTKIAE---TVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTAS 419
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
20214-20295 6.36e-23

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 98.05  E-value: 6.36e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20214 TLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIVV 20293
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 20294 KV 20295
Cdd:cd05748      81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
13804-13891 8.46e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 97.95  E-value: 8.46e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13804 PSPPVNLSASEQTQSSVQLTWEPPlKDGGSPILGYIIERQEEGKDNWIRCNMKPVPELTYKVTGLQKGNKYLYRVSAENA 13883
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 13884 AGVSDPSE 13891
Cdd:cd00063      80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24331-24421 8.54e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 97.95  E-value: 8.54e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24331 PGPPKSLEVTNIAKDSMTVCWNRPDSDGGsEIIGYIVEKRDRSGIRWIKCNKRRITDLRLRVTGLTEDHEYEFRVSAENA 24410
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 24411 AGVGEPSPATV 24421
Cdd:cd00063      80 GGESPPSESVT 90
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
31757-32019 8.67e-23

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 104.68  E-value: 8.67e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYMiaeDLGRGEFGIVHRCVETSSKKTFMAKFVKV-KGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd06659      20 RQLLENYV---KIGEGSTGVVCIAREKHSGRQVAVKMMDLrKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVL 96
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISG---LDIferinTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQL-K 31911
Cdd:cd06659      97 MEYLQGgalTDI-----VSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTL--DGRVKLSDFGFCAQIsK 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTfDEEAFQEISLEAM 31991
Cdd:cd06659     170 DVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPP-KLKNSHKASPVLR 248
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd06659     249 DFLERMLVRDPQERATAQELLDHPFLLQ 276
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
31769-32017 9.40e-23

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 103.67  E-value: 9.40e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHrCVETSSKKTFMAKFVKVKGTDQVLVKK-------EISILNIARHRNIL-YLHESFEsmEELVMIF-EFI 31839
Cdd:cd06631       9 LGKGAYGTVY-CGLTSTGQLIAVKQVELDTSDKEKAEKeyeklqeEVDLLKTLKHVNIVgYLGTCLE--DNVVSIFmEFV 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQL----KPGDN 31915
Cdd:cd06631      86 PGGSIASILARFG-ALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMP--NGVIKLIDFGCAKRLcinlSSGSQ 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFT---APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGiNPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMD 31992
Cdd:cd06631     163 SQLLKSmrgTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATG-KPPWADMNPMAAIFAIGSGRKPVPRLPDKFSPEARD 241
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06631     242 FVHACLTRDQDERPSAEQLLKHPFI 266
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15415-15507 9.41e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 97.95  E-value: 9.41e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15415 PDAPDKPIVDDVTSNSMVVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKALLSSLKTKVDGLLEGLTYVFRVCAENAA 15494
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|...
gi 1958765569 15495 GPGKFSPPSDPKT 15507
Cdd:cd00063      81 GESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
6541-6629 9.75e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.71  E-value: 9.75e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6541 VIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGK 6620
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  6621 SSCTAVVDV 6629
Cdd:pfam07679    82 AEASAELTV 90
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
31770-32018 1.17e-22

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 105.00  E-value: 1.17e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31770 GRGEFGIVHRCVETSSKKTFMAKfvKVKGTD-----QVL-VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLD 31843
Cdd:cd05599      10 GRGAFGEVRLVRKKDTGHVYAMK--KLRKSEmlekeQVAhVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEFLPGGD 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFE---RINTsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQArqlKPGDNFRLLF 31920
Cdd:cd05599      88 MMTllmKKDT----LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGH--IKLSDFGLC---TGLKKSHLAY 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 TA---PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYT--FDEEAfqEISLEAMDFID 31995
Cdd:cd05599     159 STvgtPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETlvFPPEV--PISPEAKDLIE 236
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31996 RLL--VKERKSRMTASEALKHPWLK 32018
Cdd:cd05599     237 RLLcdAEHRLGANGVEEIKSHPFFK 261
I-set pfam07679
Immunoglobulin I-set domain;
7856-7945 1.21e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.33  E-value: 1.21e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVG 7935
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7936 AVASSAVLVI 7945
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
4949-5038 1.40e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 97.33  E-value: 1.40e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVG 5028
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5029 SKDSRGALIV 5038
Cdd:pfam07679    81 EAEASAELTV 90
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
31769-32010 1.48e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 104.66  E-value: 1.48e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVhrcVETSSKKTFMAKFVKVKGTDQVLVKKEISilNIARHRNILY----------LHESFESMEELVMIFEF 31838
Cdd:cd05604       4 IGKGSFGKV---LLAKRKRDGKYYAVKVLQKKVILNRKEQK--HIMAERNVLLknvkhpflvgLHYSFQTTDKLYFVLDF 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ-LKPGDNFR 31917
Cdd:cd05604      79 VNGGELFFHLQRERS-FPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGH--IVLTDFGLCKEgISNSDTTT 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRL 31997
Cdd:cd05604     156 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRP----GISLTAWSILEEL 231
                           250
                    ....*....|...
gi 1958765569 31998 LVKERKSRMTASE 32010
Cdd:cd05604     232 LEKDRQLRLGAKE 244
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
31761-32016 1.60e-22

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 103.61  E-value: 1.60e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTF-MAKFVKVKgtDQVLVKK----EISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd07847       1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVaIKKFVESE--DDPVIKKialrEIRMLKQLKHPNLVNLIEVFRRKRKLHLV 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFI--SGLDIFERiNTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPG 31913
Cdd:cd07847      79 FEYCdhTVLNELEK-NPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENIL--ITKQGQIKLCDFGFARILTGP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTAPEYY-APEVHQHDVV-SSATDMWSLGTLVYVLLSG---------------INPFLAETNQQMIENIMNAEY 31976
Cdd:cd07847     154 GDDYTDYVATRWYrAPELLVGDTQyGPPVDVWAIGCVFAELLTGqplwpgksdvdqlylIRKTLGDLIPRHQQIFSTNQF 233
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31977 TFD------------EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07847     234 FKGlsipepetreplESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25868-26388 2.16e-22

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 108.55  E-value: 2.16e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25868 SGLTAGEEYVFRVAAVNEKGRSDPRQLGVPVVAKDIEIKPSVELPFNTFNVKANDQL--KIDIPFKGRPQATVAWKKDGQ 25945
Cdd:COG3401      11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLgtGGRAGTTSGVAAVAVAAAPPT 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25946 VLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIVLDrpgPPGPIRIDEVSCDNVSISWTPPEY 26025
Cdd:COG3401      91 ATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYAL---GAGLYGVDGANASGTTASSVAGAG 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26026 DGGCQISNYIVEKRETTSTTWQVVsqavarTSIKIVRLTTGSEYQFRVCAENRYGKSSYSESSAVVaeYPFSPPGPPgTP 26105
Cdd:COG3401     168 VVVSPDTSATAAVATTSLTVTSTT------LVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVT--TPTTPPSAP-TG 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26106 KVVHATKSTMV-VSWQvPVNDGGsqVIGYHLEYKERSSILWSKANKVliADTQMKVSGLDEGLLYEYRVYAENIAGIGkc 26184
Cdd:COG3401     239 LTATADTPGSVtLSWD-PVTESD--ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNE-- 311
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26185 SKACEPVPARDPCDPPGQPE---VTNITRKSVSLKWSKPrydGGAKITGYIVERRELPDGRWLKCNFTnVQETYFEVTEL 26261
Cdd:COG3401     312 SAPSNVVSVTTDLTPPAAPSgltATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGL 387
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26262 TEDQRYEFRVFARNAADSVSEPSE----STGPITVKDDVEAPRIMMDvkfrdvivVKAGEVLKINADIAGRPLPVISWAK 26337
Cdd:COG3401     388 TPGTTYYYKVTAVDAAGNESAPSEevsaTTASAASGESLTASVDAVP--------LTDVAGATAAASAASNPGVSAAVLA 459
                           490       500       510       520       530
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 26338 DGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVN 26388
Cdd:COG3401     460 DGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
31762-32017 2.48e-22

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 102.61  E-value: 2.48e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV----------LVKKEISILNIARHRNIL-YLHESFESmE 31830
Cdd:cd06628       1 KWIKGALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAEnkdrkksmldALQREIALLRELQHENIVqYLGSSSDA-N 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 ELVMIFEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQL 31910
Cdd:cd06628      80 HLNIFLEYVPGGSVATLLNNYG-AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG--IKISDFGISKKL 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPG------DNFRLLFTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENI-MNAEYTFDEea 31982
Cdd:cd06628     157 EANslstknNGARPSLQGSVFWmAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIgENASPTIPS-- 234
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 31983 fqEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06628     235 --NISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
31769-32010 2.68e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 104.33  E-value: 2.68e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGtdqVLVKKEISilNIARHRNILY----------LHESFESMEELVMIFEF 31838
Cdd:cd05602      15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKA---ILKKKEEK--HIMSERNVLLknvkhpflvgLHFSFQTTDKLYFVLDY 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFELNEREVVsYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ-LKPGDNFR 31917
Cdd:cd05602      90 INGGELFYHLQRERCFLEPRARF-YAAEIASALGYLHSLNIVYRDLKPENILLDSQGH--IVLTDFGLCKEnIEPNGTTS 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRL 31997
Cdd:cd05602     167 TFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKP----NITNSARHLLEGL 242
                           250
                    ....*....|...
gi 1958765569 31998 LVKERKSRMTASE 32010
Cdd:cd05602     243 LQKDRTKRLGAKD 255
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
31762-32017 2.96e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 102.12  E-value: 2.96e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK------VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd08222       1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKVLKeisvgeLQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINT---SAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqtrKNSIIKIIEFGQARQLKP 31912
Cdd:cd08222      81 TEYCEGGDLDDKISEykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL---KNNVIKVGDFGISRILMG 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 GDNFRLLFTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAetnqqmiENIMNAEYTFDEEAFQEI----S 31987
Cdd:cd08222     158 TSDLATTFTGTPYYmSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDG-------QNLLSVMYKIVEGETPSLpdkyS 230
                           250       260       270
                    ....*....|....*....|....*....|
gi 1958765569 31988 LEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd08222     231 KELNAIYSRMLNKDPALRPSAAEILKIPFI 260
I-set pfam07679
Immunoglobulin I-set domain;
33698-33787 3.04e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 96.17  E-value: 3.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRG 33777
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 33778 QCSATASLTV 33787
Cdd:pfam07679    81 EAEASAELTV 90
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
31769-32008 3.42e-22

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 103.51  E-value: 3.42e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVhRCVETSSKKTFMAkfVKVKGTDQVLVKKEISilNIARHRNILY----------LHESFESMEELVMIFEF 31838
Cdd:cd05603       3 IGKGSFGKV-LLAKRKCDGKFYA--VKVLQKKTILKKKEQN--HIMAERNVLLknlkhpflvgLHYSFQTSEKLYFVLDY 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFELNEREVVsYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKiiEFGQARQ-LKPGDNFR 31917
Cdd:cd05603      78 VNGGELFFHLQRERCFLEPRARF-YAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLT--DFGLCKEgMEPEETTS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfqeiSLEAMDFIDRL 31997
Cdd:cd05603     155 TFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGK----TVAACDLLQGL 230
                           250
                    ....*....|.
gi 1958765569 31998 LVKERKSRMTA 32008
Cdd:cd05603     231 LHKDQRRRLGA 241
I-set pfam07679
Immunoglobulin I-set domain;
7577-7666 3.59e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 96.17  E-value: 3.59e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAG 7656
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7657 QDESSALLTV 7666
Cdd:pfam07679    81 EAEASAELTV 90
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
31765-32024 3.71e-22

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 102.25  E-value: 3.71e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHRCVETSSK-----KTFMAKFVKVKGTDQVLvKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd14117      10 IGRPLGKGKFGNVYLAREKQSKfivalKVLFKSQIEKEGVEHQL-RREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYA 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQlKPGDNFRLL 31919
Cdd:cd14117      89 PRGELYKELQKHG-RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGE--LKIADFGWSVH-APSLRRRTM 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYYAPEV---HQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDR 31996
Cdd:cd14117     165 CGTLDYLPPEMiegRTHD---EKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFP----PFLSDGSRDLISK 237
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31997 LLVKERKSRMTASEALKHPWLKQRMDRV 32024
Cdd:cd14117     238 LLRYHPSERLPLKGVMEHPWVKANSRRV 265
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
31761-31960 3.95e-22

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 102.50  E-value: 3.95e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCvetSSKKTfmAKFVKVK----GTDQVLVKK----EISILNIARHRNILYLHESFESMEEL 31832
Cdd:cd07846       1 EKYENLGLVGEGSYGMVMKC---RHKET--GQIVAIKkfleSEDDKMVKKiamrEIKMLKQLRHENLVNLIEVFRRKKRW 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31833 VMIFEFI--SGLDIFERINTSafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQL 31910
Cdd:cd07846      76 YLVFEFVdhTVLDDLEKYPNG---LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENIL--VSQSGVVKLCDFGFARTL 150
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31911 K-PGDNFRLLFTAPEYYAPEVHQHDV-VSSATDMWSLGTLVYVLLSGiNPFL 31960
Cdd:cd07846     151 AaPGEVYTDYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTG-EPLF 201
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
31762-32018 4.24e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 102.65  E-value: 4.24e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV-------KGTDQVLVKkEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd07841       1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLgerkeakDGINFTALR-EIKLLQELKHPNIIGLLDVFGHKSNINL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGlDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQL-KPG 31913
Cdd:cd07841      80 VFEFMET-DLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIA--SDGVLKLADFGLARSFgSPN 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNF------------RLLFTAPEYyapevhqhdvvSSATDMWSLGTLVYVLLSGInPFLAETNQ--QMiENIMNAEYTFD 31979
Cdd:cd07841     157 RKMthqvvtrwyrapELLFGARHY-----------GVGVDMWSVGCIFAELLLRV-PFLPGDSDidQL-GKIFEALGTPT 223
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31980 EE---------------AFQEISL---------EAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd07841     224 EEnwpgvtslpdyvefkPFPPTPLkqifpaasdDALDLLQRLLTLNPNKRITARQALEHPYFS 286
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17524-17613 5.01e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 95.64  E-value: 5.01e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17524 PDAPEQPVVTEVTKDSALVTWNKPNDGGKPITNYILEKRETMSKRWVRVTKEPIhPYTKYRVPDLLEGCQYEFRVSAENE 17603
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 17604 IGIGDPSPPS 17613
Cdd:cd00063      80 GGESPPSESV 89
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
31762-32019 5.24e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 102.99  E-value: 5.24e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTfmakfVKVKG-----TDQVLVKK---EISILNIARHRNILYLH-----ESFES 31828
Cdd:cd07834       1 RYELLKPIGSGAYGVVCSAYDKRTGRK-----VAIKKisnvfDDLIDAKRilrEIKILRHLKHENIIGLLdilrpPSPEE 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31829 MEELVMIFEFIsGLDiFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQAR 31908
Cdd:cd07834      76 FNDVYIVTELM-ETD-LHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNIL--VNSNCDLKICDFGLAR 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31909 QLKPGDNFRLL--FTAPEYY-APEV----HQHdvvSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEE 31981
Cdd:cd07834     152 GVDPDEDKGFLteYVVTRWYrAPELllssKKY---TKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEE 228
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31982 AFQEISL---------------------------EAMDFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd07834     229 DLKFISSekarnylkslpkkpkkplsevfpgaspEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
20882-21397 5.33e-22

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 107.40  E-value: 5.33e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20882 KDEYEAPTIVLDPTIKDGLTVKAGDSIVLSAISILGKPLPkssWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGE 20961
Cdd:COG3401      34 KTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRA---GTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTG 110
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20962 YTITATNPFGTKEEHVKVSVLDVPGPP--------GPIEISNVSAEKATLTWTPPLEDGGSPIKAYVLEKRETSRLLWTV 21033
Cdd:COG3401     111 LTSSDEVPSPAVGTATTATAVAGGAATagtyalgaGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTST 190
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21034 VSEDiqacrhVVTKLIQGNEYLFRVSAVNhyGKGEPVQSEPVKMVDRFGPPGPPGKPEISNVTKNTATVSWkRPIDDGGs 21113
Cdd:COG3401     191 TLVD------GGGDIEPGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW-DPVTESD- 260
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21114 eITGYHVERREKKGLRWVRATKTPVSDLRckVTGLQEGNTYEFRVSAENRAGIgpPSDASNPVLMKDVAYPPGPPSNAHV 21193
Cdd:COG3401     261 -ATGYRVYRSNSGDGPFTKVATVTTTSYT--DTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTA 335
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21194 TDTTKKSASLAWGKPHydgGLEITGYVVEHQKVGDDAWIKdtTGTALRITQFVVPDLQTKEKYNFRISAVNDAGVgEPAV 21273
Cdd:COG3401     336 TAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTK--IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAP 409
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21274 IPNVEIVEKETAPDFELDAElrrTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKHRANIENTESFTLLIIPECNRYD 21353
Cdd:COG3401     410 SEEVSATTASAASGESLTAS---VDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTT 486
                           490       500       510       520
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 21354 TGKFVMTIENPAGkkSGFVNVRVLDTPGPVLNLRPTDITKDSVT 21397
Cdd:COG3401     487 ANLSVTTGSLVGG--SGASSVTNSVSVIGASAAAAVGGAPDGTP 528
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
29569-29649 5.35e-22

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 95.35  E-value: 5.35e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29569 VTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMVK 29648
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 29649 V 29649
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16829-16926 5.63e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 95.64  E-value: 5.63e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16829 PGAPDKPTVSSVTRNSMTVNWEEPEYDGGsPVTGYWLEMKDTTSKRWKRVNRDPIKAMtlgvSYKVTGLIEGSDYQFRVY 16908
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSET----SYTLTGLKPGTEYEFRVR 75
                            90
                    ....*....|....*...
gi 1958765569 16909 AINAAGVGPASLPSDPVT 16926
Cdd:cd00063      76 AVNGGGESPPSESVTVTT 93
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31762-32016 6.15e-22

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 101.00  E-value: 6.15e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14662       1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14662      81 GELFERI-CNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVG 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEV---HQHDvvSSATDMWSLGTLVYVLLSGINPFLAETN----QQMIENIMNAEYTFDEeaFQEISLEAMDFI 31994
Cdd:cd14662     160 TPAYIAPEVlsrKEYD--GKVADVWSCGVTLYVMLVGAYPFEDPDDpknfRKTIQRIMSVQYKIPD--YVRVSQDCRHLL 235
                           250       260
                    ....*....|....*....|..
gi 1958765569 31995 DRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14662     236 SRIFVANPAKRITIPEIKNHPW 257
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
31763-32017 6.60e-22

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 101.05  E-value: 6.60e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14070       4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIdkkKAKKDSYVTknLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFG---QARQLKPGD 31914
Cdd:cd14070      84 LCPGGNLMHRIYDKK-RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN--IKLIDFGlsnCAGILGYSD 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAET------NQQMIENIMNAEYTfdeeafqEISL 31988
Cdd:cd14070     161 PFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfslralHQKMVDKEMNPLPT-------DLSP 233
                           250       260
                    ....*....|....*....|....*....
gi 1958765569 31989 EAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14070     234 GAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
31761-32017 6.99e-22

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 100.76  E-value: 6.99e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHR--CVETSSKKTFMAKFVKVK----GTDQVLVKKEISILNIAR-HRNILYLHESFESMEELV 31833
Cdd:cd14019       1 NKYRIIEKIGEGTFSSVYKaeDKLHDLYDRNKGRLVALKhiypTSSPSRILNELECLERLGgSNNVSGLITAFRNEDQVV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINTSAFElnerEVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIkIIEFGQARQLKPG 31913
Cdd:cd14019      81 AVLPYIEHDDFRDFYRKMSLT----DIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGV-LVDFGLAQREEDR 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRllftAPE-----YYAPEV-----HQhdvvSSATDMWSLGTLVYVLLSGINPFLaetnqqmieniMNAEytfDEEAF 31983
Cdd:cd14019     156 PEQR----APRagtrgFRAPEVlfkcpHQ----TTAIDIWSAGVILLSILSGRFPFF-----------FSSD---DIDAL 213
                           250       260       270
                    ....*....|....*....|....*....|....*....
gi 1958765569 31984 QEI-----SLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14019     214 AEIatifgSDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17625-17713 7.76e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 95.26  E-value: 7.76e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17625 PSPPINPEAIDTTCNSVDLTWQPPRHDGGsKILGYIVEYQKVGDEEWRRANHTPEScpETKYKVTGLRDGQTYKFRVLAV 17704
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGS--ETSYTLTGLKPGTEYEFRVRAV 77

                    ....*....
gi 1958765569 17705 NEAGESDPA 17713
Cdd:cd00063      78 NGGGESPPS 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
899-989 8.44e-22

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 94.96  E-value: 8.44e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd20972      81 GSDTTSAEIFV 91
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
31761-32014 8.46e-22

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 100.86  E-value: 8.46e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK----VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd14188       1 KRYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPhsrvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENiiYQTRKNSIIKIIEFGQARQLKPGDNF 31916
Cdd:cd14188      81 EYCSRRSMAHILKARKV-LTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGN--FFINENMELKVGDFGLAARLEPLEHR 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 R-LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFID 31995
Cdd:cd14188     158 RrTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLP----SSLLAPAKHLIA 233
                           250
                    ....*....|....*....
gi 1958765569 31996 RLLVKERKSRMTASEALKH 32014
Cdd:cd14188     234 SMLSKNPEDRPSLDEIIRH 252
I-set pfam07679
Immunoglobulin I-set domain;
31053-31132 9.87e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.63  E-value: 9.87e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31053 DVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29242-29649 1.15e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 106.24  E-value: 1.15e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29242 TFTITVVVIGRPGPVTGPIEVSSVSAESCVLSWSEPKDDGGTEITNYIVEKRESGTTAWQLINSSVKRTQIKVTHLT--K 29319
Cdd:COG3401     122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDieP 201
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29320 YKEYCFRVSSENRFGVSKPLESVPIVAehPFVPPSAPTRPEVYYVSANAMSIRWEEPYHDGgskIVGYWVEKKERNTILW 29399
Cdd:COG3401     202 GTTYYYRVAATDTGGESAPSNEVSVTT--PTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPF 276
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29400 VKENKVPclECNYKVTGLVEGLEYQFRTYALNAAGV-SKASEASRPIMAQNPVDPPGRPEVTDVTRSTVSLVWSAPMydg 29478
Cdd:COG3401     277 TKVATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS--- 351
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29479 GSKVVGYIIERkpvSEVGDGRWLKCNyTIVSDNFFTVTALSEGDTYEFRVLAKNAAGIISKGSEstgPVTCRDEYAPPKA 29558
Cdd:COG3401     352 DADVTGYNVYR---STSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSE---EVSATTASAASGE 424
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29559 ELDARLQGDLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNAS 29638
Cdd:COG3401     425 SLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASS 504
                           410
                    ....*....|.
gi 1958765569 29639 GTKSVSVMVKV 29649
Cdd:COG3401     505 VTNSVSVIGAS 515
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31762-32017 1.19e-21

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 100.00  E-value: 1.19e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSK-----KTFMAKFVKVKGT--DQVLVKKEISIL---NIARHRNILYLHESFESMEE 31831
Cdd:cd14005       1 QYEVGDLLGKGGFGTVYSGVRIRDGlpvavKFVPKSRVTEWAMinGPVPVPLEIALLlkaSKPGVPGVIRLLDWYERPDG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISG-LDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiIKIIEFGQARQL 31910
Cdd:cd14005      81 FLLIMERPEPcQDLFDFITERG-ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGE-VKLIDFGCGALL 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGdNFRLLFTAPEYYAPEVHQHDVV--SSATdMWSLGTLVYVLLSGINPFlaETNQQMIENIMNAEYTfdeeafqeISL 31988
Cdd:cd14005     159 KDS-VYTDFDGTRVYSPPEWIRHGRYhgRPAT-VWSLGILLYDMLCGDIPF--ENDEQILRGNVLFRPR--------LSK 226
                           250       260
                    ....*....|....*....|....*....
gi 1958765569 31989 EAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14005     227 ECCDLISRCLQFDPSKRPSLEQILSHPWF 255
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27281-27374 1.21e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.49  E-value: 1.21e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27281 EPPRNVRITDISKNSVNLSWQQPAFDGGsKITGYIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAV 27360
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 27361 GsVSNPSEVVGPIT 27374
Cdd:cd00063      81 G-ESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19211-19293 1.23e-21

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 94.22  E-value: 1.23e-21
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19211 PGPVSDLKVSDVTKTSCHVSWAPPENDGG-SPVTHYIVEKREaERKTWSTVTPEVKKTSFNVTNLVPGNEYFFRVTAVNE 19289
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  19290 YGPG 19293
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
33416-33505 1.26e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.63  E-value: 1.26e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAG 33495
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 33496 SVSSSCKLTI 33505
Cdd:pfam07679    81 EAEASAELTV 90
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
31745-32006 1.32e-21

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 102.20  E-value: 1.32e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31745 EVTMTKASHSKTKelYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAK------FVKVKGTDQVLvkKEISILNIARHRN 31818
Cdd:PTZ00263      4 AYMFTKPDTSSWK--LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKclkkreILKMKQVQHVA--QEKSILMELSHPF 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31819 ILYLHESFESMEELVMIFEFISGLDIFERINTSAFELNErevVS--YVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKN 31896
Cdd:PTZ00263     80 IVNMMCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPND---VAkfYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31897 siIKIIEFGQARQLkPGDNFRLLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEY 31976
Cdd:PTZ00263    157 --VKVTDFGFAKKV-PDRTFTLCGT-PEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRL 232
                           250       260       270
                    ....*....|....*....|....*....|
gi 1958765569 31977 TFDeeafQEISLEAMDFIDRLLVKERKSRM 32006
Cdd:PTZ00263    233 KFP----NWFDGRARDLVKGLLQTDHTKRL 258
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
19420-19500 1.32e-21

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 94.19  E-value: 1.32e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19420 ITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKIKVT 19499
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19500 V 19500
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31337-31430 1.39e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.49  E-value: 1.39e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31337 PSVPGKPTITAVTKDSCVVAWKPPASDGGaKIRNYYLEKREKKQNKWIAVTTEEIRETVFSVQNLIEGLEYEFRVKCENL 31416
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 31417 GGESEWSETSEPVT 31430
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
4292-4381 1.43e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 1.43e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYG 4371
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4372 SVSCTATLTV 4381
Cdd:pfam07679    81 EAEASAELTV 90
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
31769-32016 1.56e-21

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 101.66  E-value: 1.56e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKvkgTDQVLVKKEI-------SILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd05571       3 LGKGTFGKVILCREKATGELYAIKILK---KEVIIAKDEVahtltenRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNG 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFerintsaFELNEREVVS------YVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQAR-QLKPGD 31914
Cdd:cd05571      80 GELF-------FHLSRERVFSedrtrfYGAEIVLALGYLHSQGIVYRDLKLENLLLD--KDGHIKITDFGLCKeEISYGA 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFI 31994
Cdd:cd05571     151 TTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFP----STLSPEAKSLL 226
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31995 DRLLVKERKSRM-----TASEALKHPW 32016
Cdd:cd05571     227 AGLLKKDPKKRLgggprDAKEIMEHPF 253
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
31763-32017 1.62e-21

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 100.25  E-value: 1.62e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK----GTDQ-----VLVKKEISILNIARHRNILYLHESFESMEELV 31833
Cdd:cd14076       3 YILGRTLGEGEFGKVKLGWPLPKANHRSGVQVAIKlirrDTQQencqtSKIMREINILKGLTHPNIVRLLDVLKTKKYIG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKiiEFGQARQLKP- 31912
Cdd:cd14076      83 IVLEFVSGGELFDYILARRR-LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVIT--DFGFANTFDHf 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 -GDNFRLLFTAPEYYAPEVhqhdVVS------SATDMWSLGTLVYVLLSGINPFLAETNQQMIEN-------IMNAEYTF 31978
Cdd:cd14076     160 nGDLMSTSCGSPCYAAPEL----VVSdsmyagRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNvprlyryICNTPLIF 235
                           250       260       270
                    ....*....|....*....|....*....|....*....
gi 1958765569 31979 DEeafqEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14076     236 PE----YVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
I-set pfam07679
Immunoglobulin I-set domain;
5511-5600 1.62e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 1.62e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAG 5590
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5591 HSQCSGHLTV 5600
Cdd:pfam07679    81 EAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30785-31145 1.76e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 105.47  E-value: 1.76e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30785 AAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFGISKPlkseEPVIPKTPLNPPEPPSNPPEVLDVTKSSVSLSWSR 30864
Cdd:COG3401     180 VATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP----SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDP 255
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30865 PKDDGgsrVTGYYIERKETSTDKWVRHNKTqiTTTMYTVTGLVPDAEYQFRIIAQNDVGlsETSPASEPVVCKDPFDKPS 30944
Cdd:COG3401     256 VTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLTPPA 328
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30945 QPGELEILSISKDSVILQWEKPEcdgGKEILGYWVEYRQSGDSAWKKSNKErIKDRQFTIGGLLEATEYEFRVFAENETG 31024
Cdd:COG3401     329 APSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31025 L-SRPRRTAMSVKTKLTSGEAPGVRKemADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLT 31103
Cdd:COG3401     405 NeSAPSEEVSATTASAASGESLTASV--DAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT 482
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 31104 VMTEEQEDEGVYTCVATNEVGEVETSSKLLLQAAPQFHPGYP 31145
Cdd:COG3401     483 DTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAP 524
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14496-14584 1.90e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.10  E-value: 1.90e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14496 PWPPGKPTVKDIGKTSLVLNWTKPEHDGGaKIESYVIEMLKTGTDDWVRVAEGVPT-TEHLLTGLMEGQEYSFRVRAVNK 14574
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 14575 AGESEPSEPS 14584
Cdd:cd00063      80 GGESPPSESV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
21628-22304 2.06e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 105.47  E-value: 2.06e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21628 NTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITIQVHDIPGPPTGPIKFDEVSSDFVTfswepPENDGGVPISNYV 21707
Cdd:COG3401       4 SYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGG-----GLGTGGRAGTTSG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21708 VEMRQTDSTTWVElATTVIRTTYKATRLTTGVEYQFRVKAQNRYGVGPGITSASVVANYPFKVPGPPGTPQVTAVTKDSM 21787
Cdd:COG3401      79 VAAVAVAAAPPTA-TGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASG 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21788 TISWHEPLSDGGSPILGYHIERKERNGILWQTVSKALVPGNIfkstglTDGIAYEFRVIAENMAGKSKPSKPSEPTFald 21867
Cdd:COG3401     158 TTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDI------EPGTTYYYRVAATDTGGESAPSNEVSVTT--- 228
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21868 PIDPPGKPVPL---NITRHTVALKWAKPEYTGgfkITSYVVEKRDLPNGRWLKANFSNilENEFTVSGLTEDAAYEFRVI 21944
Cdd:COG3401     229 PTTPPSAPTGLtatADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTYYYRVT 303
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21945 AKNAAGAISPPSEPSDAITcrdDLEAprimvdvkfkdtitlkageafkleadvsgrppptmewakdgkelegtgkleiki 22024
Cdd:COG3401     304 AVDAAGNESAPSNVVSVTT---DLTP------------------------------------------------------ 326
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22025 adfsthlinkdssrtdsgayiltatnpggfakhifnvkvldrPGPPEGpLAVSDVTSEKCVLSWLPPLDdggAKIDHYIV 22104
Cdd:COG3401     327 ------------------------------------------PAAPSG-LTATAVGSSSITLSWTASSD---ADVTGYNV 360
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22105 QKRETSRLAWTNVATEVQVTKLKVTKLLKGNEYIFRVMAVNKYGVG----EPLESEPVLAVDPYGPPDPPKNPEVTTITK 22180
Cdd:COG3401     361 YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNEsapsEEVSATTASAASGESLTASVDAVPLTDVAG 440
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22181 DSMVVCWGHPDSDGGSEIINYIVERRDKAGQRWVKCNKKALTDLRFKVSGLTEGHEYEFRI-----MAENAAGVSAPSAT 22255
Cdd:COG3401     441 ATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGassvtNSVSVIGASAAAAV 520
                           650       660       670       680       690
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22256 SPFYKACDSV-FKPGPPGNPRVLDTSRSSISIAWNKPIYDGGSEITGYMV 22304
Cdd:COG3401     521 GGAPDGTPNVtGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGN 570
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30545-30632 2.09e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.10  E-value: 2.09e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30545 PGKPQNPRVTDTTRTSVSLAWSVPEDEGGsKVTGYLIEMQKVDQREWTKCNTTPTKIREYTLTHLPQGAEYRFRVLACNA 30624
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 30625 GGPGEPAE 30632
Cdd:cd00063      80 GGESPPSE 87
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
31763-32017 2.19e-21

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 99.86  E-value: 2.19e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK----EISILNIARHRNILYLHESFESMEELVMI-FE 31837
Cdd:cd14165       3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKflprELEILARLNHKSIIKTYEIFETSDGKVYIvME 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFR 31917
Cdd:cd14165      83 LGVQGDLLEFI-KLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLD--KDFNIKLTDFGFSKRCLRDENGR 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFT-----APEYYAPEVHQHDVVS-SATDMWSLGTLVYVLLSGINPFLAETNQQMIEniMNAEYTFDEEAFQEISLEAM 31991
Cdd:cd14165     160 IVLSktfcgSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLK--IQKEHRVRFPRSKNLTSECK 237
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14165     238 DLIYRLLQPDVSQRLCIDEVLSHPWL 263
I-set pfam07679
Immunoglobulin I-set domain;
8235-8325 2.35e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.86  E-value: 2.35e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVG 8314
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|.
gi 1958765569  8315 SDTCvgSVTLK 8325
Cdd:pfam07679    81 EAEA--SAELT 89
I-set pfam07679
Immunoglobulin I-set domain;
7200-7290 2.56e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.48  E-value: 2.56e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDtSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGV 7279
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  7280 GHASCSTALKV 7290
Cdd:pfam07679    80 GEAEASAELTV 90
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
31769-32018 2.65e-21

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 100.07  E-value: 2.65e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFV------KVKGTDQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05631       8 LGKGGFGEVCACQVRATGKMYACKKLekkrikKRKGEAMALNEKRI--LEKVNSRFVVSLAYAYETKDALCLVLTIMNGG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DI-FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd05631      86 DLkFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGH--IRISDLGLAVQIPEGETVRGRVG 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENImNAEYTFDEEAFQE-ISLEAMDFIDRLLVK 32000
Cdd:cd05631     164 TVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEV-DRRVKEDQEEYSEkFSEDAKSICRMLLTK 242
                           250       260
                    ....*....|....*....|...
gi 1958765569 32001 ERKSRM-----TASEALKHPWLK 32018
Cdd:cd05631     243 NPKERLgcrgnGAAGVKQHPIFK 265
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28766-28855 2.67e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 93.72  E-value: 2.67e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28766 PSAPAVVKVTDTSKTTVSLEWARPVFDGGmEIIGYIIEMCKADLGDWHKVNTEPCVKTRYTVTDLQAGEEYKFRVSAING 28845
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 28846 AGKGDSCEVT 28855
Cdd:cd00063      80 GGESPPSESV 89
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
31769-32018 3.27e-21

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 99.39  E-value: 3.27e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGivhrcvetsskKTFMAKfvKVKGTDQ-----VLVKKEISILN---IARH----RNIL----------YLHESF 31826
Cdd:cd05583       2 LGTGAYG-----------KVFLVR--KVGGHDAgklyaMKVLKKATIVQkakTAEHtmteRQVLeavrqspflvTLHYAF 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31827 ESMEELVMIFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQ 31906
Cdd:cd05583      69 QTDAKLHLILDYVNGGELFTHLYQREH-FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLD--SEGHVVLTDFGL 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARQLKPGDNFRLL-FTAP-EYYAPEVHQ-----HDvvsSATDMWSLGTLVYVLLSGINPFLAE---TNQQMI-ENIMNAE 31975
Cdd:cd05583     146 SKEFLPGENDRAYsFCGTiEYMAPEVVRggsdgHD---KAVDWWSLGVLTYELLTGASPFTVDgerNSQSEIsKRILKSH 222
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 1958765569 31976 YTFDeeafQEISLEAMDFIDRLLVKERKSRM-----TASEALKHPWLK 32018
Cdd:cd05583     223 PPIP----KTFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPFFK 266
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
31760-32015 3.42e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 99.04  E-value: 3.42e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIaedLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT---DQVLVKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd08220       2 YEKIRV---VGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMtkeERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVM 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFEL-NEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtRKNSIIKIIEFGQARQLKPGDN 31915
Cdd:cd08220      79 EYAPGGTLFEYIQQRKGSLlSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLN-KKRTVVKIGDFGISKILSSKSK 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEislEAMDFID 31995
Cdd:cd08220     158 AYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRYSE---ELRHLIL 234
                           250       260
                    ....*....|....*....|
gi 1958765569 31996 RLLVKERKSRMTASEALKHP 32015
Cdd:cd08220     235 SMLHLDPNKRPTLSEIMAQP 254
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
31769-32016 3.60e-21

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 98.94  E-value: 3.60e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFG----IVHRCvetssKKTFMA-KFVKVKGTDQVLVKKEISI-LNIARHRNILYLHE-SFESMEELVMIFEFISG 31841
Cdd:cd13987       1 LGEGTYGkvllAVHKG-----SGTKMAlKFVPKPSTKLKDFLREYNIsLELSVHPHIIKTYDvAFETEDYYVFAQEYAPY 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARqlKPGDNFRLLFT 31921
Cdd:cd13987      76 GDLFSIIPPQV-GLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTR--RVGSTVKRVSG 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEV-----HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQ----QMIENIMNAEYTFDEEAFQEISLEAMD 31992
Cdd:cd13987     153 TIPYTAPEVceakkNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDdqfyEEFVRWQKRKNTAVPSQWRRFTPKALR 232
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31993 FIDRLLVKERKSRMTASEA---LKHPW 32016
Cdd:cd13987     233 MFKKLLAPEPERRCSIKEVfkyLGDRW 259
I-set pfam07679
Immunoglobulin I-set domain;
3199-3288 3.63e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.09  E-value: 3.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYG 3278
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  3279 VATTSASLSV 3288
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8893-8981 3.63e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 93.09  E-value: 3.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPIG 8972
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  8973 SASSSAKLI 8981
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16424-16516 4.02e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 93.33  E-value: 4.02e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16424 PGPPKDLKVSDITRGSCRLSWKMPDDDGGDrIKGYVIEKKTIDGKAWTKVNPNCGS-TAFVVPDLISEQQYFFRVRAENR 16502
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 16503 FGIGPPAETIQRTT 16516
Cdd:cd00063      80 GGESPPSESVTVTT 93
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
31769-32015 4.20e-21

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 100.46  E-value: 4.20e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGT---DQV-LVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05601       9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETlaqEEVsFFEEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGD--NFRLLFTA 31922
Cdd:cd05601      89 LSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGH--IKLADFGSAAKLSSDKtvTSKMPVGT 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PEYYAPEVHQ---HDVVSS---ATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDR 31996
Cdd:cd05601     167 PDYIAPEVLTsmnGGSKGTygvECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKVSESAVDLIKG 246
                           250
                    ....*....|....*....
gi 1958765569 31997 LLVkERKSRMTASEALKHP 32015
Cdd:cd05601     247 LLT-DAKERLGYEGLCCHP 264
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16217-16308 4.30e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.30e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16217 PGPPSCPEVKDKTKSSISLAWKPPaKDGGSPIKGYIVEMQEEGTTDWKKVNEPDklLTACECVVPNLKELRKYRFRVKAV 16296
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTP--GSETSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|..
gi 1958765569 16297 NEAGESEPSDTT 16308
Cdd:cd00063      78 NGGGESPPSESV 89
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
23751-23830 4.38e-21

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 92.65  E-value: 4.38e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23751 YSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIEII 23830
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28664-28751 4.43e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.43e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28664 PDAPGIPEPSNVTGNSITLTWTRPESDGGnEIQHYILERREKKSTRWVKViSKRPISETRFKVTGLVEGNEYEFHVMAEN 28743
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEV-EVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*...
gi 1958765569 28744 AAGVGPAS 28751
Cdd:cd00063      79 GGGESPPS 86
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14395-14487 4.47e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.47e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14395 PGPPTRLEPSDITKDAVTLTWCEPDDDGGsPITGYWVERLDPDTDKWVRCNKMPVKDTTYRVKGLTNKKKYRFRVLAENL 14474
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 14475 AGPGKPSRSTEPI 14487
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20299-20390 4.56e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.56e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20299 PGPPVNVTVKEISKDSAYITWDPPIiDGGSPIINYVVEKRDAERKSWSTVTTECPK-TSFRVSNLEEGKSYFFRVFAENE 20377
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 20378 YGIGDPGETRDAV 20390
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22952-23045 4.74e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.74e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22952 DPPGRPEAIIVTRNSVTLQWKKPTYDGGsKITGYVVEKKELPDGRWMKASFTNIIDTQFEVTGLIEDHRYEFRVIARNAA 23031
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 23032 GVfSEPSESTGAIT 23045
Cdd:cd00063      81 GE-SPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28119-28450 4.77e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 104.31  E-value: 4.77e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28119 SEYVRFSKTENKITLSIKNVKKENGGKYTVIL----DNAVCRNSFPITIITLG-PPSKPKGpIRFDEIKADSAIMSWDIP 28193
Cdd:COG3401     178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVaatdTGGESAPSNEVSVTTPTtPPSAPTG-LTATADTPGSVTLSWDPV 256
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28194 EDDGggeITCYSIEKREASQTNWKMVcSSVARTTFKVSNLVKDSEYQFRVRAENRYGV-SEPlvSNVIVAKHQFRIPGPP 28272
Cdd:COG3401     257 TESD---ATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAP--SNVVSVTTDLTPPAAP 330
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28273 GKPVIYNVTSDGMSLTWDAPvydGGSEVTGFHVEKKERNSILWQRVNTSpISGREYRATGLIEGLDYQFRVYAENSAGLS 28352
Cdd:COG3401     331 SGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNE 406
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28353 SPSDPSKFTLAVSPVDPPGTPDYIDVTRETITLKWNPPLRDGGSKIVAYSIEKRQGSDRWVrcnFTDVSECQYTVSGLSP 28432
Cdd:COG3401     407 SAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA---VPFTTTSSTVTATTTD 483
                           330
                    ....*....|....*...
gi 1958765569 28433 GDRYEFRIIARNAVGTIS 28450
Cdd:COG3401     484 TTTANLSVTTGSLVGGSG 501
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20000-20092 4.78e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 4.78e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20000 PGRCDPPVISNITKDHMTVSWKAPADDGGsPITGYLVEKRETQAVNWTKVNRKPVIERTLKATGLQEGTEYEFRVTAINK 20079
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 20080 AGPGKPSDASKAV 20092
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
8611-8700 5.26e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 5.26e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAG 8690
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8691 RASCTTQLFV 8700
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5978-6066 5.63e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 5.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5978 QIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGS 6057
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  6058 SSCDAYLRV 6066
Cdd:pfam07679    82 AEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30740-30934 5.88e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.93  E-value: 5.88e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30740 PNTPEGpLEYDDIQTRSVRVSWRPPADdggADILGYILERREVPKAAWYTIdSRVRGTSLVVKGLKENVEYHFRVSAENQ 30819
Cdd:COG3401     233 PSAPTG-LTATADTPGSVTLSWDPVTE---SDATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYYRVTAVDA 307
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30820 FGISKPLKSEEPVIPKTPLNPPEPPSNppeVLDVTKSSVSLSWSRPKDDGgsrVTGYYIERKETSTDKWVRHNKTqITTT 30899
Cdd:COG3401     308 AGNESAPSNVVSVTTDLTPPAAPSGLT---ATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAET-VTTT 380
                           170       180       190
                    ....*....|....*....|....*....|....*
gi 1958765569 30900 MYTVTGLVPDAEYQFRIIAQNDVGLSetSPASEPV 30934
Cdd:COG3401     381 SYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEV 413
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
31762-32017 6.03e-21

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 98.87  E-value: 6.03e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIV----------HRCVETSSKKTFMAKF----------VKVKGTDQV-------LVKKEISILNIA 31814
Cdd:cd14200       1 QYKLQSEIGKGSYGVVklaynesddkYYAMKVLSKKKLLKQYgfprrppprgSKAAQGEQAkplapleRVYQEIAILKKL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31815 RHRNILYLHESFESMEE--LVMIFEFISGLDIFERINTSAFelNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQ 31892
Cdd:cd14200      81 DHVNIVKLIEVLDDPAEdnLYMVFDLLRKGPVMEVPSDKPF--SEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31893 trKNSIIKIIEFGQARQLKpGDNFRLLFTA--PEYYAPEV---HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQM 31967
Cdd:cd14200     159 --DDGHVKIADFGVSNQFE-GNDALLSSTAgtPAFMAPETlsdSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILAL 235
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31968 IENIMNAEYTFDEEAfqEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14200     236 HNKIKNKPVEFPEEP--EISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16371-16766 6.88e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.54  E-value: 6.88e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16371 HDIPEDAQLETAENSSVIVIPECTRAHSGKYSITAKNKAGQKTANCRVKVM---DAPGPPKDLKVSDITRGSCRLSWkmp 16447
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTATADTPGSVTLSW--- 253
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16448 DDDGGDRIKGYVIEKKTIDGKAWTKVNPNcGSTAFVVPDLISEQQYFFRVRAENRFGI-GPPAETIQRTTArdpIYPPDL 16526
Cdd:COG3401     254 DPVTESDATGYRVYRSNSGDGPFTKVATV-TTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTD---LTPPAA 329
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16527 PIKLKIGLITKNTVHLSWKPPKndgGSPVTHYIVECLAWDPTGKKKEAwrqcnrRDVEELEFTVEDLVEGGEYEFRVKAV 16606
Cdd:COG3401     330 PSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIA------ETVTTTSYTDTGLTPGTTYYYKVTAV 400
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16607 NEAGV-SKPSATVGPVTVKDQTCPPSIELKEFMEVEEGTDVNIVAKIKGVPFPTLTW--FKAPPKKPDSKEPVVYDTHVN 16683
Cdd:COG3401     401 DAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVlaDGGDTGNAVPFTTTSSTVTAT 480
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16684 KQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTASKEMRLNVLGRPGPPVGPIKFESISADQMTLSWLPPKDDGGSKITN 16763
Cdd:COG3401     481 TTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560

                    ...
gi 1958765569 16764 YVI 16766
Cdd:COG3401     561 VSG 563
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20101-20189 7.06e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 7.06e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20101 PGPPAFPKVYDTTRSSVSLSWgKPAFDGGSPIIGYLVEVKRADSDHWVRCNlPEKLQKTRFEVTGLMENTEYQFRVYAVN 20180
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*....
gi 1958765569 20181 KIGYSDPSD 20189
Cdd:cd00063      79 GGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23249-23338 7.27e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 7.27e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23249 PDAPKAPEVTAVTKDSMIVVWERPASDGGsEILGYVLEKRDKEGIRWTRCHKRLIGELRLRVTGLLENHNYEFRVSAENA 23328
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|
gi 1958765569 23329 AGLSEPSPPS 23338
Cdd:cd00063      80 GGESPPSESV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26495-26585 7.63e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 7.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26495 PSPPTSLEITSVTKDSMTLCWSRPETDGGsDISGYIIERREKNSLRWMRVNKKPVYDLRVKSTGLREGCEYEYRVFAENA 26574
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 26575 AGLSLPSDTSP 26585
Cdd:cd00063      80 GGESPPSESVT 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
23844-24121 7.63e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.54  E-value: 7.63e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23844 FDEVSAESITLSWNPPLYTGGCQITNYIVQKRDTTTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENRYGQSFAleS 23923
Cdd:COG3401     144 GAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--S 221
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23924 EPIVAQYPYKEPGPPGTPFVTAVSKDSMVVQWHEPINNGgspVIGYHLERKERNSILWTKVNKTIihDTQFKALNLEEGI 24003
Cdd:COG3401     222 NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGT 296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24004 EYEFRVYAENivGVGKASKNS-ECYVARDPcDPPGTPEAIIVKR---NEITLQWTkPVYDGGsmITGYIVEKRDLPEGRW 24079
Cdd:COG3401     297 TYYYRVTAVD--AAGNESAPSnVVSVTTDL-TPPAAPSGLTATAvgsSSITLSWT-ASSDAD--VTGYNVYRSTSGGGTY 370
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 24080 MKASFTnVIETQFTVSGLTEDQRYEFRVIAKNAAGAISKPSD 24121
Cdd:COG3401     371 TKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSE 411
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18216-18307 7.86e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 7.86e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18216 PSPPGKPVVTDITENAATVSWTLPKSDGGsPITGYYVERREI-TGKWVRVNKTPIADLKFRVTGLYEGNTYEFRVFAENL 18294
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 18295 AGLSNPSPSSDPI 18307
Cdd:cd00063      80 GGESPPSESVTVT 92
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
31757-32019 8.16e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 99.94  E-value: 8.16e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYMIAEDLGRGEFGIVHRCVETSSKKTfmakfVKVK--------GTDQVLVKKEISIL-NIARHRNILYLHESF- 31826
Cdd:cd07852       3 KHILRRYEILKKLGKGAYGIVWKAIDKKTGEV-----VALKkifdafrnATDAQRTFREIMFLqELNDHPNIIKLLNVIr 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31827 -ESMEELVMIFEFI-SGL------DIFERINtsafelneREVVSYvrQVCEALEFLHSQNIGHFDIRPENIIYqtrkNS- 31897
Cdd:cd07852      78 aENDKDIYLVFEYMeTDLhaviraNILEDIH--------KQYIMY--QLLKALKYLHSGGVIHRDLKPSNILL----NSd 143
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31898 -IIKIIEFGQARQLKPGDNFRLLFTAPEY-----Y-APEV----HQHdvvSSATDMWSLGTLVYVLLSG----------- 31955
Cdd:cd07852     144 cRVKLADFGLARSLSQLEEDDENPVLTDYvatrwYrAPEIllgsTRY---TKGVDMWSVGCILGEMLLGkplfpgtstln 220
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31956 -------------------INPFLAETnqqMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07852     221 qlekiievigrpsaediesIQSPFAAT---MLESLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPY 297

                    ...
gi 1958765569 32017 LKQ 32019
Cdd:cd07852     298 VAQ 300
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21091-21174 1.03e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 1.03e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21091 EISNVTKNTATVSWKRPiDDGGSEITGYHVERREKKGLRWVRATKTPVSDLRCKVTGLQEGNTYEFRVSAENRAGIGPPS 21170
Cdd:cd00063       8 RVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86

                    ....
gi 1958765569 21171 DASN 21174
Cdd:cd00063      87 ESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28269-28361 1.04e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 1.04e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28269 PGPPGKPVIYNVTSDGMSLTWDAPVYDGGsEVTGFHVEKKERNSILWQRVNTSPISGREYRATGLIEGLDYQFRVYAENS 28348
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 28349 AGLSSPSDPSKFT 28361
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25116-25209 1.15e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 91.79  E-value: 1.15e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25116 DPPGRPEAIIITRNSVTLKWKKPTYDGGsKITGYIVEKKDLPDGRWMKASFTNVVETEFTVTGLVEDQRYEFRVIARNAA 25195
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 25196 dNFSEPSESSGAIT 25209
Cdd:cd00063      81 -GESPPSESVTVTT 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
32201-32293 1.20e-20

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 91.71  E-value: 1.20e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:cd20951      81 IHGEASSSASVVV 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15807-15899 1.21e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 91.79  E-value: 1.21e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15807 PTSPERLTYTERTKSTITLDWKEPRSDGGsPIQGYIIEKRRHDKPDFERVNKRLCPTTSFLVDNLDEHQMYEFRVKAVND 15886
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 15887 IGESEPSLPLNVV 15899
Cdd:cd00063      80 GGESPPSESVTVT 92
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
31762-32012 1.53e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 96.97  E-value: 1.53e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK--VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd08219       1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRlpKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAFEL-NEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd08219      81 DGGDLMQKIKLQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLT--QNGKVKLGDFGSARLLTSPGAYAC 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAP-EVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTfdeEAFQEISLEAMDFIDRL 31997
Cdd:cd08219     159 TYVGTPYYVPpEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYK---PLPSHYSYELRSLIKQM 235
                           250
                    ....*....|....*
gi 1958765569 31998 LVKERKSRMTASEAL 32012
Cdd:cd08219     236 FKRNPRSRPSATTIL 250
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
31757-32018 1.55e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 98.51  E-value: 1.55e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYMIaedLGRGEFGIVHRCVETSSKKTFMAKFV------KVKGTDQVLVKKEIsiLNIARHRNILYLHESFESME 31830
Cdd:cd05632       1 KNTFRQYRV---LGKGGFGEVCACQVRATGKMYACKRLekkrikKRKGESMALNEKQI--LEKVNSQFVVNLAYAYETKD 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 ELVMIFEFISGLDI-FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ 31909
Cdd:cd05632      76 ALCLVLTIMNGGDLkFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGH--IRISDLGLAVK 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENImNAEYTFDEEAFQ-EISL 31988
Cdd:cd05632     154 IPEGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEV-DRRVLETEEVYSaKFSE 232
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 31989 EAMDFIDRLLVKERKSRM-----TASEALKHPWLK 32018
Cdd:cd05632     233 EAKSICKMLLTKDPKQRLgcqeeGAGEVKRHPFFR 267
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
31769-31971 1.80e-20

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 96.45  E-value: 1.80e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRcvetsskktfmakfVKVKGTDqVLVK----------------KEISILNIARHRNILYLHESFESMEEL 31832
Cdd:cd13999       1 IGSGSFGEVYK--------------GKWRGTD-VAIKklkveddndellkefrREVSILSKLRHPNIVQFIGACLSPPPL 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31833 VMIFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKP 31912
Cdd:cd13999      66 CIVTEYMPGGSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLD--ENFTVKIADFGLSRIKNS 143
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 GDNFRLLFT-APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENI 31971
Cdd:cd13999     144 TTEKMTGVVgTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAV 203
I-set pfam07679
Immunoglobulin I-set domain;
4760-4849 1.90e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.16  E-value: 1.90e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4760 PTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEAG 4839
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4840 SQTSVGELIV 4849
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
9182-9271 1.99e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 91.16  E-value: 1.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9182 PVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAG 9261
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  9262 SDTSKCKVTI 9271
Cdd:pfam07679    81 EAEASAELTV 90
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
31742-32014 2.04e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 98.95  E-value: 2.04e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31742 ETREVTMTKASHSKTKELYEKYMIaedLGRGEFGIVHRCVETSSKKTFMAKFVKvkgTDQVLVKKEIS-------ILNIA 31814
Cdd:cd05594       9 EEMEVSLTKPKHKVTMNDFEYLKL---LGKGTFGKVILVKEKATGRYYAMKILK---KEVIVAKDEVAhtltenrVLQNS 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31815 RHRNILYLHESFESMEELVMIFEFISGLDIFerintsaFELNEREVVS------YVRQVCEALEFLHSQ-NIGHFDIRPE 31887
Cdd:cd05594      83 RHPFLTALKYSFQTHDRLCFVMEYANGGELF-------FHLSRERVFSedrarfYGAEIVSALDYLHSEkNVVYRDLKLE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31888 NIIYQtrKNSIIKIIEFGQARQ-LKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ 31966
Cdd:cd05594     156 NLMLD--KDGHIKITDFGLCKEgIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 233
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31967 MIENIMNAEYTFDeeafQEISLEAMDFIDRLLVKERKSRM-----TASEALKH 32014
Cdd:cd05594     234 LFELILMEEIRFP----RTLSPEAKSLLSGLLKKDPKQRLgggpdDAKEIMQH 282
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
31741-32018 2.11e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 97.87  E-value: 2.11e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31741 DETREVTMTKASHSKTKELYEKYmiaEDLGRGEFGIVHRCVETSSKKTFMAKFVKV-KGTDQVLVKKEISILNIARHRNI 31819
Cdd:cd06655       2 EEIMEKLRTIVSIGDPKKKYTRY---EKIGQGASGTVFTAIDVATGQEVAIKQINLqKQPKKELIINEILVMKELKNPNI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31820 LYLHESFESMEELVMIFEFISGLDIFERINTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiI 31899
Cdd:cd06655      79 VNFLDSFLVGDELFVVMEYLAGGSLTDVVTETC--MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGS--V 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31900 KIIEFGQARQLKPGDNFR-LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIEnIMNAEYTF 31978
Cdd:cd06655     155 KLTDFGFCAQITPEQSKRsTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTP 233
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|
gi 1958765569 31979 DEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd06655     234 ELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
31762-32015 2.30e-20

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 96.61  E-value: 2.30e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV-LVKKEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd06613       1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFeIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 G---LDIFERINTsafeLNEREVvSYV-RQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNF 31916
Cdd:cd06613      81 GgslQDIYQVTGP----LSELQI-AYVcRETLKGLAYLHSTGKIHRDIKGANILLTEDGD--VKLADFGVSAQLTATIAK 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFTAPEYY-APEVHQ---HDVVSSATDMWSLGtlvyvlLSGINpfLAETNQQMIE-NIMNAEYTFDEEAFQEISLEA- 31990
Cdd:cd06613     154 RKSFIGTPYWmAPEVAAverKGGYDGKCDIWALG------ITAIE--LAELQPPMFDlHPMRALFLIPKSNFDPPKLKDk 225
                           250       260       270
                    ....*....|....*....|....*....|..
gi 1958765569 31991 -------MDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd06613     226 ekwspdfHDFIKKCLTKNPKKRPTATKLLQHP 257
I-set pfam07679
Immunoglobulin I-set domain;
6353-6438 2.31e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.78  E-value: 2.31e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6353 PVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVG 6432
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*.
gi 1958765569  6433 SDTCIC 6438
Cdd:pfam07679    81 EAEASA 86
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
13703-13795 2.38e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 91.02  E-value: 2.38e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13703 PGPPLNVTITDVNRFGVSLTWEPPEYDGGaEITNYVIELRDKTSIRWDTAMTVRAEDLSATVTDVVEGQEYSFRVRAQNR 13782
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 13783 IGVGKPSAATPFV 13795
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
13511-13891 2.56e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.00  E-value: 2.56e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13511 PPKIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTKTVDTTAEQTSFRILEAKKED-----KGRYKIVLQN 13585
Cdd:COG3401     134 GAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDiepgtTYYYRVAATD 213
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13586 KHGK---AEGFINLQVIDVPGPVRNLEVTETFDGEVSLAWEEPLTDGgskIIGYVVERRDIKRKTWVLVTDRADScEFTV 13662
Cdd:COG3401     214 TGGEsapSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTTT-SYTD 289
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13663 TGLQKgGVEYLFRVSARNRVG-TGEPVETdspVEARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEydgGAEITNYVIEl 13741
Cdd:COG3401     290 TGLTN-GTTYYYRVTAVDAAGnESAPSNV---VSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVY- 361
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13742 RDKTSIRWDTAMTVRAEDLSATVTDVVEGQEYSFRVRAQNRIGVGkpSAATPFVKV----ADPIERPSPPVNLSASEQTQ 13817
Cdd:COG3401     362 RSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSAttasAASGESLTASVDAVPLTDVA 439
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 13818 SSVQLTWEPPLKDGGSPILGYIIERQEEGKDNWIRCN-MKPVPELTYKVTGLQKGNKYLYRVSAENAAGVSDPSE 13891
Cdd:COG3401     440 GATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTvTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGA 514
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14696-14787 2.95e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.63  E-value: 2.95e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14696 PGPPYALTVVDVTKRHVDLKWEPPKNDGGrPIQRYIIEKKEKLGTRWVKAGKTSGPDCNFRVTDVIEGTEVQFQVRAENE 14775
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 14776 AGVGHPSEPTEI 14787
Cdd:cd00063      80 GGESPPSESVTV 91
I-set pfam07679
Immunoglobulin I-set domain;
8424-8511 3.03e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.39  E-value: 3.03e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8424 IVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKD 8503
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*...
gi 1958765569  8504 SCTVSIQV 8511
Cdd:pfam07679    83 EASAELTV 90
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
31759-32019 3.15e-20

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 96.78  E-value: 3.15e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYmiaEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARH---RNILYLHESFESMEELV 31833
Cdd:cd06917       2 LYRRL---ELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVsdIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLW 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIfeRINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPG 31913
Cdd:cd06917      79 IIMDYCEGGSI--RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN--VKLCDFGVAASLNQN 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTAPEYY-APEVHQHDVVSSA-TDMWSLGTLVYVLLSGINPFLAETNQQMIENIM-NAEYTFDEEAFqeiSLEA 31990
Cdd:cd06917     155 SSKRSTFVGTPYWmAPEVITEGKYYDTkADIWSLGITTYEMATGNPPYSDVDALRAVMLIPkSKPPRLEGNGY---SPLL 231
                           250       260
                    ....*....|....*....|....*....
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd06917     232 KEFVAACLDEEPKDRLSADELLKSKWIKQ 260
I-set pfam07679
Immunoglobulin I-set domain;
4387-4476 3.21e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.39  E-value: 3.21e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4467 ADICQAELTI 4476
Cdd:pfam07679    81 EAEASAELTV 90
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
31763-32017 3.26e-20

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 96.21  E-value: 3.26e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK----EISILNIARHRNILYLHESFESME-ELVMIFE 31837
Cdd:cd14163       2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRflprELQIVERLDHKNIIHVYEMLESADgKIYLVME 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKnsiIKIIEFGQARQL-KPGDNF 31916
Cdd:cd14163      82 LAEDGDVFDCV-LHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT---LKLTDFGFAKQLpKGGREL 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFT-APEYYAPEVHQ---HDvvSSATDMWSLGTLVYVLLSGINPFLAETNQQMienIMNAEYTFDEEAFQEISLEAMD 31992
Cdd:cd14163     158 SQTFCgSTAYAAPEVLQgvpHD--SRKGDIWSMGVVLYVMLCAQLPFDDTDIPKM---LCQQQKGVSLPGHLGVSRTCQD 232
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14163     233 LLKRLLEPDMVLRPSIEEVSWHPWL 257
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
14212-14292 3.45e-20

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 89.96  E-value: 3.45e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14212 LTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVN 14291
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 14292 V 14292
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16524-16622 3.58e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.63  E-value: 3.58e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16524 PDLPIKLKIGLITKNTVHLSWKPPKNDGGsPVTHYIVEClawdpTGKKKEAWRQCNRRDVEELEFTVEDLVEGGEYEFRV 16603
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEY-----REKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRV 74
                            90
                    ....*....|....*....
gi 1958765569 16604 KAVNEAGVSKPSATVGPVT 16622
Cdd:cd00063      75 RAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17229-17322 3.62e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.63  E-value: 3.62e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17229 PERPEDLEVKEVTKNTVTLTWNPPKYDGGsEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNI 17308
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 17309 VGQGKPSFCTKPIT 17322
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26198-26291 3.87e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 3.87e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26198 DPPGQPEVTNITRKSVSLKWSKPRYDGGaKITGYIVERRELPDGRWLKCNFTNVQETYFEVTELTEDQRYEFRVFARNAA 26277
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 26278 dSVSEPSESTGPIT 26291
Cdd:cd00063      81 -GESPPSESVTVTT 93
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
31769-32018 3.88e-20

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 96.66  E-value: 3.88e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFV------KVKGTDQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05605       8 LGKGGFGEVCACQVRATGKMYACKKLekkrikKRKGEAMALNEKQI--LEKVNSRFVVSLAYAYETKDALCLVLTIMNGG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DI-FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd05605      86 DLkFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGH--VRISDLGLAVEIPEGETIRGRVG 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKE 32001
Cdd:cd05605     164 TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQLLQKD 243
                           250       260
                    ....*....|....*....|..
gi 1958765569 32002 RKSRM-----TASEALKHPWLK 32018
Cdd:cd05605     244 PKTRLgcrgeGAEDVKSHPFFK 265
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
31769-32035 3.91e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 97.76  E-value: 3.91e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKvKG-------TDQVLVKKEI-SILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd05589       7 LGRGHFGKVLLAEYKPTGELFAIKALK-KGdiiardeVESLMCEKRIfETVNSARHPFLVNLFACFQTPEHVCFVMEYAA 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSAFelNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQ-LKPGDNFRLL 31919
Cdd:cd05589      86 GGDLMMHIHEDVF--SEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDT--EGYVKIADFGLCKEgMGFGDRTSTF 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLLV 31999
Cdd:cd05589     162 CGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYP----RFLSTEAISIMRRLLR 237
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 1958765569 32000 KERKSRMTASE-----ALKHP------WLKQRMDRVSTKVIRTLRHR 32035
Cdd:cd05589     238 KNPERRLGASErdaedVKKQPffrnidWEALLARKIKPPFVPTIKSP 284
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
31769-31973 3.95e-20

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 96.07  E-value: 3.95e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK-VKGT----DQVLVKKEISILNIARHRNIL-YLHESFESmEELVMIFEFISG- 31841
Cdd:cd00192       3 LGEGAFGEVYKGKLKGGDGKTVDVAVKtLKEDasesERKDFLKEARVMKKLGHPNVVrLLGVCTEE-EPLYLVMEYMEGg 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 -LDIFERINTSAFE------LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKnsIIKIIEFGQARQLKPGD 31914
Cdd:cd00192      82 dLLDFLRKSRPVFPspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDL--VVKISDFGLSRDIYDDD 159
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31915 NFRLLFTAPE---YYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIMN 31973
Cdd:cd00192     160 YYRKKTGGKLpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRK 222
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1417-1507 3.98e-20

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 90.25  E-value: 3.98e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:cd05744      81 GENSFNAELVV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31634-31725 3.99e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 3.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31634 PDPPRGVKVSDVSRDSVNLTWTEPASDGGsKVTNYIVEKCATTAERWLRV--GQARETRYTVVNLFGKTSYQFRVIAENK 31711
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 31712 FGLSKPSEPSEPTV 31725
Cdd:cd00063      80 GGESPPSESVTVTT 93
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
31769-32018 4.00e-20

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 97.46  E-value: 4.00e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHrCVETSSKKTFMAkfVKVKGTDQVL---------VKKEISILNiARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05592       3 LGKGSFGKVM-LAELKGTNQYFA--IKALKKDVVLedddvectmIERRVLALA-SQHPFLTHLFCTFQTESHLFFVMEYL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSA-FELNEREVvsYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd05592      79 NGGDLMFHIQQSGrFDEDRARF--YGAEIICGLQFLHSRGIIYRDLKLDNVLLD--REGHIKIADFGMCKENIYGENKAS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTA-PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRL 31997
Cdd:cd05592     155 TFCGtPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYP----RWLTKEAASCLSLL 230
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31998 LVKERKSRM-----TASEALKHPWLK 32018
Cdd:cd05592     231 LERNPEKRLgvpecPAGDIRDHPFFK 256
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
31769-32019 4.08e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 96.63  E-value: 4.08e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFV------KVKGTDQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05630       8 LGKGGFGEVCACQVRATGKMYACKKLekkrikKRKGEAMALNEKQI--LEKVNSRFVVSLAYAYETKDALCLVLTLMNGG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DI-FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd05630      86 DLkFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGH--IRISDLGLAVHVPEGQTIKGRVG 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKE 32001
Cdd:cd05630     164 TVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKD 243
                           250       260
                    ....*....|....*....|...
gi 1958765569 32002 RKSRM-----TASEALKHPWLKQ 32019
Cdd:cd05630     244 PAERLgcrggGAREVKEHPLFKK 266
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31763-32018 4.11e-20

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 95.69  E-value: 4.11e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV---KVKG----TDQVLVKKEISIL----NIARHRNILYLHESFESMEE 31831
Cdd:cd14101       2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQIsrnRVQQwsklPGVNPVPNEVALLqsvgGGPGHRGVIRLLDWFEIPEG 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEF-ISGLDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiIKIIEFGQARQL 31910
Cdd:cd14101      82 FLLVLERpQHCQDLFDYI-TERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGD-IKLIDFGSGATL 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KpgDNFRLLFTAPEYYAP----EVHQHDVVSSAtdMWSLGTLVYVLLSGINPFlaetnqQMIENIMNAEYTFDeeafQEI 31986
Cdd:cd14101     160 K--DSMYTDFDGTRVYSPpewiLYHQYHALPAT--VWSLGILLYDMVCGDIPF------ERDTDILKAKPSFN----KRV 225
                           250       260       270
                    ....*....|....*....|....*....|..
gi 1958765569 31987 SLEAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd14101     226 SNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14000-14089 4.27e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 4.27e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14000 PSAPKELKFSDVTKDSVHLTWEPPDDDGGsPLTGYVVEKRDMSRKTWTKVM-DFVTDLEFTVPDLVQGKEYLFKVCARNK 14078
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 14079 CGPGEPAYTDE 14089
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30444-30537 4.57e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 4.57e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30444 PGPPETLQIFDISRDGMTLTWYPPEDDGGsQVTGYIIERKEVRADRWVRVNKVPVTMTRYRSTGLIEGLEYEHRVTAINA 30523
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 30524 RGTGKPSRPSKPTV 30537
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
4573-4663 4.60e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.01  E-value: 4.60e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4573 PSFVKKVDPSYLMlPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDA 4652
Cdd:pfam07679     1 PKFTQKPKDVEVQ-EGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  4653 GSDSCSTEVVI 4663
Cdd:pfam07679    80 GEAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
20900-20981 4.94e-20

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 89.57  E-value: 4.94e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20900 LTVKAGDSIVLSaISILGKPLPKSSWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEHVKV 20979
Cdd:cd05748       2 IVVRAGESLRLD-IPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 20980 SV 20981
Cdd:cd05748      81 KV 82
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
31769-32019 5.24e-20

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 97.29  E-value: 5.24e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK----VKGTDQVLVKKEISILNIAR-HRNILYLHESFESMEELVMIFEFISGLD 31843
Cdd:cd05590       3 LGKGSFGKVMLARLKESGRLYAVKVLKkdviLQDDDVECTMTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiiKIIEFGQARQ-LKPGDNFRLLFTA 31922
Cdd:cd05590      83 LMFHIQKSR-RFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHC--KLADFGMCKEgIFNGKTTSTFCGT 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLLVKER 32002
Cdd:cd05590     160 PDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYP----TWLSQDAVDILKAFMTKNP 235
                           250       260
                    ....*....|....*....|...
gi 1958765569 32003 KSRMTA------SEALKHPWLKQ 32019
Cdd:cd05590     236 TMRLGSltlggeEAILRHPFFKE 258
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
14084-14516 5.41e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.85  E-value: 5.41e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14084 PAYTDEPVNMSAPATVPDPPENVKWRD-RTANSIFLTWDPPKNDGGSRIKGYIVEKCPRGSDKWVACGEPVPDTKMEVTG 14162
Cdd:COG3401     119 SPAVGTATTATAVAGGAATAGTYALGAgLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGD 198
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14163 LEEGKWYAYRVKALNRQGASKPSKPTEEIQAVDTQEAPeifldvkllAGLTVKAGTkielPATVTgkpepkITWTKAD-- 14240
Cdd:COG3401     199 IEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAP---------TGLTATADT----PGSVT------LSWDPVTes 259
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14241 -----TLLR-PDQRITIENVPKKSTVTITDSKRSDTGTY--IIEAVNVCG---RATAVVEVNV-LDKPGPPAAFDITDVT 14308
Cdd:COG3401     260 datgyRVYRsNSGDGPFTKVATVTTTSYTDTGLTNGTTYyyRVTAVDAAGnesAPSNVVSVTTdLTPPAAPSGLTATAVG 339
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14309 NESCLLTWNPPRDDGgskITNYVVERKATDSDVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAENMYGVG----EPVQAT 14384
Cdd:COG3401     340 SSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNEsapsEEVSAT 416
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14385 PIIAKYQFDPPGPPTR-LEPSDITKDAVTLTWCEPDDDGGSPITGYWVERLDPDTDKWVrcNKM-PVKDTTYRVKGLTNK 14462
Cdd:COG3401     417 TASAASGESLTASVDAvPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSS--TVTaTTTDTTTANLSVTTG 494
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 14463 KKYRFRVLAENLAGPGKPSRSTEPILIKDPIDPPWPPGKPTVKDIGKTSLVLNW 14516
Cdd:COG3401     495 SLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLIT 548
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
31763-32016 5.69e-20

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 96.19  E-value: 5.69e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK--VKGTDQVLVKKEISILN-IARHRNILYLHESF--ESMEELVMIFE 31837
Cdd:cd07831       1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKkhFKSLEQVNNLREIQALRrLSPHPNILRLIEVLfdRKTGRLALVFE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISgLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqtrKNSIIKIIEFGQARqlkpGDNFR 31917
Cdd:cd07831      81 LMD-MNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI---KDDILKLADFGSCR----GIYSK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFT---------APE------YYAPEVhqhdvvssatDMWSLGTLVYVLLSgINPFLAETNQ----QMIENIM------ 31972
Cdd:cd07831     153 PPYTeyistrwyrAPEclltdgYYGPKM----------DIWAVGCVFFEILS-LFPLFPGTNEldqiAKIHDVLgtpdae 221
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31973 ---------NAEYTFDEEAFQEI-------SLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07831     222 vlkkfrksrHMNYNFPSKKGTGLrkllpnaSAEGLDLLKKLLAYDPDERITAKQALRHPY 281
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
104-194 5.74e-20

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 89.79  E-value: 5.74e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLD---FQISQEGDLYSLLIAEAYPEDSGTYSVNATN 180
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569   181 SVGRATSTADLLVQ 194
Cdd:cd20951      81 IHGEASSSASVVVE 94
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
31769-32018 5.89e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 96.06  E-value: 5.89e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFV------KVKGTDQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05577       1 LGRGGFGEVCACQVKATGKMYACKKLdkkrikKKKGETMALNEKII--LEKVSSPFIVSLAYAFETKDKLCLVLTLMNGG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DI-FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd05577      79 DLkYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH--VRISDLGLAVEFKGGKKIKGRVG 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVV-SSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVK 32000
Cdd:cd05577     157 THGYMAPEVLQKEVAyDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQK 236
                           250       260
                    ....*....|....*....|...
gi 1958765569 32001 ERKSRM-----TASEALKHPWLK 32018
Cdd:cd05577     237 DPERRLgcrggSADEVKEHPFFR 259
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25298-25978 6.61e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 6.61e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25298 VGGTKTIPITVKVLDRPGPPEGPLKVTGVTAEKCYLAWNPPLQDGGASISHYIIEKRETSRLSWTQVSTEVQALNYKVTK 25377
Cdd:COG3401      52 PGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAV 131
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25378 LLPGNEYIFRVMAVNKYGVGEPLESEPVIACNPYKLPGPPSTPEASAITKDSMVLTWTRPVDDGGAEIEgyilekrdkeg 25457
Cdd:COG3401     132 AGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIE----------- 200
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25458 irwtkcnkktltdlrfrvtgltEGHSYEFRVAAENAAGVGEPSEPsvfYRACDALYPPGPPSNPKVTDTSRSSVSLAWNK 25537
Cdd:COG3401     201 ----------------------PGTTYYYRVAATDTGGESAPSNE---VSVTTPTTPPSAPTGLTATADTPGSVTLSWDP 255
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25538 PIYDGgapVRGYVIELKEAAADEWTTCTppsGLQGKQFTVTKLKENTEYNFRICAFNTEGVGEPAtipgsvvaqermeap 25617
Cdd:COG3401     256 VTESD---ATGYRVYRSNSGDGPFTKVA---TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAP--------------- 314
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25618 eieldadlrkvvtlraSATlrlfVTIKGRPEPevkwekaegilteraqievtssytmlvidnvtrfdsgrynltlennsg 25697
Cdd:COG3401     315 ----------------SNV----VSVTTDLTP------------------------------------------------ 326
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25698 sktafvnvrvldsPSAPVNLTVREVKKDSVTLSWEPPLidgGAKVTNYIVEKRETTRKAYATITNNCTKTTFKIENLQEG 25777
Cdd:COG3401     327 -------------PAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPG 390
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25778 CSYYFRVLASNEYGIG------LPAETTEPVKVSEPPLPPGRVTLVDVTRNTATIKWEKPEsDGGSKITGYVVEMQTKGS 25851
Cdd:COG3401     391 TTYYYKVTAVDAAGNEsapseeVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNP-GVSAAVLADGGDTGNAVP 469
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25852 EKWSTCTQVKTLEAT---ISGLTAGEEYVFRVAAVNEKGRSDPRQLGVPVVA-KDIEIKPSVELPFNTFNVKANDQLKID 25927
Cdd:COG3401     470 FTTTSSTVTATTTDTttaNLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGgAPDGTPNVTGASPVTVGASTGDVLITD 549
                           650       660       670       680       690
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 25928 IPFKGRPQATV---AWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYE 25978
Cdd:COG3401     550 LVSLTTSASSSvsgAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLVL 603
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25515-25603 7.22e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.48  E-value: 7.22e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25515 PGPPSNPKVTDTSRSSVSLAWNKPIYDGGaPVRGYVIELKEAAADEWTTCTPPSGLQgKQFTVTKLKENTEYNFRICAFN 25594
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAVN 78

                    ....*....
gi 1958765569 25595 TEGVGEPAT 25603
Cdd:cd00063      79 GGGESPPSE 87
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
18722-18805 7.50e-20

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 7.50e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18722 VLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDatDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAGSfvAYA 18801
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQ--PLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGE--KSA 76

                    ....
gi 1958765569 18802 TVNV 18805
Cdd:cd05748      77 TINV 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14296-14387 7.65e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.48  E-value: 7.65e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14296 PGPPAAFDITDVTNESCLLTWNPPRDDGGsKITNYVVERKATDSDVWHKLSST-VKDTNFKATKLTPNKEYIFRVAAENM 14374
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 14375 YGVGEPVQATPII 14387
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
32201-32293 7.78e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 89.24  E-value: 7.78e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPgddDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS---SDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:pfam07679    78 SAGEAEASAELTV 90
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
31763-32017 7.83e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 94.80  E-value: 7.83e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFG--IVHRCVETSS----KKTFMAKFVKVKGTDqvlVKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd08221       2 YIPVRVLGRGAFGeaVLYRKTEDNSlvvwKEVNLSRLSEKERRD---ALNEIDILSLLNHDNIITYYNHFLDGESLFIEM 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFELNEREVVS-YVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLkpGDN 31915
Cdd:cd08221      79 EYCNGGNLHDKIAQQKNQLFPEEVVLwYLYQIVSAVSHIHKAGILHRDIKTLNIFLT--KADLVKLGDFGISKVL--DSE 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFT---APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAeTNQ-QMIENIMNAEYTFDEEAFqeiSLEAM 31991
Cdd:cd08221     155 SSMAESivgTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDA-TNPlRLAVKIVQGEYEDIDEQY---SEEII 230
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd08221     231 QLVHDCLHQDPEDRPTAEELLERPLL 256
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21771-21863 7.88e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.48  E-value: 7.88e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21771 PGPPGTPQVTAVTKDSMTISWHEPLSDGGsPILGYHIERKERNGILWQTVSKALVPGNIFKSTGLTDGIAYEFRVIAENM 21850
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 21851 AGKSKPSKPSEPT 21863
Cdd:cd00063      80 GGESPPSESVTVT 92
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
31769-32017 8.17e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 97.07  E-value: 8.17e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKvkgTDQVLVKKEIS-------ILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd05593      23 LGKGTFGKVILVREKASGKYYAMKILK---KEVIIAKDEVAhtltesrVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 99
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFerintsaFELNEREVVS------YVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQ-LKPGD 31914
Cdd:cd05593     100 GELF-------FHLSRERVFSedrtrfYGAEIVSALDYLHSGKIVYRDLKLENLMLD--KDGHIKITDFGLCKEgITDAA 170
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFI 31994
Cdd:cd05593     171 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSADAKSLL 246
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31995 DRLLVKERKSRM-----TASEALKHPWL 32017
Cdd:cd05593     247 SGLLIKDPNKRLgggpdDAKEIMRHSFF 274
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24273-24538 9.77e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.08  E-value: 9.77e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24273 TSRLAWTVVASEVVTNSLKVTKLLEGNEYIFRIMAVNKYGVGEPleSAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWN 24352
Cdd:COG3401     177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD 254
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24353 RPDSDGgseIIGYIVEKRDRSGIRWIKCNKrrITDLRLRVTGLTEDHEYEFRVSAENAAGV-GEPS-PATVYYKacdpVF 24430
Cdd:COG3401     255 PVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSnVVSVTTD----LT 325
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24431 KPGPPTNVHIVDTTKNSITLAWGKPiydGGSDILGYVVEICKADEEEWQIVTpqTGLRVTRFEISKLIEHQEYKIRVCAL 24510
Cdd:COG3401     326 PPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ETVTTTSYTDTGLTPGTTYYYKVTAV 400
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 24511 NKVGLGEAASVPGTVKPEDKLEAPELDL 24538
Cdd:COG3401     401 DAAGNESAPSEEVSATTASAASGESLTA 428
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21380-21469 1.01e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.01e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21380 PGPVLNLRPTDITKDSVTLHWDLPLiDGGSRITNYIVEKREATRKSYSTVTTKCHK-CTYKVTGLTEGCEYFFRVMAENE 21458
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 21459 YGIGEPTETTE 21469
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27679-27770 1.04e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.04e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27679 PGPPAKIRIADSTKSSITLGWSKPVYDGGsDVTGYVVEMRQGEEEEWTIVSTKgEARTTEYVVSNLKPGVNYYFQVSAVN 27758
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVT-PGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|..
gi 1958765569 27759 CAGQGEPITMTE 27770
Cdd:cd00063      79 GGGESPPSESVT 90
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
31761-32018 1.08e-19

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 95.56  E-value: 1.08e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT-DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd06656      19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 98
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFR-L 31918
Cdd:cd06656      99 AGGSLTDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM--DGSVKLTDFGFCAQITPEQSKRsT 174
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIEnIMNAEYTFDEEAFQEISLEAMDFIDRLL 31998
Cdd:cd06656     175 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQNPERLSAVFRDFLNRCL 253
                           250       260
                    ....*....|....*....|
gi 1958765569 31999 VKERKSRMTASEALKHPWLK 32018
Cdd:cd06656     254 EMDVDRRGSAKELLQHPFLK 273
I-set pfam07679
Immunoglobulin I-set domain;
6636-6725 1.08e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.85  E-value: 1.08e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6636 PSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAG 6715
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6716 SDECRALLTV 6725
Cdd:pfam07679    81 EAEASAELTV 90
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
31769-32019 1.11e-19

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 95.45  E-value: 1.11e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFG---IVHRCVETSSKKTFMAKFVK-------VKGTDQVLVKKEIsILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd05613       8 LGTGAYGkvfLVRKVSGHDAGKLYAMKVLKkativqkAKTAEHTRTERQV-LEHIRQSPFLVTLHYAFQTDTKLHLILDY 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd05613      87 INGGELFTHLSQRE-RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDS--SGHVVLTDFGLSKEFLLDENERA 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 --LFTAPEYYAPEVHQ-----HDvvsSATDMWSLGTLVYVLLSGINPFL--AETNQQ--MIENIMNAEYTFDeeafQEIS 31987
Cdd:cd05613     164 ysFCGTIEYMAPEIVRggdsgHD---KAVDWWSLGVLMYELLTGASPFTvdGEKNSQaeISRRILKSEPPYP----QEMS 236
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1958765569 31988 LEAMDFIDRLLVKERKSRM-----TASEALKHPWLKQ 32019
Cdd:cd05613     237 ALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQK 273
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
19868-20474 1.13e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 99.69  E-value: 1.13e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19868 FSVNRKDSGDYTITAENSSGSKSATIKLKVLDKPGPPASVKINKMYADRAMLSWEPPLEDGGSEITNYIVDKRETSRPNW 19947
Cdd:COG3401      36 ILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSD 115
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19948 AQVSATVPitsctvekliegheyqfricaENKYGVGDPIFTEPVIAKNPYDPPGRCDPPVISNITKD-HMTVSWKAPADD 20026
Cdd:COG3401     116 EVPSPAVG---------------------TATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASsVAGAGVVVSPDT 174
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20027 GGSPITGYLVEKRETQAVNWTKVNRKPviertlkatglqeGTEYEFRVTAINKAGPGKPSDASKAVYAQDPlypPGPPAF 20106
Cdd:COG3401     175 SATAAVATTSLTVTSTTLVDGGGDIEP-------------GTTYYYRVAATDTGGESAPSNEVSVTTPTTP---PSAPTG 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20107 PKVYDTTRSSVSLSWGKPAFDGgspIIGYLVEVKRADSDHWVRCNlpeKLQKTRFEVTGLMENTEYQFRVYAVNKIG-YS 20185
Cdd:COG3401     239 LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVA---TVTTTSYTDTGLTNGTTYYYRVTAVDAAGnES 312
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20186 DPSDVpdkhcpkdilippegeldaelrktlilragvtmrlyVPVKGRPPPkitwskpnvnlrerigldikstdfdtflrc 20265
Cdd:COG3401     313 APSNV------------------------------------VSVTTDLTP------------------------------ 326
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20266 envnkydagkyiltlenscgkkeytivvkvldtPGPPVNVTVKEISKDSAYITWDPPiidGGSPIINYVVEKRDAERKSW 20345
Cdd:COG3401     327 ---------------------------------PAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTY 370
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20346 STVTTECPKTSFRVSNLEEGKSYFFRVFAENEYGI-GDPGETRDAVKASETPGPVVDLKVLAVTksSCTIGWKKPRSDGG 20424
Cdd:COG3401     371 TKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVP--LTDVAGATAAASAA 448
                           570       580       590       600       610
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20425 SRITGYVVDFLTEENKWQRVMKSLSLQYSTKDLKEGKEYTFRVSAENENG 20474
Cdd:COG3401     449 SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVG 498
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29854-29944 1.15e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.15e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29854 PGPPSAPRVVDTTKSSISLAWTKPMYDGGtDIIGYVLEMQEKDTDQWCRVhTNTTIRNNEFTVPDLKMGQKYSFRVAAVN 29933
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEV-EVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|.
gi 1958765569 29934 AKGMSDYSETT 29944
Cdd:cd00063      79 GGGESPPSESV 89
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
28480-28560 1.15e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 88.42  E-value: 1.15e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIE--RRMNMEITDVlgSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEIT 28557
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKetGRVQIETTAS--STSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    ...
gi 1958765569 28558 VKV 28560
Cdd:cd05748      80 VKV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
18032-18112 1.15e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 88.42  E-value: 1.15e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18032 LVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLT 18111
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 18112 V 18112
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30943-31028 1.16e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.16e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30943 PSQPGELEILSISKDSVILQWEKPECDGGkEILGYWVEYRQSGDSAWKKSNKERIKDRQFTIGGLLEATEYEFRVFAENE 31022
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 31023 TGLSRP 31028
Cdd:cd00063      80 GGESPP 85
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
31769-32008 1.19e-19

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 96.23  E-value: 1.19e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMakfVKVKGTDQVLVKKEISilNIARHRNILY----------LHESFESMEELVMIFEF 31838
Cdd:cd05575       3 IGKGSFGKVLLARHKAEGKLYA---VKVLQKKAILKRNEVK--HIMAERNVLLknvkhpflvgLHYSFQTKDKLYFVLDY 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFerintsaFELNEREVVS------YVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ-LK 31911
Cdd:cd05575      78 VNGGELF-------FHLQRERHFPeprarfYAAEIASALGYLHSLNIIYRDLKPENILLDSQGH--VVLTDFGLCKEgIE 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAM 31991
Cdd:cd05575     149 PSDTTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRT----NVSPSAR 224
                           250
                    ....*....|....*..
gi 1958765569 31992 DFIDRLLVKERKSRMTA 32008
Cdd:cd05575     225 DLLEGLLQKDRTKRLGS 241
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30850-30935 1.24e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 89.09  E-value: 1.24e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30850 VLDVTKSSVSLSWSRPKDDGGsRVTGYYIERKETSTDKWVRHNKTQITTTMYTVTGLVPDAEYQFRIIAQNDVGLSETSP 30929
Cdd:cd00063       9 VTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSE 87

                    ....*.
gi 1958765569 30930 ASEPVV 30935
Cdd:cd00063      88 SVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15097-15184 1.56e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.56e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15097 DVEVHNPTAKAMTITWKPPLYDGGsKIMGYIIEKLAKGEDRWKRCNEHLVPVLTYTAKGLEEGKEYQFRVRAENAAGIGE 15176
Cdd:cd00063       6 NLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84

                    ....*...
gi 1958765569 15177 PSRATPPT 15184
Cdd:cd00063      85 PSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26887-26970 1.57e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.57e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26887 PSPPEKLGVTSVSKDSVSLSWLKPEHDGGsRILHYVVEALEKGQKNWVKCAV--VKTTHHVVSGLREGHEYFFRVFAENQ 26964
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 26965 AGLSDP 26970
Cdd:cd00063      80 GGESPP 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
14908-14988 1.57e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 88.03  E-value: 1.57e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14908 IVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASINVK 14987
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 14988 V 14988
Cdd:cd05748      82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18908-19001 1.59e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.59e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18908 PGRPDPPEVTKVSKEEMTVVWNAPEYDGGKsITGYYLEKKEKHAVRWVPVNKSAIPERRLKVQNLLPGHEYQFRVKAENE 18987
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 18988 VGIGEPSLPSRPVV 19001
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14596-14682 1.59e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.59e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14596 PSPPRWLEVINITKNTADLKWTVPEKDGGsPITNYIVEKRDVRRKGWQTVDTT-VKDTKCTVTPLTEGSLYVFRVAAENA 14674
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 14675 IGQSDYTE 14682
Cdd:cd00063      80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14797-14888 1.62e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 1.62e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14797 PSPPLDLHVTDAGRKHIAIAWKPPEKNGGsPIIGYHVEMCPVGTEKWMRVNSRPIKDLKFKVeEGVVPDKEYVLRVRAVN 14876
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTL-TGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|..
gi 1958765569 14877 AVGVSDPSEISE 14888
Cdd:cd00063      79 GGGESPPSESVT 90
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
31769-32021 1.91e-19

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 94.80  E-value: 1.91e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTD----QVLvkKEISILNIARHRNILYLHESF--ESMEELVMIFEFISG- 31841
Cdd:cd06621       9 LGEGAGGSVTKCRLRNTKTIFALKTITTDPNPdvqkQIL--RELEINKSCASPYIVKYYGAFldEQDSSIGIAMEYCEGg 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 -LD-IFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSIiKIIEFGQARQLkpGDNFRLL 31919
Cdd:cd06621      87 sLDsIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILL-TRKGQV-KLCDFGVSGEL--VNSLAGT 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQ--------QMIENIMNAEYTFDEEAFQEISLEA 31990
Cdd:cd06621     163 FTGTSYYmAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiellSYIVNMPNPELKDEPENGIKWSESF 242
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWLKQRM 32021
Cdd:cd06621     243 KDFIEKCLEKDGTRRPGPWQMLAHPWIKAQE 273
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24725-24808 2.25e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 2.25e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24725 PSPPGKVTLTDVSQTSASLMWEKPEHDGGsRILGYVVEMQPKGTEKWSVV--AESKVCSAVVSGLSSGQEYQFRVKAYNE 24802
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 24803 KGKSDP 24808
Cdd:cd00063      80 GGESPP 85
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
31769-32018 2.29e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 95.01  E-value: 2.29e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVhRCVETSSKKTFMAkfVKVKGTDQVLVKKEIS-------ILNIARHRNIL-YLHESFESMEELVMIFEFIS 31840
Cdd:cd05620       3 LGKGSFGKV-LLAELKGKGEYFA--VKALKKDVVLIDDDVEctmvekrVLALAWENPFLtHLYCTFQTKEHLFFVMEFLN 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSA-FELneREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd05620      80 GGDLMFHIQDKGrFDL--YRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLD--RDGHIKIADFGMCKENVFGDNRAST 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTA-PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENImnaeyTFDEEAFQE-ISLEAMDFIDRL 31997
Cdd:cd05620     156 FCGtPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI-----RVDTPHYPRwITKESKDILEKL 230
                           250       260
                    ....*....|....*....|..
gi 1958765569 31998 LVKERKSRMTASEALK-HPWLK 32018
Cdd:cd05620     231 FERDPTRRLGVVGNIRgHPFFK 252
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25808-25891 2.32e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 2.32e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25808 PLPPGRVTLVDVTRNTATIKWEKPESDGGsKITGYVVEMQTKGSEKWSTCT--QVKTLEATISGLTAGEEYVFRVAAVNE 25885
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 25886 KGRSDP 25891
Cdd:cd00063      80 GGESPP 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18854-19394 2.37e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.92  E-value: 2.37e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18854 VWSTYSANVLTPGATVTRLIEGNEYIFRVRAENKIGTGPPTESKPVIAKTkYDRPGRPDPPEVTKVSKEEMTVVWNAPEY 18933
Cdd:COG3401      88 PPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAAT-AGTYALGAGLYGVDGANASGTTASSVAGA 166
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18934 DGGKSITGYYLEKKEKHAVRWVPVNKSAIPERrlkvqnLLPGHEYQFRVKAENEVGIgepSLPSRPVVAKDPIEPPGPPT 19013
Cdd:COG3401     167 GVVVSPDTSATAAVATTSLTVTSTTLVDGGGD------IEPGTTYYYRVAATDTGGE---SAPSNEVSVTTPTTPPSAPT 237
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19014 NFKVVDTTKNSITLAWgKPVYDGGApiIGYVVEmRpkiaDASPDEGWKRCNAAAQLvrmEFTVTSLDENQEYEFRVCAQN 19093
Cdd:COG3401     238 GLTATADTPGSVTLSW-DPVTESDA--TGYRVY-R----SNSGDGPFTKVATVTTT---SYTDTGLTNGTTYYYRVTAVD 306
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19094 QVGIgrpaelkeairpkeileppeidldasmrklvvvragcpirlfaivRGRPAPKVTwrkvgidnvvrkgqvdlvdtma 19173
Cdd:COG3401     307 AAGN---------------------------------------------ESAPSNVVS---------------------- 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19174 flvipnstrddsgkysltlVNPAGEKavfvnvkvldtPGPVSDLKVSDVTKTSCHVSWAPPEndgGSPVTHYIVEKREAE 19253
Cdd:COG3401     320 -------------------VTTDLTP-----------PAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSG 366
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19254 RKTWSTVTPEVKKTSFNVTNLVPGNEYFFRVTAVNEYGP-GVPTDVPKPVLASDPLSEPDPPRKVEVTEMTKNSATLAWL 19332
Cdd:COG3401     367 GGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAAS 446
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 19333 PPLRDGGAKIDGYIISYREEDQP--ADRWTEYSVVKDLSLIITGLKEGKKYKFRVAARNAVGVS 19394
Cdd:COG3401     447 AASNPGVSAAVLADGGDTGNAVPftTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
I-set pfam07679
Immunoglobulin I-set domain;
7482-7570 2.53e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.08  E-value: 2.53e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7482 RIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGK 7561
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  7562 SSCTVSVHV 7570
Cdd:pfam07679    82 AEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
8518-8607 2.58e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 2.58e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAG 8597
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  8598 SDECSAPLTV 8607
Cdd:pfam07679    81 EAEASAELTV 90
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
31761-32015 2.59e-19

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 95.72  E-value: 2.59e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG------TDQVLVKKEIsiLNIARHRNILYLHESFESMEELVM 31834
Cdd:cd05610       4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADminknmVHQVQAERDA--LALSKSPFIVHLYYSLQSANNVYL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQA-----RQ 31909
Cdd:cd05610      82 VMEYLIGGDVKSLLHIYGY-FDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGH--IKLTDFGLSkvtlnRE 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LK--------------------PG------------------------------DNFRLLFTaPEYYAPEVHQHDVVSSA 31939
Cdd:cd05610     159 LNmmdilttpsmakpkndysrtPGqvlslisslgfntptpyrtpksvrrgaarvEGERILGT-PDYLAPELLLGKPHGPA 237
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31940 TDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfQEISLEAMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd05610     238 VDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGE-EELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
31761-32015 2.73e-19

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 93.58  E-value: 2.73e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHR--CVETSSKktfmakfVKVK-------GTDQVLVKKEISILNIARHRNILYLHESFESMEE 31831
Cdd:cd06610       1 DDYELIEVIGSGATAVVYAayCLPKKEK-------VAIKridlekcQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISG---LDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQAR 31908
Cdd:cd06610      74 LWLVMPLLSGgslLDIMKSSYPRGG-LDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGS--VKIADFGVSA 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31909 QL-KPGDN-FRLLFT---APEYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGINPFlaeTNQQMIENIM----NAEYTF 31978
Cdd:cd06610     151 SLaTGGDRtRKVRKTfvgTPCWMAPEVmEQVRGYDFKADIWSFGITAIELATGAAPY---SKYPPMKVLMltlqNDPPSL 227
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1958765569 31979 DEEA-FQEISLEAMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd06610     228 ETGAdYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHK 265
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17105-17508 2.89e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.54  E-value: 2.89e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17105 YSLLAKNEGGERKKTIIVDVLDVPGPVGIP--FLSDNLTNDSCKLTWFSPEDDGgspITNYVIQKREADRRAWTPVTyTV 17182
Cdd:COG3401     207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVA-TV 282
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17183 TRQNATVQGLIQGKSYFFRIAAENSIG-MGPFVETpnALVIRDpITVPERPEDLEVKEVTKNTVTLTWNPPKydgGSEII 17261
Cdd:COG3401     283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNV--VSVTTD-LTPPAAPSGLTATAVGSSSITLSWTASS---DADVT 356
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17262 NYVLESRLIGTEKFHKVTnDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQGkpSFCTKPITCKDELAPPTLDLDfRDKLT 17341
Cdd:COG3401     357 GYNVYRSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASGESLT-ASVDA 432
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17342 VRVGEAFALTGRYSGkPKPKVDWFKDEADVlEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFCQVNVV 17421
Cdd:COG3401     433 VPLTDVAGATAAASA-ASNPGVSAAVLADG-GDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17422 DRPGPPVGPVVFDeVTKEYMVISWKPPLDDGGSEITNYIIEKKELGKDIWMPVTSASAKTTCKVPKLLEGKDYIFRIHAE 17501
Cdd:COG3401     511 VIGASAAAAVGGA-PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589

                    ....*..
gi 1958765569 17502 NLYGISD 17508
Cdd:COG3401     590 NDVAGVH 596
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14100-14189 3.07e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.94  E-value: 3.07e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14100 PDPPENVKWRDRTANSIFLTWDPPKNDGGsRIKGYIVEKCPRGSDKWVACG-EPVPDTKMEVTGLEEGKWYAYRVKALNR 14178
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 14179 QGASKPSKPTE 14189
Cdd:cd00063      80 GGESPPSESVT 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
19878-20192 3.08e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.54  E-value: 3.08e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19878 YTITAENSSGSKSATIKLKVLDK---PGPPASVKINKMYADRAMLSWEPPLEDGgseITNYIVDKRETSRPNWAQVsATV 19954
Cdd:COG3401     207 YRVAATDTGGESAPSNEVSVTTPttpPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKV-ATV 282
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19955 PITSCTVEKLIEGHEYQFRICAENKYGVGDPiFTEPVIAKNPYDPPgrcDPPV---ISNITKDHMTVSWKAPADdggSPI 20031
Cdd:COG3401     283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESA-PSNVVSVTTDLTPP---AAPSgltATAVGSSSITLSWTASSD---ADV 355
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20032 TGYLVEKRETQAVNWTKVNrKPVIERTLKATGLQEGTEYEFRVTAINKAGPGkpSDASKAVYAQdPLYPPGPPAFPKVYD 20111
Cdd:COG3401     356 TGYNVYRSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSAT-TASAASGESLTASVD 431
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20112 TTRSSVSLSWGKPAFDGGSPIIGYLVEVKRADSDhwvrcNLPEKLQKTRFEVTGLMENTEYQFRVYAVNKIGYSDPSDVP 20191
Cdd:COG3401     432 AVPLTDVAGATAAASAASNPGVSAAVLADGGDTG-----NAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVT 506

                    .
gi 1958765569 20192 D 20192
Cdd:COG3401     507 N 507
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24034-24127 3.17e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.94  E-value: 3.17e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24034 DPPGTPEAIIVKRNEITLQWTKPVYDGGSmITGYIVEKRDLPEGRWMKASFTNVIETQFTVSGLTEDQRYEFRVIAKNAA 24113
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 24114 GaISKPSDSTGPIT 24127
Cdd:cd00063      81 G-ESPPSESVTVTT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
25228-25310 3.29e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 87.26  E-value: 3.29e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25228 VIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAaRMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPIT 25307
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETG-RVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    ...
gi 1958765569 25308 VKV 25310
Cdd:cd05748      80 VKV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
19817-19897 3.33e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 87.26  E-value: 3.33e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 19897 V 19897
Cdd:cd05748      82 V 82
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
31769-32018 3.41e-19

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 93.95  E-value: 3.41e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVhrCVET---SSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd06658      30 IGEGSTGIV--CIATekhTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALT 107
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSafELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQL-KPGDNFRLLFTAPE 31924
Cdd:cd06658     108 DIVTHT--RMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTS--DGRIKLSDFGFCAQVsKEVPKRKSLVGTPY 183
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31925 YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfQEISLEAMDFIDRLLVKERKS 32004
Cdd:cd06658     184 WMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDS-HKVSSVLRGFLDLMLVREPSQ 262
                           250
                    ....*....|....
gi 1958765569 32005 RMTASEALKHPWLK 32018
Cdd:cd06658     263 RATAQELLQHPFLK 276
I-set pfam07679
Immunoglobulin I-set domain;
1801-1889 3.73e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 3.73e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDG-IHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGgTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  1880 VTEHKVKLEI 1889
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20688-20781 3.77e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.55  E-value: 3.77e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20688 PDAPPPPNIVDVRHDSVSLTWTDPKKTGGsPITGYHIEFKERNSLLWKRANKTPIRMKDFKVTGLTEGLEYEFRVMAINL 20767
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 20768 AGVGKPSLPSEPVV 20781
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
5137-5225 3.84e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 3.84e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5137 FTEKLEPsQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGS 5216
Cdd:pfam07679     3 FTQKPKD-VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  5217 DHCTSIVIV 5225
Cdd:pfam07679    82 AEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18043-18353 3.89e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.15  E-value: 3.89e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18043 PAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTgeYQLTVSNAAGTKTVAVHLTVLDVPGPPTGP 18122
Cdd:COG3401     159 TASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYY--YRVAATDTGGESAPSNEVSVTTPTTPPSAP 236
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18123 INIL--DVTPEYMTISWQPPKDDGgspVINYIVEKQDTRKGTWGVVsAGSSKLKLKVPHLQKGCEYVFRVKAENKMGV-G 18199
Cdd:COG3401     237 TGLTatADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeS 312
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18200 PPLDSIPTVAKHkfSPPSPPGKPVVTDITENAATVSWTlPKSDGGspITGYYVERREI-TGKWVRVNKTpIADLKFRVTG 18278
Cdd:COG3401     313 APSNVVSVTTDL--TPPAAPSGLTATAVGSSSITLSWT-ASSDAD--VTGYNVYRSTSgGGTYTKIAET-VTTTSYTDTG 386
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 18279 LYEGNTYEFRVFAENLAGLSnpSPSSDPIKAcRPIKPPGPPINPKLKDKTKESADLVWTKPLSDGGSPILGYVVE 18353
Cdd:COG3401     387 LTPGTTYYYKVTAVDAAGNE--SAPSEEVSA-TTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVL 458
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
31761-32018 4.02e-19

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 94.02  E-value: 4.02e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT-DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd06654      20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 99
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFR-L 31918
Cdd:cd06654     100 AGGSLTDVVTETC--MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM--DGSVKLTDFGFCAQITPEQSKRsT 175
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIEnIMNAEYTFDEEAFQEISLEAMDFIDRLL 31998
Cdd:cd06654     176 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALY-LIATNGTPELQNPEKLSAIFRDFLNRCL 254
                           250       260
                    ....*....|....*....|
gi 1958765569 31999 VKERKSRMTASEALKHPWLK 32018
Cdd:cd06654     255 EMDVEKRGSAKELLQHQFLK 274
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22398-22866 4.54e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 97.77  E-value: 4.54e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22398 GRPAPEVKWAREHGESLDKASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFVNVRVLDTPGPPQNLKIKEVTK 22477
Cdd:COG3401      68 GTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGL 147
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22478 TSVTLTWEPPLLDGGSKIKNYIVEKRESTRKAYSTVATNCHKTSWKIDQL--QEGCSYYFRVLAENEYGIGLPAETAESV 22555
Cdd:COG3401     148 YGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGdiEPGTTYYYRVAATDTGGESAPSNEVSVT 227
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22556 KASERPLPPGKITLMDVTRNSVSLSWEKPEhdgGSRILGYIVEMQSKGSDKWATCATVKVTEATITGLIQGEEYSFRVSA 22635
Cdd:COG3401     228 TPTTPPSAPTGLTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTA 304
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22636 QNEKGI-SDPrqlSVPV-IAKDLVIPPAFKLLfntfTVLAGEDLKIDVPFIGRPTPTVTWHK---DDVPLKQTTRVNAES 22710
Cdd:COG3401     305 VDAAGNeSAP---SNVVsVTTDLTPPAAPSGL----TATAVGSSSITLSWTASSDADVTGYNvyrSTSGGGTYTKIAETV 377
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22711 TENNSLLTIKEAcrEDVGHYTVKLTNSAG---------EATETLNVIVLDKPGPPTGPVKMDEVTADSVTLSWEPPKYDG 22781
Cdd:COG3401     378 TTTSYTDTGLTP--GTTYYYKVTAVDAAGnesapseevSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSA 455
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22782 GSSINNYIVEKRDTSTTAWQIVSATVARTTIKASRLKTGCeyqfrIAAENRYGKSTYLNSEPVIAQYPFKVPGPPGTPFV 22861
Cdd:COG3401     456 AVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGS-----LVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNV 530

                    ....*
gi 1958765569 22862 TLASK 22866
Cdd:COG3401     531 TGASP 535
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27578-27670 4.58e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 4.58e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27578 PGPPSIPEVTKITKNSMTVVWNRPTvDGGSEINGYFLEKRDKKSLAWLKVLKETIRDTRQKVTGLTENSDYQYRVCAVNA 27657
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 27658 AGMGPFSEPSDFY 27670
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22561-22644 4.67e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 4.67e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22561 PLPPGKITLMDVTRNSVSLSWEKPEHDGGsRILGYIVEMQSKGSDKWATCAT--VKVTEATITGLIQGEEYSFRVSAQNE 22638
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 22639 KGISDP 22644
Cdd:cd00063      80 GGESPP 85
I-set pfam07679
Immunoglobulin I-set domain;
6259-6349 4.75e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.31  E-value: 4.75e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPA 6338
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  6339 GSTSCSTKVIV 6349
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22853-22945 5.15e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.15e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22853 PGPPGTPFVTLASKDSMEVQWhEPVSDGGSRVIGYHLERKERNSILWVKLNKTPIPQTKFKTTGLEEGIEYEFRVSAENI 22932
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 22933 VGIGKPSKPSECY 22945
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22464-22553 5.68e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.68e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22464 PGPPQNLKIKEVTKTSVTLTWEPPLLDGGsKIKNYIVEKRESTRKAYSTVATNCHK-TSWKIDQLQEGCSYYFRVLAENE 22542
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 22543 YGIGLPAETAE 22553
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18809-18900 5.84e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.84e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18809 PGPVRNLKIADVSSDRCTIRWDPPEDDGGcEIQNYILEKCESKRMVWSTYSANVLT-PGATVTRLIEGNEYIFRVRAENK 18887
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 18888 IGTGPPTESKPVI 18900
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26790-26881 5.90e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.17  E-value: 5.90e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26790 PGPPANITVREVTKETAVLSWDVPENDGGaPVKNYHIEKREASKKAWVSV-TNNCSRLSYKVTNLQEGAVYYFRVSGENE 26868
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 26869 FGVGVPAETKEGV 26881
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20299-20381 5.90e-19

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 86.51  E-value: 5.90e-19
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20299 PGPPVNVTVKEISKDSAYITWDPPIIDGG-SPIINYVVEKRDaERKSWSTVTTECPKTSFRVSNLEEGKSYFFRVFAENE 20377
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  20378 YGIG 20381
Cdd:smart00060    80 AGEG 83
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
31729-32018 5.94e-19

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 95.46  E-value: 5.94e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31729 DKTRAMNYDEEVDETRE-------VTMTKASHSKTKELY---EKYMIAEDLGRGEFGIVHRCVETSSKKTF----MAKFV 31794
Cdd:cd05622      31 DGLDALVYDLDFPALRKnknidnfLSRYKDTINKIRDLRmkaEDYEVVKVIGRGAFGEVQLVRHKSTRKVYamklLSKFE 110
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31795 KVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERIntSAFELNEREVVSYVRQVCEALEFL 31874
Cdd:cd05622     111 MIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLM--SNYDVPEKWARFYTAEVVLALDAI 188
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31875 HSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFR--LLFTAPEYYAPEVHQHD----VVSSATDMWSLGTL 31948
Cdd:cd05622     189 HSMGFIHRDVKPDNMLLD--KSGHLKLADFGTCMKMNKEGMVRcdTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVF 266
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31949 VYVLLSGINPFLAETNQQMIENIMNAE--YTFDEEAfqEISLEAMDFIDRLLVKE--RKSRMTASEALKHPWLK 32018
Cdd:cd05622     267 LYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPDDN--DISKEAKNLICAFLTDRevRLGRNGVEEIKRHLFFK 338
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20787-20876 6.70e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.78  E-value: 6.70e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20787 DPPGKPEVISVTRNSVTLIWTEPKYDGGhKLTGYIVEKRDLPSKSWMKANHVNVPDCAFTVTDLVEGGKYEFRIRAKNTA 20866
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|
gi 1958765569 20867 GaISAPSEST 20876
Cdd:cd00063      81 G-ESPPSESV 89
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
24146-24227 6.84e-19

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 86.49  E-value: 6.84e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24146 TIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNV 24225
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 24226 KV 24227
Cdd:cd05748      81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24207-24483 7.13e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 97.38  E-value: 7.13e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24207 QYILRASNVAGSKSFPVNVKVLDRPGPPEGP--VQVTGVTSEKCTLAWSPPlqdGGSDISHYVVEKRETSRLAWTVVAsE 24284
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVA-T 281
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24285 VVTNSLKVTKLLEGNEYIFRIMAVNKYGVGEPLeSAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWNRPDSDGgseIIG 24364
Cdd:COG3401     282 VTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAP-SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD---VTG 357
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24365 YIVEKRDRSGIRWIKCNKrRITDLRLRVTGLTEDHEYEFRVSAENAAGVGEPSPATVyykACDPVFKPGPPTNVHIVDTT 24444
Cdd:COG3401     358 YNVYRSTSGGGTYTKIAE-TVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEV---SATTASAASGESLTASVDAV 433
                           250       260       270
                    ....*....|....*....|....*....|....*....
gi 1958765569 24445 KNSITLAWGKPIYDGGSDILGYVVEICKADEEEWQIVTP 24483
Cdd:COG3401     434 PLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTT 472
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25711-25800 7.60e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.78  E-value: 7.60e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25711 PSAPVNLTVREVKKDSVTLSWEPPLIDGGaKVTNYIVEKRETTRKAYATI-TNNCTKTTFKIENLQEGCSYYFRVLASNE 25789
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 25790 YGIGLPAETTE 25800
Cdd:cd00063      80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22268-22355 7.60e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.78  E-value: 7.60e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22268 PGPPGNPRVLDTSRSSISIAWNKPIYDGGsEITGYMVEIALPEEDEWQVVTPPAGlKATSYTITNLIENQEYKIRIYAMN 22347
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*...
gi 1958765569 22348 SEGLGEPA 22355
Cdd:cd00063      79 GGGESPPS 86
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26000-26091 7.90e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.78  E-value: 7.90e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26000 PGPPGPIRIDEVSCDNVSISWTPPEYDGGcQISNYIVEKRETTSTTWQVV-SQAVARTSIKIVRLTTGSEYQFRVCAENR 26078
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 26079 YGKSSYSESSAVV 26091
Cdd:cd00063      80 GGESPPSESVTVT 92
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
31762-32015 7.99e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 92.22  E-value: 7.99e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRcvetsskktfmakfVKVKGTDQVLVKKEIS-----------------ILNIARHRNIL-YLH 31823
Cdd:cd08217       1 DYEVLETIGKGSFGTVRK--------------VRRKSDGKILVWKEIDygkmsekekqqlvsevnILRELKHPNIVrYYD 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31824 ESFESMEELVMIF-EFISGLD----IFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIG-----HFDIRPENIIYQT 31893
Cdd:cd08217      67 RIVDRANTTLYIVmEYCEGGDlaqlIKKCKKENQY-IPEEFIWKIFTQLLLALYECHNRSVGggkilHRDLKPANIFLDS 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31894 RKNsiIKIIEFGQARQLKPGDNFRLLFTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIM 31972
Cdd:cd08217     146 DNN--VKLGDFGLARVLSHDSSFAKTYVGTPYYmSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIK 223
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|...
gi 1958765569 31973 NAEYTFDEEAFqeiSLEAMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd08217     224 EGKFPRIPSRY---SSELNEVIKSMLNVDPDKRPSVEELLQLP 263
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23643-23734 1.01e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.40  E-value: 1.01e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23643 PQPPGKITVDDVTRNSVSLSWTKPEHDGGsKIIQYIVEMQAKNTDKWSEC--ARVKSLEAVITSLTQGEEYLFRVIAVNE 23720
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 23721 KGRSDPRSLAVPIT 23734
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16729-16821 1.05e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.40  E-value: 1.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16729 PGPPVGpIKFESISADQMTLSWLPPKDDGGsKITNYVIEKREANRKTWVRVSSEP-KECMYTIPKLLEGHEYVFRIMAQN 16807
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 16808 KYGIGEPLDSEPET 16821
Cdd:cd00063      79 GGGESPPSESVTVT 92
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
31759-32017 1.08e-18

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 93.40  E-value: 1.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVkgtdqvlVKK-------EISIL-NIARHR-----NILYLHES 31825
Cdd:cd14134      10 LTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRN-------VEKyreaakiEIDVLeTLAEKDpngksHCVQLRDW 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31826 FESMEELVMIFEfISGLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENII-------------- 31890
Cdd:cd14134      83 FDYRGHMCIVFE-LLGPSLYDFLKKNNYGpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlvdsdyvkvynpkk 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31891 -YQTR--KNSIIKIIEFGQA-------------RQlkpgdnfrllftapeYYAPEVhqhdVV----SSATDMWSLGTLVY 31950
Cdd:cd14134     162 kRQIRvpKSTDIKLIDFGSAtfddeyhssivstRH---------------YRAPEV----ILglgwSYPCDVWSIGCILV 222
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31951 VLLSGINPF--------LAetnqqMIENIM---------------NAEYT------FDEEA----------------FQE 31985
Cdd:cd14134     223 ELYTGELLFqthdnlehLA-----MMERILgplpkrmirrakkgaKYFYFyhgrldWPEGSssgrsikrvckplkrlMLL 297
                           330       340       350
                    ....*....|....*....|....*....|....*
gi 1958765569 31986 ISLEAMDFID---RLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14134     298 VDPEHRLLFDlirKMLEYDPSKRITAKEALKHPFF 332
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22730-23290 1.12e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 96.61  E-value: 1.12e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22730 YTVKLTNSAGEATETLNVIVLDKPGPPTGPVKMDEVTADSVTLSWEPPKYDGGSSInnyivekRDTSTTAWQIVSATVAR 22809
Cdd:COG3401      25 ALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVA-------AVAVAAAPPTATGLTTL 97
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22810 TTIKASRLKTGCEYQFRIAAENRYGKSTYLNSEPVIAQYPFKVPGPPGTPFVTLASKDSMEVQWHEPVSDGGSRVIGYhl 22889
Cdd:COG3401      98 TGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTS-- 175
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22890 erkeRNSILWVKLNKTPIPQTKFKTTGLEEGIEYEFRVSAENIVGIGKPSKPSECYAAHDPCDPPGRPEAIIVTRNSVTL 22969
Cdd:COG3401     176 ----ATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTL 251
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22970 QWKKPTYDGgskITGYVVEKKELPDGRWMKASFTNiiDTQFEVTGLIEDHRYEFRVIARNAAGVFSEPSEstgaitarde 23049
Cdd:COG3401     252 SWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSN---------- 316
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23050 vepprismdpkykdtvvvqagesfkidadiygkpipttqwvkgdqelsstarleikttdfatslsvkdavrvdsgnyilk 23129
Cdd:COG3401         --------------------------------------------------------------------------------
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23130 aknvagekSVTVNVKVLdRPGPPEGpVAISGVTAEKCMLAWKPPLqdgGSDIINYIVERRETSRLVWTLVDANVQTLSCK 23209
Cdd:COG3401     317 --------VVSVTTDLT-PPAAPSG-LTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYT 383
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23210 VTKLLEGNEYIFRIMAVNKYGVgEPLESEPLIAKNPFVVPDAPKAPEVTAVT------KDSMIVVWERPASDGGSEILGY 23283
Cdd:COG3401     384 DTGLTPGTTYYYKVTAVDAAGN-ESAPSEEVSATTASAASGESLTASVDAVPltdvagATAAASAASNPGVSAAVLADGG 462

                    ....*..
gi 1958765569 23284 VLEKRDK 23290
Cdd:COG3401     463 DTGNAVP 469
I-set pfam07679
Immunoglobulin I-set domain;
1417-1507 1.19e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 86.16  E-value: 1.19e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVViKEDGTQSLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVT-YEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19604-19697 1.26e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.01  E-value: 1.26e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19604 PSEPKNARVTKVNKDCIFVAWDRPDSDGGsPITGYLIERKERNSLLWVKANDTIVRSTEYPCAGLVEGLEYSFRIYALNK 19683
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 19684 AGSSPPSKPTEYVT 19697
Cdd:cd00063      80 GGESPPSESVTVTT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
21982-22063 1.35e-18

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 85.72  E-value: 1.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21982 TITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNV 22061
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                    ..
gi 1958765569 22062 KV 22063
Cdd:cd05748      81 KV 82
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
31769-32016 1.40e-18

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 91.26  E-value: 1.40e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK------EISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd06625       8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEvkalecEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKP---GDNFRLL 31919
Cdd:cd06625      88 SVKDEIKAYG-ALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGN--VKLGDFGASKRLQTicsSTGMKSV 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENImnAEYTFDEEAFQEISLEAMDFIDRLLV 31999
Cdd:cd06625     165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKI--ATQPTNPQLPPHVSEDARDFLSLIFV 242
                           250
                    ....*....|....*..
gi 1958765569 32000 KERKSRMTASEALKHPW 32016
Cdd:cd06625     243 RNKKQRPSAEELLSHSF 259
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
31762-32013 1.42e-18

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 91.56  E-value: 1.42e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV------KGTDQVLvkKEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd08224       1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIfemmdaKARQDCL--KEIDLLQQLNHPNIIKYLASFIENNELNIV 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAFE---LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQL-- 31910
Cdd:cd08224      79 LELADAGDLSRLIKHFKKQkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITA--NGVVKLGDLGLGRFFss 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNFRLLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQM--IENIMNAEYT-FDEEAFqeiS 31987
Cdd:cd08224     157 KTTAAHSLVGT-PYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNLYslCKKIEKCEYPpLPADLY---S 232
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31988 LEAMDFIDRLLVKERKSRMTASEALK 32013
Cdd:cd08224     233 QELRDLVAACIQPDPEKRPDISYVLD 258
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
17741-17818 1.52e-18

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 85.33  E-value: 1.52e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17741 HIKVGDTLRLSAIIKGVPFPKVTWKKEDRE--APTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd05748       3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPlkETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
20749-21250 1.61e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 96.22  E-value: 1.61e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20749 VTGLTEGLEYEFRVMAINLAGVGKPSLPSEPVVALDPIDPPGKPEVISVTRNSVTLIWTEPKYDGghkLTGYIVEKRDLP 20828
Cdd:COG3401     196 GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSG 272
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20829 SKSWMKANHVNVPdcAFTVTDLVEGGKYEFRIRAKNTAGAISApsestgtiickdeyeaptivldptikdgltvkagdsi 20908
Cdd:COG3401     273 DGPFTKVATVTTT--SYTDTGLTNGTTYYYRVTAVDAAGNESA------------------------------------- 313
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20909 vlsaisilgkplpksswskagkdirPSDIAQITSTPTssmltvkyatrkdageytitatnpfgtkeehvkvsvldVPGPP 20988
Cdd:COG3401     314 -------------------------PSNVVSVTTDLT--------------------------------------PPAAP 330
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20989 GPIEISNVSAEKATLTWTPPLedgGSPIKAYVLEKRETSRLLWTVVSEDIQACRHVVTKLIQGNEYLFRVSAVNHYGKgE 21068
Cdd:COG3401     331 SGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-E 406
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21069 PVQSEPVkMVDRFGPPGPPGKPEISNVTKNTATVSWKRPIDDGGSEITGYHVERREKKGLRWVRATKTPV---------- 21138
Cdd:COG3401     407 SAPSEEV-SATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSStvtatttdtt 485
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21139 -SDLRCKVTGLQEGNTYEFRVSAENRAGIGPPSDASNPVLMKDVAYPPGPPSNAHVTDTTKKSASLAWGKPHYD--GGLE 21215
Cdd:COG3401     486 tANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSsvSGAG 565
                           490       500       510
                    ....*....|....*....|....*....|....*
gi 1958765569 21216 ITGYVVEHQKVGDDAWIKDTTGTALRITQFVVPDL 21250
Cdd:COG3401     566 LGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTL 600
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
31761-32018 1.67e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 92.19  E-value: 1.67e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:PLN00009      2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPStaiREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISgLDIFERINTSA-FELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiIKIIEFGQARQLK-PGDN 31915
Cdd:PLN00009     82 YLD-LDLKKHMDSSPdFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNA-LKLADFGLARAFGiPVRT 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPEV---HQHdvVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISL---- 31988
Cdd:PLN00009    160 FTHEVVTLWYRAPEIllgSRH--YSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGVTSlpdy 237
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31989 ---------------------EAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:PLN00009    238 ksafpkwppkdlatvvptlepAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
31769-31974 1.70e-18

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 92.46  E-value: 1.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVH--RCVETSSKKTFMAKFVKVKGT----DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05582       3 LGQGSFGKVFlvRKITGPDAGTLYAMKVLKKATlkvrDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFTA 31922
Cdd:cd05582      83 DLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGH--IKLTDFGLSKESIDHEKKAYSFCG 159
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31923 P-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNA 31974
Cdd:cd05582     160 TvEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKA 212
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
31769-32018 1.70e-18

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 92.63  E-value: 1.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKgtdQVLVKKEISilNIARHRNILY------------LHESFESMEELVMIF 31836
Cdd:cd05586       1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKK---VIVAKKEVA--HTIGERNILVrtaldespfivgLKFSFQTPTDLYLVT 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQAR-QLKPGDN 31915
Cdd:cd05586      76 DYMSGGELFWHLQKEG-RFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDA--NGHIALCDFGLSKaDLTDNKT 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPEVHQHDV-VSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfqeISLEAMDFI 31994
Cdd:cd05586     153 TNTFCGTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDV---LSDEGRSFV 229
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31995 DRLLVKERKSRMTA----SEALKHPWLK 32018
Cdd:cd05586     230 KGLLNRNPKHRLGAhddaVELKEHPFFA 257
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
31719-32022 1.89e-18

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 94.33  E-value: 1.89e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31719 EPSEPTVTKEDKTRAMNYDEEVDETREVTmTKASHSKTKElyekYMIAEDLGRGEFGIVHR--CVETSSKktfmakfVKV 31796
Cdd:PTZ00036     29 EMNDKKLDEEERSHNNNAGEDEDEEKMID-NDINRSPNKS----YKLGNIIGNGSFGVVYEaiCIDTSEK-------VAI 96
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31797 KGT--DQVLVKKEISILNIARHRNILYLH-----ESFESMEE---LVMIFEFISG-----LDIFERiNTSAFELNEREVV 31861
Cdd:PTZ00036     97 KKVlqDPQYKNRELLIMKNLNHINIIFLKdyyytECFKKNEKnifLNVVMEFIPQtvhkyMKHYAR-NNHALPLFLVKLY 175
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31862 SYvrQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiIKIIEFGQARQLKPGDNFRLLFTAPEYYAPEVHQHDV-VSSAT 31940
Cdd:PTZ00036    176 SY--QLCRALAYIHSKFICHRDLKPQNLLIDPNTHT-LKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATnYTTHI 252
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31941 DMWSLGTLV------YVLLSG----------INPFLAETNQQMieNIMNAEYT---FDEEAFQEISL--------EAMDF 31993
Cdd:PTZ00036    253 DLWSLGCIIaemilgYPIFSGqssvdqlvriIQVLGTPTEDQL--KEMNPNYAdikFPDVKPKDLKKvfpkgtpdDAINF 330
                           330       340
                    ....*....|....*....|....*....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWLKQRMD 32022
Cdd:PTZ00036    331 ISQFLKYEPLKRLNPIEALADPFFDDLRD 359
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
31769-32006 1.92e-18

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 92.37  E-value: 1.92e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK---VKGTDQV---LVKKEISILNiARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05616       8 LGKGSFGKVMLAERKGTDELYAVKILKkdvVIQDDDVectMVEKRVLALS-GKPPFLTQLHSCFQTMDRLYFVMEYVNGG 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ-LKPGDNFRLLFT 31921
Cdd:cd05616      87 DLMYHIQQVG-RFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH--IKIADFGMCKEnIWDGVTTKTFCG 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLLVKE 32001
Cdd:cd05616     164 TPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYP----KSMSKEAVAICKGLMTKH 239

                    ....*
gi 1958765569 32002 RKSRM 32006
Cdd:cd05616     240 PGKRL 244
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18735-19097 1.93e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.84  E-value: 1.93e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18735 AGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAGSFVAYATVNVLDKPGPVRN 18814
Cdd:COG3401      63 SGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYA 142
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18815 LKIADVSSDRCTIRWDPPeDDGGCEIQNYILEKCESKRMVWSTYSANVLTPGATVTRLIEGNEYIFRVRAENKIGTGPPt 18894
Cdd:COG3401     143 LGAGLYGVDGANASGTTA-SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP- 220
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18895 eSKPVIAKTKYDRPGRPDPPEVTKVSKEEMTVVWNAPEydgGKSITGYYLEKKEKHAVRWVPVNKSAIPErrLKVQNLLP 18974
Cdd:COG3401     221 -SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKVATVTTTS--YTDTGLTN 294
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18975 GHEYQFRVKAENevGIGEPSLPSRPVVAKDPIEPPGPPTNFKVVDTTKNSITLAWgKPVYDGGApiIGYVVEmRpkiaDA 19054
Cdd:COG3401     295 GTTYYYRVTAVD--AAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW-TASSDADV--TGYNVY-R----ST 364
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 1958765569 19055 SPDEGWKRCNAAAQLVrmEFTVTSLDENQEYEFRVCAQNQVGI 19097
Cdd:COG3401     365 SGGGTYTKIAETVTTT--SYTDTGLTPGTTYYYKVTAVDAAGN 405
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
23089-23628 2.11e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.84  E-value: 2.11e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23089 WVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNVKVLDRPGPPEGPVA-ISGVTAEKCM 23167
Cdd:COG3401      74 GTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYAlGAGLYGVDGA 153
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23168 LAWKPPLQDGGSDIINYIVERRETSRLVWTLVDANVQTLSCKVTKLLEGNEYIFRIMAVNKYGVGEPleSEPLIAKNPFV 23247
Cdd:COG3401     154 NASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTT 231
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23248 VPDAPKAPEVTAVTKDSMIVVWERPASDGgseILGYVLEKRDKEGIRWTRchkrlIGEL---RLRVTGLLENHNYEFRVS 23324
Cdd:COG3401     232 PPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTK-----VATVtttSYTDTGLTNGTTYYYRVT 303
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23325 AENAAGlsEPSPPSAYQKACDPIYKPGPPNNPKVMDVTRSSVFLSWTKPiydGGCEIQGYIVEKCDVSVGEWTMCTppTG 23404
Cdd:COG3401     304 AVDAAG--NESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIA--ET 376
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23405 INKTNLEVEKLLEKHEYNFRICAINKAGVGEhaDVPGPVMVEEKLEAPDIDLDLELRKVINIRAGGSlrlFVPIKGRPTP 23484
Cdd:COG3401     377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNES--APSEEVSATTASAASGESLTASVDAVPLTDVAGA---TAAASAASNP 451
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23485 EVKWGKVDGEIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTleNSSGTKSAFVTVRVLDTPSPPVNLKVTEITKDSVSI 23564
Cdd:COG3401     452 GVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTT--GSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPN 529
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 23565 TW-EPPLLDGGSKIKNYIVEKREATRKSYAAVVTNCHKNSWKIDQLQEGcSYYFRVTAENEYGIG 23628
Cdd:COG3401     530 VTgASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLG-GSLLTTTSTNTNDVA 593
I-set pfam07679
Immunoglobulin I-set domain;
32306-32396 2.13e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.39  E-value: 2.13e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGlDYYALHIRDTLPEDTGYYRVTATNTA 32385
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569 32386 GSTSCQAHLQV 32396
Cdd:pfam07679    80 GEAEASAELTV 90
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
31761-32015 2.20e-18

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 91.83  E-value: 2.20e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK-VKgtdQVLVKKEISIL-NIARHRNILYLHESF--ESMEELVMIF 31836
Cdd:cd14132      18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKpVK---KKKIKREIKILqNLRGGPNIVKLLDVVkdPQSKTPSLIF 94
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtRKNSIIKIIEFGQARQLKPGDNF 31916
Cdd:cd14132      95 EYVNNTDFKTLYPT----LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMID-HEKRKLRLIDWGLAEFYHPGQEY 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 R-----LLFTAPE------YYAPEVhqhdvvssatDMWSLGTLVYVLLSGINPFLA-ETNQQMIENIMNA-------EY- 31976
Cdd:cd14132     170 NvrvasRYYKGPEllvdyqYYDYSL----------DMWSLGCMLASMIFRKEPFFHgHDNYDQLVKIAKVlgtddlyAYl 239
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31977 ------------------------TFDEEAFQE-ISLEAMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd14132     240 dkygielpprlndilgrhskkpweRFVNSENQHlVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
I-set pfam07679
Immunoglobulin I-set domain;
5791-5879 2.35e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.00  E-value: 2.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5791 PIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANEGG 5870
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  5871 SCACTARVA 5879
Cdd:pfam07679    81 EAEASAELT 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30147-30240 2.35e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 85.24  E-value: 2.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30147 PLVPTKLEVVDVTKSTVTLAWEKPLYDGGsRLTGYVLEACKAGTERWMKVVTLKPTVLDHTVISLNEGEQYLFRVRAQNE 30226
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 30227 KGVSEPREIVTPVT 30240
Cdd:cd00063      80 GGESPPSESVTVTT 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33079-33162 2.44e-18

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 84.86  E-value: 2.44e-18
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33079 PRSITVHEGESARFSCDTDGEPVPTVTWLR-GGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQ 33157
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  33158 FTLTV 33162
Cdd:smart00410    81 TTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16706-17023 2.71e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.45  E-value: 2.71e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16706 YSITAVN--NLGTASKEMRLNVLGRPGPPVGPIKFESISADQMTLSWLPPKDDGgskITNYVIEKREANRKTWVRVSsEP 16783
Cdd:COG3401     207 YRVAATDtgGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVA-TV 282
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16784 KECMYTIPKLLEGHEYVFRIMAQNKYGIGEPlDSEPETARNLFSVPGAPDKPTVSSVTRNSMTVNWEEPEydgGSPVTGY 16863
Cdd:COG3401     283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESA-PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGY 358
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16864 WLEMKDTTSKRWkrvnrDPIKAMTLGVSYKVTGLIEGSDYQFRVYAINAAGVgpASLPSDPVTARDPVAPPGPPFPKVTD 16943
Cdd:COG3401     359 NVYRSTSGGGTY-----TKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN--ESAPSEEVSATTASAASGESLTASVD 431
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16944 wtksSVDLEWSPPLKDGGSKITGYIVEYKEEGKEEWEKGKDKEVRGTKLVVTGLKEGAFYKFRVRAVNIAGVGEPGEVTD 17023
Cdd:COG3401     432 ----AVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
31762-32017 2.72e-18

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 91.18  E-value: 2.72e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIV----------HRCVETSSKKTFM--AKFVK----------VKGTDQVL-----VKKEISILNIA 31814
Cdd:cd14199       3 QYKLKDEIGKGSYGVVklayneddntYYAMKVLSKKKLMrqAGFPRrppprgaraaPEGCTQPRgpierVYQEIAILKKL 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31815 RHRNILYLHESFE--SMEELVMIFEFISGLDIFERINTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyq 31892
Cdd:cd14199      83 DHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVMEVPTLKP--LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLL-- 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31893 TRKNSIIKIIEFGQARQLKPGDNFrLLFT--APEYYAPEV---HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQM 31967
Cdd:cd14199     159 VGEDGHIKIADFGVSNEFEGSDAL-LTNTvgTPAFMAPETlseTRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSL 237
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31968 IENIMNAEYTFDEEAfqEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14199     238 HSKIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
I-set pfam07679
Immunoglobulin I-set domain;
1038-1127 3.08e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.00  E-value: 3.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKqtGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEG--GTYTLTISNVQPDDSGKYTCVATNS 78
                            90
                    ....*....|
gi 1958765569  1118 HGETSASASL 1127
Cdd:pfam07679    79 AGEAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19311-19394 3.08e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.86  E-value: 3.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19311 PDPPRKVEVTEMTKNSATLAWLPPLRDGGaKIDGYIISYREEDQpaDRWTEYSV--VKDLSLIITGLKEGKKYKFRVAAR 19388
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGS--GDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 1958765569 19389 NAVGVS 19394
Cdd:cd00063      78 NGGGES 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
25772-26180 3.33e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.07  E-value: 3.33e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25772 ENLQEGCSYYFRVLASNEYGIGLPAETTEPVKVSEPPLPPGRVTLVDVTRNTATIKWEKPESDGgskITGYVVEMQTKGS 25851
Cdd:COG3401     197 GDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGD 273
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25852 EKWSTCTQVKTLEATISGLTAGEEYVFRVAAVNEKG-RSDPrqlgvpvvakdieikpsvelpfntfnvkandqlkidipf 25930
Cdd:COG3401     274 GPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP--------------------------------------- 314
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25931 kgrpqatvawkkdgqvlrettrvnvssskivttlsikeasredvgtyelcvSNTAgSITVPITVivldrPGPPGPIRIDE 26010
Cdd:COG3401     315 ---------------------------------------------------SNVV-SVTTDLTP-----PAAPSGLTATA 337
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26011 VSCDNVSISWTPPEYDGgcqISNYIVEKRETTSTTWQVVSQAVARTSIKIVRLTTGSEYQFRVCAENRYGKssYSESSAV 26090
Cdd:COG3401     338 VGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN--ESAPSEE 412
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26091 VAEYPFSPPGPPGTPKVVHATKSTMVVSWQVPVNDGGSQVIGYHLEYKERSSILWSKANKVLIADTqmkvSGLDEGLLYE 26170
Cdd:COG3401     413 VSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT----ATTTDTTTAN 488
                           410
                    ....*....|
gi 1958765569 26171 YRVYAENIAG 26180
Cdd:COG3401     489 LSVTTGSLVG 498
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
31767-32016 3.79e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 90.62  E-value: 3.79e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKV---KGTDQVLVKkEISILNIARHRNILYLHESFESMEELVMIFEFISG-L 31842
Cdd:cd07836       6 EKLGEGTYATVYKGRNRTTGEIVALKEIHLdaeEGTPSTAIR-EISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKdL 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK-PGDNFRLLFT 31921
Cdd:cd07836      85 KKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGE--LKLADFGLARAFGiPVNTFSNEVV 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISL------------ 31988
Cdd:cd07836     163 TLWYRAPDVlLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISQlpeykptfpryp 242
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 1958765569 31989 -------------EAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07836     243 pqdlqqlfphadpLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
31763-32017 4.05e-18

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 90.80  E-value: 4.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQ---VLVKKEISIL---------NIARHRNILYLHESFESME 31830
Cdd:cd07838       1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEgipLSTIREIALLkqlesfehpNVVRLLDVCHGPRTDRELK 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 eLVMIFEFIS-GLDIFERiNTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKnsIIKIIEFGQARQ 31909
Cdd:cd07838      81 -LTLVFEHVDqDLATYLD-KCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDG--QVKLADFGLARI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LKpgdnFRLLFTAPE----YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIM------------- 31972
Cdd:cd07838     157 YS----FEMALTSVVvtlwYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFdviglpseeewpr 232
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31973 NAEYTFD----------EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07838     233 NSALPRSsfpsytprpfKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26596-26688 4.09e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 4.09e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26596 PSPPSKPKIVDSGKTTITIGWVKPLFDGGaPITGYTVEYKKSEETDWK-VAIQSFRGTEYTMSGLTTGAEYVFRVRSLNK 26674
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKeVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 26675 VGASDPSDITDPQV 26688
Cdd:cd00063      80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
8328-8418 4.21e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 84.62  E-value: 4.21e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8328 PQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDkGEIVRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKNDA 8407
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  8408 GVQECYATLSV 8418
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
23812-24468 4.21e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 94.68  E-value: 4.21e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23812 YGITVANVVGQKTAAIEIITLDKPDPPKGPVKfdEVSAESITLSWNPPLYTGGCQITNYIVQK---RDTTTTVWDVVSAT 23888
Cdd:COG3401       9 LDAGIAASAAANTAVNALSKAGGSGKTILVYL--AVVLSVTTKESPGTLLVAAGLSSGGGLGTggrAGTTSGVAAVAVAA 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23889 VARTTLKVTKLKTGTEYQFRIFAENRYGQSFALESEPIVAQYPYKEPGPPGTPF--VTAVSKDSMVVQWHEPINNGGSPV 23966
Cdd:COG3401      87 APPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTyaLGAGLYGVDGANASGTTASSVAGA 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23967 IGYHLERKERNSILWTKVNKTIIHDTQFKALNLEEGIEYEFRVYAENIVGVGKASKNSECYVARDPCDPPGTPEAIIVKR 24046
Cdd:COG3401     167 GVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTP 246
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24047 NEITLQWTKPVYDGgsmITGYIVEKRDLPEGRWMKASFTNviETQFTVSGLTEDQRYEFRVIAKNAAGAISKPSDStgpi 24126
Cdd:COG3401     247 GSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNV---- 317
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24127 takdevelprismdpkfrdtivvnagetfrleadVHGKPLPTIewlrgdkeieesarceikntdfkallivkdairidgg 24206
Cdd:COG3401     318 ----------------------------------VSVTTDLTP------------------------------------- 326
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24207 qyilrasnvagsksfpvnvkvldrPGPPEGpVQVTGVTSEKCTLAWSPPLqdgGSDISHYVVEKRETSRLAWTVVASEVV 24286
Cdd:COG3401     327 ------------------------PAAPSG-LTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVT 378
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24287 TNSLKVTKLLEGNEYIFRIMAVNKYGVgEPLESAPVLMKNPFVLPGPPKSLEVT------NIAKDSMTVCWNRPDSDGGS 24360
Cdd:COG3401     379 TTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAPSEEVSATTASAASGESLTASVDavpltdVAGATAAASAASNPGVSAAV 457
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24361 EIIGYIVEKRDRSGIRWI---KCNKRRITDLRLRVTGLTEDHEYEFRVSAENAAGVGEPSPATVYYK-ACDPVFKPGPPT 24436
Cdd:COG3401     458 LADGGDTGNAVPFTTTSStvtATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPdGTPNVTGASPVT 537
                           650       660       670
                    ....*....|....*....|....*....|..
gi 1958765569 24437 NVHIVDTTKNSITLAWGKPIYDGGSDILGYVV 24468
Cdd:COG3401     538 VGASTGDVLITDLVSLTTSASSSVSGAGLGSG 569
I-set pfam07679
Immunoglobulin I-set domain;
22670-22749 4.46e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 84.23  E-value: 4.46e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNVIV 22749
Cdd:pfam07679    11 EVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
31757-32019 4.48e-18

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 91.52  E-value: 4.48e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYMIAEDLGRGEFGIVHrCVETSSKKTFMAkfVKVKGTDQVLVKKEIS-------ILNIA-RHRNILYLHESFES 31828
Cdd:cd05619       1 KLTIEDFVLHKMLGKGSFGKVF-LAELKGTNQFFA--IKALKKDVVLMDDDVEctmvekrVLSLAwEHPFLTHLFCTFQT 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31829 MEELVMIFEFISGLDIFERINTS-AFELNEREVvsYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQA 31907
Cdd:cd05619      78 KENLFFVMEYLNGGDLMFHIQSChKFDLPRATF--YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH--IKIADFGMC 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLKPGDNFRLLFTA-PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENImnaeyTFDEEAFQE- 31985
Cdd:cd05619     154 KENMLGDAKTSTFCGtPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI-----RMDNPFYPRw 228
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 31986 ISLEAMDFIDRLLVKERKSRMTASEALK-HPWLKQ 32019
Cdd:cd05619     229 LEKEAKDILVKLFVREPERRLGVRGDIRqHPFFRE 263
I-set pfam07679
Immunoglobulin I-set domain;
5042-5131 4.55e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 84.23  E-value: 4.55e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5042 PSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVAG 5121
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5122 SVECSANLFV 5131
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21870-21963 4.55e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 4.55e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21870 DPPGKPVPLNITRHTVALKWAKPEYTGGfKITSYVVEKRDLPNGRWLKANFSNILENEFTVSGLTEDAAYEFRVIAKNAA 21949
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|....
gi 1958765569 21950 GaISPPSEPSDAIT 21963
Cdd:cd00063      81 G-ESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16111-16205 4.60e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 4.60e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16111 PGPPGKPKVLERTKGSMLVSWTPPLDNGGsPITGYWLEKREEGGAYWSRVSRAPITKVglkgvEFSVPRLIEGVKYQFRA 16190
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSET-----SYTLTGLKPGTEYEFRV 74
                            90
                    ....*....|....*
gi 1958765569 16191 MAINAAGIGPPSEPS 16205
Cdd:cd00063      75 RAVNGGGESPPSESV 89
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
31736-32018 4.92e-18

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 92.37  E-value: 4.92e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31736 YDEEVDETREVTMTKashsktkelyEKYMIAEDLGRGEFGIVHRCVETSSKKTF----MAKFVKVKGTDQVLVKKEISIL 31811
Cdd:cd05621      37 YEKIVNKIRELQMKA----------EDYDVVKVIGRGAFGEVQLVRHKASQKVYamklLSKFEMIKRSDSAFFWEERDIM 106
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31812 NIARHRNILYLHESFESMEELVMIFEFISGLDIferIN-TSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENII 31890
Cdd:cd05621     107 AFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDL---VNlMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNML 183
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31891 YQtrKNSIIKIIEFGQARQLKPGDNFR--LLFTAPEYYAPEVHQHD----VVSSATDMWSLGTLVYVLLSGINPFLAETN 31964
Cdd:cd05621     184 LD--KYGHLKLADFGTCMKMDETGMVHcdTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLVGDTPFYADSL 261
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31965 QQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKE--RKSRMTASEALKHPWLK 32018
Cdd:cd05621     262 VGTYSKIMDHKNSLNFPDDVEISKHAKNLICAFLTDRevRLGRNGVEEIKQHPFFR 317
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25314-25406 5.17e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 5.17e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25314 PGPPEGpLKVTGVTAEKCYLAWNPPLQDGGAsISHYIIEKRETSRLSWTQVSTE-VQALNYKVTKLLPGNEYIFRVMAVN 25392
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 25393 KYGVGEPLESEPVI 25406
Cdd:cd00063      79 GGGESPPSESVTVT 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
32886-32975 5.24e-18

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 84.39  E-value: 5.24e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32886 PRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESS---KIHYTNTSGVLTLEILDCQTEDSGTYRAVCTN 32962
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 32963 YKGEASDYATLDV 32975
Cdd:cd20951      81 IHGEASSSASVVV 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
19450-19935 5.32e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 94.30  E-value: 5.32e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19450 DVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKIKVTVMDAPGPPQPPFDISEIDADACSLSWHIPL 19529
Cdd:COG3401      83 AVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASS 162
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19530 EdGGSNITNYIVEKCDVSRGDWVTALASVTKTSCrVGKLIPGQEYIFRVRAENRFGISEPltSPKMLAKFPFDVPSEPKN 19609
Cdd:COG3401     163 V-AGAGVVVSPDTSATAAVATTSLTVTSTTLVDG-GGDIEPGTTYYYRVAATDTGGESAP--SNEVSVTTPTTPPSAPTG 238
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19610 ARVTKVNKDCIFVAWDRPDSDGgspITGYLIERKERNSLLWVKANDtiVRSTEYPCAGLVEGLEYSFRIYALNKAGSspP 19689
Cdd:COG3401     239 LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGN--E 311
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19690 SKPTEYVTARMPVDPPGKPEVVDVT---KNSASLIWARPKhdgGSKIIGYFVEACKLPGDKWVRCNTTPHQIpleEYTAT 19766
Cdd:COG3401     312 SAPSNVVSVTTDLTPPAAPSGLTATavgSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTT---SYTDT 385
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19767 GLEENAQYQFRAIAKTAVNISqpSEPSDPVTILAENVPP--RIELSVEMKSLLTVKAGTNVCLDATVFGKPMPTVSWKKD 19844
Cdd:COG3401     386 GLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASgeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGD 463
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19845 S---TPIKQTEGVKMAMK-RNLCTLELFSVNRKDSGDYTITAENSS---GSKSATIKLKVLDKPGPPASVKINKMYADRA 19917
Cdd:COG3401     464 TgnaVPFTTTSSTVTATTtDTTTANLSVTTGSLVGGSGASSVTNSVsviGASAAAAVGGAPDGTPNVTGASPVTVGASTG 543
                           490
                    ....*....|....*...
gi 1958765569 19918 MLSWEPPLEDGGSEITNY 19935
Cdd:COG3401     544 DVLITDLVSLTTSASSSV 561
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23935-24028 6.10e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.09  E-value: 6.10e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23935 PGPPGTPFVTAVSKDSMVVQWHEPiNNGGSPVIGYHLERKERNSILWTKVNKTIIHDTQFKALNLEEGIEYEFRVYAENI 24014
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 24015 VGVGKASKNSECYV 24028
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19009-19107 6.46e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.09  E-value: 6.46e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19009 PGPPTNFKVVDTTKNSITLAWGKPVYDGGaPIIGYVVEMRPKiadasPDEGWKRCNAAAQLVRmEFTVTSLDENQEYEFR 19088
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREK-----GSGDWKEVEVTPGSET-SYTLTGLKPGTEYEFR 73
                            90
                    ....*....|....*....
gi 1958765569 19089 VCAQNQVGIGRPAELKEAI 19107
Cdd:cd00063      74 VRAVNGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17625-17710 7.00e-18

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 83.43  E-value: 7.00e-18
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17625 PSPPINPEAIDTTCNSVDLTWQPPRHDGGSkilGYIVEYQKVGDEEWRRANHTPESCPETKYKVTGLRDGQTYKFRVLAV 17704
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT---GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  17705 NEAGES 17710
Cdd:smart00060    78 NGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21671-21763 7.33e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 83.70  E-value: 7.33e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21671 PGPPTGpIKFDEVSSDFVTFSWEPPENDGGvPISNYVVEMRQTDSTTWVELATTVI-RTTYKATRLTTGVEYQFRVKAQN 21749
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 21750 RYGVGPGITSASVV 21763
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21477-21568 7.70e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 83.70  E-value: 7.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21477 PLPPDSLNIMDITKNTVSLAWPKPRHDGGsKITGYVIEAQRKGSDQWTHIST--VKGLECVVRNLTEGEEYTFQVMAVNS 21554
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 21555 AGRSAPRESRPVIV 21568
Cdd:cd00063      80 GGESPPSESVTVTT 93
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
31769-32018 8.32e-18

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 91.28  E-value: 8.32e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTF----MAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05596      34 IGRGAFGEVQLVRHKSTKKVYamklLSKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDL 113
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERIntSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLlFTA-- 31922
Cdd:cd05596     114 VNLM--SNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLD--ASGHLKLADFGTCMKMDKDGLVRS-DTAvg 188
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 -PEYYAPEVHQ----HDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAE--YTFDEEafQEISLEAMDFID 31995
Cdd:cd05596     189 tPDYISPEVLKsqggDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKnsLQFPDD--VEISKDAKSLIC 266
                           250       260
                    ....*....|....*....|....*
gi 1958765569 31996 RLLV--KERKSRMTASEALKHPWLK 32018
Cdd:cd05596     267 AFLTdrEVRLGRNGIEEIKAHPFFK 291
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24432-24526 9.00e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 83.70  E-value: 9.00e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24432 PGPPTNVHIVDTTKNSITLAWGKPIYDGGsDILGYVVEICKADEEEWQIVTPQTGlRVTRFEISKLIEHQEYKIRVCALN 24511
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1958765569 24512 KVGLGEaASVPGTVK 24526
Cdd:cd00063      79 GGGESP-PSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26041-26530 9.10e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 93.91  E-value: 9.10e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26041 TTSTTWQVVSQAVARTSIKIVRLTTGSEYQFRVCAENRYGK--SSYSESSAVVAEYPFSPPGPPGTPKVVHATKSTMVVS 26118
Cdd:COG3401      75 TTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDevPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGAN 154
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26119 WQVPVNDGGSQVIGYHLEYKERSSILWSKANKVLIADTQMKVSGLDEGLLYEYRVYAENIAGIGKCSKACEPVPARDPCD 26198
Cdd:COG3401     155 ASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPS 234
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26199 PPGQPEVTNITRKSVSLKWSKPRYDGgakITGYIVERRELPDGRWLKcnFTNVQETYFEVTELTEDQRYEFRVFARNAAD 26278
Cdd:COG3401     235 APTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTK--VATVTTTSYTDTGLTNGTTYYYRVTAVDAAG 309
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26279 SVSEPSestgpitvkddveaprimmdvkfrdvivvkagEVLKINADIAgrplpviswakdgveieerakteivstdsntt 26358
Cdd:COG3401     310 NESAPS--------------------------------NVVSVTTDLT-------------------------------- 325
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26359 ltvkdcvrrdtgqyvltlknvagtrtmavnckvldKPGPPAGpLEINGLTAEKCSLSWgrpQEDGGADIDYYIVEKRETS 26438
Cdd:COG3401     326 -----------------------------------PPAAPSG-LTATAVGSSSITLSW---TASSDADVTGYNVYRSTSG 366
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26439 RLAWTICEAELRTTSCKVTKLLKGNEYIFRVTGVNKYGvgepLESVAVKALDpfTTPSPPTSLEITSVTKDSMTLCWSRP 26518
Cdd:COG3401     367 GGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG----NESAPSEEVS--ATTASAASGESLTASVDAVPLTDVAG 440
                           490
                    ....*....|..
gi 1958765569 26519 ETDGGSDISGYI 26530
Cdd:COG3401     441 ATAAASAASNPG 452
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22067-22158 1.05e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 83.31  E-value: 1.05e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22067 PGPPEGpLAVSDVTSEKCVLSWLPPLDDGGaKIDHYIVQKRETSRLAWTNVATE-VQVTKLKVTKLLKGNEYIFRVMAVN 22145
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|...
gi 1958765569 22146 KYGVGEPLESEPV 22158
Cdd:cd00063      79 GGGESPPSESVTV 91
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
31763-32017 1.08e-17

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 88.65  E-value: 1.08e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT---DQVLVKKEISILNIARHRNILYLHESFESMEELVMI-FEF 31838
Cdd:cd08223       2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNAskrERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIvMGF 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERI-NTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENiIYQTRKNsIIKIIEFGQARQLKPG-DNF 31916
Cdd:cd08223      82 CEGGDLYTRLkEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQN-IFLTKSN-IIKVGDLGIARVLESSsDMA 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTfdeEAFQEISLEAMDFIDR 31996
Cdd:cd08223     160 TTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLP---PMPKQYSPELGELIKA 236
                           250       260
                    ....*....|....*....|.
gi 1958765569 31997 LLVKERKSRMTASEALKHPWL 32017
Cdd:cd08223     237 MLHQDPEKRPSVKRILRQPYI 257
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
31762-32017 1.14e-17

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 90.53  E-value: 1.14e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT--DQVLVkkEISILNIARHR------NILYLHESFESMEELV 31833
Cdd:cd14225      44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRfhHQALV--EVKILDALRRKdrdnshNVIHMKEYFYFRNHLC 121
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFIsGLDIFERI---NTSAFELnerevvSYVRQVCEA----LEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQ 31906
Cdd:cd14225     122 ITFELL-GMNLYELIkknNFQGFSL------SLIRRFAISllqcLRLLYRERIIHCDLKPENILLRQRGQSSIKVIDFGS 194
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARQlkpgdNFRLLFTAPE---YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIM----------- 31972
Cdd:cd14225     195 SCY-----EHQRVYTYIQsrfYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMevlglpppeli 269
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31973 -NAE---YTFDEEAFQEI--------------SLEAM---------DFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14225     270 eNAQrrrLFFDSKGNPRCitnskgkkrrpnskDLASAlktsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
I-set pfam07679
Immunoglobulin I-set domain;
4862-4942 1.20e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.08  E-value: 1.20e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4862 IQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFT 4941
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569  4942 V 4942
Cdd:pfam07679    90 V 90
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
31760-32017 1.23e-17

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 89.27  E-value: 1.23e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKymiAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd07835       1 YQK---LEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPStaiREISLLKELNHPNIVRLLDVVHSENKLYLVF 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISgLDIFERINTSAFELNEREVV-SYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQlkpgdn 31915
Cdd:cd07835      78 EFLD-LDLKKYMDSSPLTGLDPPLIkSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGA--LKLADFGLARA------ 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 frllFTAP------E-----YYAPEV----HQHdvvSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDE 31980
Cdd:cd07835     149 ----FGVPvrtythEvvtlwYRAPEIllgsKHY---STPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDE 221
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31981 EAFQEISL-------------------------EAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07835     222 DVWPGVTSlpdykptfpkwarqdlskvvpsldeDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
31763-32017 1.29e-17

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 88.81  E-value: 1.29e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRcVETSSKKTFMAKFVKVKGTDQVLV---KKEISILNIARHR-NI--LYLHESFESMEELVMIF 31836
Cdd:cd14131       3 YEILKQLGKGGSSKVYK-VLNPKKKIYALKRVDLEGADEQTLqsyKNEIELLKKLKGSdRIiqLYDYEVTDEDDYLYMVM 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFiSGLDiFERINTSAFE--LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrkNSIIKIIEFGQARQLKPGd 31914
Cdd:cd14131      82 EC-GEID-LATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLV---KGRLKLIDFGIAKAIQND- 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 nfrllfTA----------PEYYAPEV------HQHDV----VSSATDMWSLGTLVYVLLSGINPFLAETNQ-QMIENIMN 31973
Cdd:cd14131     156 ------TTsivrdsqvgtLNYMSPEAikdtsaSGEGKpkskIGRPSDVWSLGCILYQMVYGKTPFQHITNPiAKLQAIID 229
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 31974 AEYTFDEEAFQEISLeaMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14131     230 PNHEIEFPDIPNPDL--IDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
31769-32017 1.45e-17

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 88.62  E-value: 1.45e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV-LVKKEISILNIARHRNILYLHESFeSMEELVMIF-EFISG--LDI 31844
Cdd:cd06624      16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVqPLHEEIALHSRLSHKNIVQYLGSV-SEDGFFKIFmEQVPGgsLSA 94
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRkNSIIKIIEFGQARQLKPGDNFRLLFTAP- 31923
Cdd:cd06624      95 LLRSKWGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTY-SGVVKISDFGTSKRLAGINPCTETFTGTl 173
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31924 EYYAPEVHQHDV--VSSATDMWSLGTLVYVLLSGINPFLAETNQQ--MIENIMnaeYTFDEEAFQEISLEAMDFIDRLLV 31999
Cdd:cd06624     174 QYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFIELGEPQaaMFKVGM---FKIHPEIPESLSEEAKSFILRCFE 250
                           250
                    ....*....|....*...
gi 1958765569 32000 KERKSRMTASEALKHPWL 32017
Cdd:cd06624     251 PDPDKRATASDLLQDPFL 268
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14496-14578 1.47e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 82.66  E-value: 1.47e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14496 PWPPGKPTVKDIGKTSLVLNWTKPEHDGGAKIESYVIEMLKTGTDDWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKA 14575
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  14576 GES 14578
Cdd:smart00060    81 GEG 83
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1249-1337 1.51e-17

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 82.84  E-value: 1.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIR-RGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05893       3 FEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQG 82
                            90
                    ....*....|
gi 1958765569  1328 NAICSGKLYV 1337
Cdd:cd05893      83 RISCTGRLMV 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18216-18298 1.51e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 82.66  E-value: 1.51e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18216 PSPPGKPVVTDITENAATVSWTLPKSDGG-SPITGYYVERREITGKWVRVNKTPiADLKFRVTGLYEGNTYEFRVFAENL 18294
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  18295 AGLS 18298
Cdd:smart00060    80 AGEG 83
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
31769-32019 1.51e-17

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 89.31  E-value: 1.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVhrCVETSSKKtfmAKFVKVKGTD------QVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd06657      28 IGEGSTGIV--CIATVKSS---GKLVAVKKMDlrkqqrRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 102
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSafELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQL-KPGDNFRLLFT 31921
Cdd:cd06657     103 ALTDIVTHT--RMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLT--HDGRVKLSDFGFCAQVsKEVPRRKSLVG 178
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNaEYTFDEEAFQEISLEAMDFIDRLLVKE 32001
Cdd:cd06657     179 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPKLKNLHKVSPSLKGFLDRLLVRD 257
                           250
                    ....*....|....*...
gi 1958765569 32002 RKSRMTASEALKHPWLKQ 32019
Cdd:cd06657     258 PAQRATAAELLKHPFLAK 275
I-set pfam07679
Immunoglobulin I-set domain;
33892-33984 1.52e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 82.69  E-value: 1.52e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSqeqQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGN 33971
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS---SDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 33972 EFGSDSATVNINI 33984
Cdd:pfam07679    78 SAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29058-29141 1.58e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 1.58e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29058 PAPPRRLDVVDTSKSSAVLAWLKPEHDGGsRITSYLLEMRQKGSDFW--VEAGHTKQLTFTVERLVENTEYEFRVKAKND 29135
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 29136 AGYSEP 29141
Cdd:cd00063      80 GGESPP 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20985-21076 1.64e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 1.64e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20985 PGPPGPIEISNVSAEKATLTWTPPlEDGGSPIKAYVLEKRETSRLLW-TVVSEDIQACRHVVTKLIQGNEYLFRVSAVNH 21063
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 21064 YGKGEPVQSEPVK 21076
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14596-14678 1.65e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 82.66  E-value: 1.65e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14596 PSPPRWLEVINITKNTADLKWTVPEKDGG-SPITNYIVEKRDVRRKgWQTVDTTVKDTKCTVTPLTEGSLYVFRVAAENA 14674
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  14675 IGQS 14678
Cdd:smart00060    80 AGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
907-989 1.66e-17

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 82.55  E-value: 1.66e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    907 KNVTVVEGESVTLECHISGYPSPKVTWYREDYQ-IESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSC 985
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569    986 YLAV 989
Cdd:smart00410    82 TLTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24917-25010 1.74e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 1.74e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24917 PGPPVGpVKFDEVSADFVVISWEPPAYTGGcQISNYIVEKRDTTTTNWQMVSATVA-RTTIKVSKLKTGTEYQFRIFAEN 24995
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1958765569 24996 RYGKSTPLDSKPVVV 25010
Cdd:cd00063      79 GGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29253-29345 1.76e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 1.76e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29253 PGPVTGpIEVSSVSAESCVLSWSEPKDDGGtEITNYIVEKRESGTTAWQLINS-SVKRTQIKVTHLTKYKEYCFRVSSEN 29331
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 29332 RFGVSKPLESVPIV 29345
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
25017-25110 1.83e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 1.83e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25017 PGPPGTPFVTSVSKDQMLVQWhEPVNDGGSKVIGYHLEQKEKNSILWVKLNKIPIQDTKFKTTGLDEGLEYEFRVSAENI 25096
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 25097 VGIGKPSKVSECYV 25110
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14000-14082 1.87e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 82.28  E-value: 1.87e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14000 PSAPKELKFSDVTKDSVHLTWEPPDDDGG-SPLTGYVVEKRDMSRKtWTKVMDFVTDLEFTVPDLVQGKEYLFKVCARNK 14078
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  14079 CGPG 14082
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
4480-4569 2.10e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 82.31  E-value: 2.10e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAG 4559
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4560 SSSSSATVAV 4569
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17922-18011 2.29e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.54  E-value: 2.29e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17922 PGPPKDLHHVDVDKTEVSLVWNKPDRDGGsPITGYLVEYQEEGAKDWIKFKT--VKNLECVVTGLQQGKTYRFRVKAENI 17999
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 18000 IGLGLPDTTIPI 18011
Cdd:cd00063      80 GGESPPSESVTV 91
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
31769-32014 2.43e-17

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 87.68  E-value: 2.43e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK----VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd14189       9 LGKGGFARCYEMTDLATNKTYAVKVIPhsrvAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 fERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENiiYQTRKNSIIKIIEFGQARQLKPGDNFR-LLFTAP 31923
Cdd:cd14189      89 -AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGN--FFINENMELKVGDFGLAARLEPPEQRKkTICGTP 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31924 EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLLVKERK 32003
Cdd:cd14189     166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLP----ASLSLPARHLLAGILKRNPG 241
                           250
                    ....*....|.
gi 1958765569 32004 SRMTASEALKH 32014
Cdd:cd14189     242 DRLTLDQILEH 252
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
31769-31988 2.48e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 88.27  E-value: 2.48e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTfmakfVKVKGTDQVLVKK---------EISILNIARHRNILYLHESFESMEEL------V 31833
Cdd:cd13989       1 LGSGGFGYVTLWKHQDTGEY-----VAIKKCRQELSPSdknrerwclEVQIMKKLNHPNVVSARDVPPELEKLspndlpL 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERIN--TSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSII-KIIEFGQARQL 31910
Cdd:cd13989      76 LAMEYCSGGDLRKVLNqpENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyKLIDLGYAKEL 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFL---------AETNQQMIENI-----MNAEY 31976
Cdd:cd13989     156 DQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLpnwqpvqwhGKVKQKKPEHIcayedLTGEV 235
                           250
                    ....*....|..
gi 1958765569 31977 TFDEEAFQEISL 31988
Cdd:cd13989     236 KFSSELPSPNHL 247
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
31769-31960 2.50e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 88.48  E-value: 2.50e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCV--ETSSKktfmakfVKVKGTDQVLVKK-------EISILNIARHRNILYLHESFESMEEL------V 31833
Cdd:cd14038       2 LGTGGFGNVLRWInqETGEQ-------VAIKQCRQELSPKnrerwclEIQIMKRLNHPNVVAARDVPEGLQKLapndlpL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINTsaFE----LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSII-KIIEFGQAR 31908
Cdd:cd14038      75 LAMEYCQGGDLRKYLNQ--FEnccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIhKIIDLGYAK 152
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31909 QLKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFL 31960
Cdd:cd14038     153 ELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15640-16002 2.61e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 92.37  E-value: 2.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15640 VTGRPVPTKVWTIEEGELDKERVVIENVGTKSELIIKNALRKDHG---RYVITATNSCGSKFAAARVEVF---DVPGPVL 15713
Cdd:COG3401     158 TTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGttyYYRVAATDTGGESAPSNEVSVTtptTPPSAPT 237
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15714 DLKPVVTNRKMCLLNWSDPADDGgseITGFIIERKDAKMHTWRQPIETERSKCDITGLIEGQEYKFRVIAKNKFGcgppV 15793
Cdd:COG3401     238 GLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAG----N 310
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15794 EIGP--ILAVDP-LGPPTSPERLTYTERTKSTITLDWkEPRSDGGspIQGYIIEKRRHDKPDFERVNKrLCPTTSFLVDN 15870
Cdd:COG3401     311 ESAPsnVVSVTTdLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTG 386
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15871 LDEHQMYEFRVKAVNDIG-ESEPSLPlnVVIQDDEVPPTIKLRLAVRGDTIKVKAGEPVNI----PADVTGLPMPKIEWS 15945
Cdd:COG3401     387 LTPGTTYYYKVTAVDAAGnESAPSEE--VSATTASAASGESLTASVDAVPLTDVAGATAAAsaasNPGVSAAVLADGGDT 464
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 15946 KNEKVIEKPTDALNITKEEVSRSEAKTElSIPKAVREDKGTYTITASNRLGSVFRNV 16002
Cdd:COG3401     465 GNAVPFTTTSSTVTATTTDTTTANLSVT-TGSLVGGSGASSVTNSVSVIGASAAAAV 520
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23350-23438 2.75e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.16  E-value: 2.75e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23350 PGPPNNPKVMDVTRSSVFLSWTKPIYDGGcEIQGYIVEKCDVSVGEWTMCTPPTGiNKTNLEVEKLLEKHEYNFRICAIN 23429
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*....
gi 1958765569 23430 KAGVGEHAD 23438
Cdd:cd00063      79 GGGESPPSE 87
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
31761-32019 2.78e-17

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 87.51  E-value: 2.78e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVH--RCVETSS-----KKTFMAKFVKVKGTDQVlvkKEISILNIARHRNIL-----YLHESfes 31828
Cdd:cd06607       1 KIFEDLREIGHGSFGAVYyaRNKRTSEvvaikKMSYSGKQSTEKWQDII---KEVKFLRQLRHPNTIeykgcYLREH--- 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31829 MEELVMIFEFISGLDIFERINTSafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQAR 31908
Cdd:cd06607      75 TAWLVMEYCLGSASDIVEVHKKP---LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLT--EPGTVKLADFGSAS 149
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31909 QLKPGDNFrllFTAPEYYAPEV------HQHDvvsSATDMWSLGtlvyvlLSGINpfLAETNQQMIE-NIMNAEYTF--- 31978
Cdd:cd06607     150 LVCPANSF---VGTPYWMAPEVilamdeGQYD---GKVDVWSLG------ITCIE--LAERKPPLFNmNAMSALYHIaqn 215
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|...
gi 1958765569 31979 DEEAFQEI--SLEAMDFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd06607     216 DSPTLSSGewSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVTR 258
I-set pfam07679
Immunoglobulin I-set domain;
6729-6818 2.89e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 2.89e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6729 PSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNNAG 6808
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6809 QASCTTRLFV 6818
Cdd:pfam07679    81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
5884-5973 2.95e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 2.95e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESG 5963
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5964 VERCYAFLLV 5973
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24231-24322 3.04e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.16  E-value: 3.04e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24231 PGPPEGpVQVTGVTSEKCTLAWSPPlQDGGSDISHYVVEKRETSRLAWTVVASEVVT-NSLKVTKLLEGNEYIFRIMAVN 24309
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|...
gi 1958765569 24310 KYGVGEPLESAPV 24322
Cdd:cd00063      79 GGGESPPSESVTV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23546-23633 3.10e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.16  E-value: 3.10e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23546 PSPPVNLKVTEITKDSVSITWEPPLLDGGsKIKNYIVEKREATRKSYAAVVTNCHK-NSWKIDQLQEGCSYYFRVTAENE 23624
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*....
gi 1958765569 23625 YGIGLPART 23633
Cdd:cd00063      80 GGESPPSES 88
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
23491-24032 3.13e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 91.99  E-value: 3.13e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23491 VDGEIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRVLDTPSPPVNLKVTEITKDSVSITWEPPL 23570
Cdd:COG3401      79 VAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGT 158
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23571 LDGGSKIKNYIVE-----KREATRKSYAAVVTNchkNSWKIDQLQEGCSYYFRVTAENEYGIGLPARTADPIKVAEVPQP 23645
Cdd:COG3401     159 TASSVAGAGVVVSpdtsaTAAVATTSLTVTSTT---LVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSA 235
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23646 PGKITVDDVTRNSVSLSWTKPEHDGgskIIQYIVEMQAKNTDKWSECARVKSLEAVITSLTQGEEYLFRVIAVNEKGRSd 23725
Cdd:COG3401     236 PTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE- 311
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23726 prslavpitakdlviepdvrpafSSYSVQVgqdlkievpisgrpkpsiSWTKDGAPlkqttrinvidsldlttlsiketh 23805
Cdd:COG3401     312 -----------------------SAPSNVV------------------SVTTDLTP------------------------ 326
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23806 kddgghygitvanvvgqktaaieiitldkPDPPKGpVKFDEVSAESITLSWNPPLYTGgcqITNYIVQKRDTTTTVWDVV 23885
Cdd:COG3401     327 -----------------------------PAAPSG-LTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKI 373
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23886 SATVARTTLKVTKLKTGTEYQFRIFAENRYGqsfaLESEP--IVAQYPYKEPGPPGTPFVTAVSKDSMVVQWHEPINNGG 23963
Cdd:COG3401     374 AETVTTTSYTDTGLTPGTTYYYKVTAVDAAG----NESAPseEVSATTASAASGESLTASVDAVPLTDVAGATAAASAAS 449
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 23964 SPVIGYHLERKERNSILWTKVNKTiihdTQFKALNLEEGIEYEFRVYAENIVGVGKASKNSECYVARDP 24032
Cdd:COG3401     450 NPGVSAAVLADGGDTGNAVPFTTT----SSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGA 514
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19311-19394 3.45e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 81.51  E-value: 3.45e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19311 PDPPRKVEVTEMTKNSATLAWLPPLRDGGakiDGYIISYREEDQPAD-RWTEYSV-VKDLSLIITGLKEGKKYKFRVAAR 19388
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYRVEYREEGsEWKEVNVtPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  19389 NAVGVS 19394
Cdd:smart00060    78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4581-4663 3.48e-17

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 81.78  E-value: 3.48e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4581 PSYLMLPGESARLHCKLKGSPVIQVTWFKNN-KELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCST 4659
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   4660 EVVI 4663
Cdd:smart00410    82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
14899-14988 3.61e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 3.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14899 PTIDLETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLG 14978
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 14979 SATASINVKV 14988
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28368-28456 3.72e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 3.72e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28368 DPPGTPDYIDVTRETITLKWNPPlRDGGSKIVAYSIEKRQ-GSDRWVRCNFTDVSECQYTVSGLSPGDRYEFRIIARNAV 28446
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREkGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                            90
                    ....*....|
gi 1958765569 28447 GTiSPPSQSS 28456
Cdd:cd00063      81 GE-SPPSESV 89
I-set pfam07679
Immunoglobulin I-set domain;
7952-8040 3.76e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.53  E-value: 3.76e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLG 8031
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  8032 TASSSAKLI 8040
Cdd:pfam07679    81 EAEASAELT 89
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16829-16916 3.84e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 81.51  E-value: 3.84e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16829 PGAPDKPTVSSVTRNSMTVNWEEPEYDGG-SPVTGYWLEMKDtTSKRWKRVNRDPIKamtlgVSYKVTGLIEGSDYQFRV 16907
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSS-----TSYTLTGLKPGTEYEFRV 74

                     ....*....
gi 1958765569  16908 YAINAAGVG 16916
Cdd:smart00060    75 RAVNGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24688-25151 4.27e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 91.60  E-value: 4.27e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24688 VENLTEGAIYYFRVMAENEFGVGVPAETSDAVKASEPPSPPGKVTLTDVSQTSASLMWEKPEhdgGSRILGYVVEMQPKG 24767
Cdd:COG3401     196 GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSG 272
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24768 TEKWSVVAESKVCSAVVSGLSSGQEYQFRVKAYNEKGksdprvlgvpviakdltiqpsfklpfntysvqagedlkieipv 24847
Cdd:COG3401     273 DGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAG------------------------------------------- 309
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24848 igrprpkiswvkdgeplrqttrvnvEETATSTILhikesskddfgkySVTATNNAgtatenlsvivlekPGPPVGpVKFD 24927
Cdd:COG3401     310 -------------------------NESAPSNVV-------------SVTTDLTP--------------PAAPSG-LTAT 336
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24928 EVSADFVVISWEPPAYTGgcqISNYIVEKRDTTTTNWQMVSATVARTTIKVSKLKTGTEYQFRIFAENRYGKSTPLdSKP 25007
Cdd:COG3401     337 AVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAP-SEE 412
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25008 VVVQY---PFKEPGPPGTPFVTSVSKDQMLVQWHEPVNDGGSKVIGYHLEQKEKNSILWvklnkipiQDTKFKTTGLDEG 25084
Cdd:COG3401     413 VSATTasaASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFT--------TTSSTVTATTTDT 484
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 25085 LEYEFRVSAENIVGIGKPSKVSECYVARDPCDPPGRPEAIIITRNSVTLKWKKPTYDGGSKITGYIV 25151
Cdd:COG3401     485 TTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLV 551
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
31769-32019 4.68e-17

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 88.01  E-value: 4.68e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK----VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05585       2 IGKGSFGKVMQVRKKDTSRIYALKTIRkahiVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSA-FELNEREVvsYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQAR-QLKPGDNFRLLFTA 31922
Cdd:cd05585      82 FHHLQREGrFDLSRARF--YTAELLCALECLHKFNVIYRDLKPENILLDYTGH--IALCDFGLCKlNMKDDDKTNTFCGT 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRLLVKER 32002
Cdd:cd05585     158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPD----GFDRDAKDLLIGLLNRDP 233
                           250       260
                    ....*....|....*....|
gi 1958765569 32003 KSRM---TASEALKHPWLKQ 32019
Cdd:cd05585     234 TKRLgynGAQEIKNHPFFDQ 253
I-set pfam07679
Immunoglobulin I-set domain;
5229-5317 5.13e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.15  E-value: 5.13e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEVG 5308
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  5309 SSTCSARVT 5317
Cdd:pfam07679    81 EAEASAELT 89
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
31769-32019 5.19e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 87.63  E-value: 5.19e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAK------FVKVKGTDQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05608       9 LGKGGFGEVSACQMRATGKLYACKklnkkrLKKRKGYEGAMVEKRI--LAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGG 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFE---LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDN-FRL 31918
Cdd:cd05608      87 DLRYHIYNVDEEnpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGN--VRISDLGLAVELKDGQTkTKG 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE----TNQQMIENIMNAEYTFDEeafqEISLEAMDFI 31994
Cdd:cd05608     165 YAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSE----KFSPASKSIC 240
                           250       260       270
                    ....*....|....*....|....*....|
gi 1958765569 31995 DRLLVKERKSRM-----TASEALKHPWLKQ 32019
Cdd:cd05608     241 EALLAKDPEKRLgfrdgNCDGLRTHPFFRD 270
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29653-29744 5.34e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.39  E-value: 5.34e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29653 PGPCGKLTVSRVTEEKCTLAWSLPQEDGGaEITHYIVERRETSRLNWVIVEAECLT-LSYVVTRLIKNNEYTFRVRAVNK 29731
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 29732 YGLGVPIESEPIV 29744
Cdd:cd00063      80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23835-23927 5.39e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.39  E-value: 5.39e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23835 PDPPKGpVKFDEVSAESITLSWNPPLYTGGcQITNYIVQKRDTTTTVW-DVVSATVARTTLKVTKLKTGTEYQFRIFAEN 23913
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 23914 RYGQSFALESEPIV 23927
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16010-16094 5.51e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 81.12  E-value: 5.51e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16010 PSPPRNLAVTDIKAESCYLTWDAPL-DNGGSEITHYIIDKRDasrKKSEWEEVTNTAVERRYGIWKLIPNGQYEFRVRAV 16088
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPdDGITGYIVGYRVEYRE---EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  16089 NKYGTS 16094
Cdd:smart00060    78 NGAGEG 83
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
31763-32017 5.77e-17

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 88.08  E-value: 5.77e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG--TDQVLVkkEISILNIAR-------HRNILYLHESFESMEELV 31833
Cdd:cd14212       1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPayFRQAML--EIAILTLLNtkydpedKHHIVRLLDHFMHHGHLC 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFIsGLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQArqlkp 31912
Cdd:cd14212      79 IVFELL-GVNLYELLKQNQFRgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKLIDFGSA----- 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 GDNFRLLFT---APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLA--ETNQ-------------QMIENIMNA 31974
Cdd:cd14212     153 CFENYTLYTyiqSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGnsEYNQlsriiemlgmppdWMLEKGKNT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31975 E--------------YTFDEEA----------------FQEISLEAM-------------------------DFIDRLLV 31999
Cdd:cd14212     233 NkffkkvaksggrstYRLKTPEefeaenncklepgkryFKYKTLEDIimnypmkkskkeqidkemetrlafiDFLKGLLE 312
                           330
                    ....*....|....*...
gi 1958765569 32000 KERKSRMTASEALKHPWL 32017
Cdd:cd14212     313 YDPKKRWTPDQALNHPFI 330
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17500-18012 6.14e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 91.22  E-value: 6.14e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17500 AENLYGISDPLVSDSMKARDRFRVPDAPEQPVVTEVTKDSALVTWNKPNDGGKPITNYILEKRETMSKRWVRVTKEPIHP 17579
Cdd:COG3401     110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17580 YT-KYRVPDLLEGCQYEFRVSAENEIGIGDPSPPSKPVFARDPiakPSPPINPEAIDTTCNSVDLTWQPPrhdGGSKILG 17658
Cdd:COG3401     190 TTlVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP---PSAPTGLTATADTPGSVTLSWDPV---TESDATG 263
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17659 YIVEYQKVGDEEWRRANHTPEscpeTKYKVTGLRDGQTYKFRVLAVNEAG-ESDPahvpepvlvkdrleppelildanma 17737
Cdd:COG3401     264 YRVYRSNSGDGPFTKVATVTT----TSYTDTGLTNGTTYYYRVTAVDAAGnESAP------------------------- 314
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17738 reqhikvgdtlrlsaiikgvpfpkvtwkkedreaptkaqidvtpvgskleirnaahedggiysltvenpagSKTVSVKVL 17817
Cdd:COG3401     315 -----------------------------------------------------------------------SNVVSVTTD 323
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17818 VLdKPGPPRDLEVSEIRKDSCYLTWKEPLDDGgsvVTNYVVERKDVATAQWSPLSTTSKKKSHMAKHLNEGNQYLFRVAA 17897
Cdd:COG3401     324 LT-PPAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTA 399
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17898 ENQYGRG-----PFVETPKPIKALDPLHPPGPPKDLHHVDVDKTEVSLVWNKPDRDGGSPITGYLVEYQEEGAKDWIKFK 17972
Cdd:COG3401     400 VDAAGNEsapseEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA 479
                           490       500       510       520
                    ....*....|....*....|....*....|....*....|
gi 1958765569 17973 TVKNLECVVTGLQQGKTYRFRVKAENIIGLGLPDTTIPIE 18012
Cdd:COG3401     480 TTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAA 519
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29411-29919 6.19e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 91.22  E-value: 6.19e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29411 NYKVTGLVEGLEYQFRTYALNAAGVSKASEASRPIMAQNPVDPPGRPEVTDVTRSTVSLVWSAPMYDGgskVVGYIIERk 29490
Cdd:COG3401     193 VDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYR- 268
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29491 pvSEVGDGRWLKcnYTIVSDNFFTVTALSEGDTYEFRVLAKNAAGIISKGSEstgpvtcrdeyappkaeldarlqgdlvT 29570
Cdd:COG3401     269 --SNSGDGPFTK--VATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSN---------------------------V 317
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29571 IRAGSDLVLDAAVGGkpepkiiwtkgdkeldlcekvslqytgkratavikycdrsdsgkytltvknasgtksvsvmvkvl 29650
Cdd:COG3401     318 VSVTTDLTPPAAPSG----------------------------------------------------------------- 332
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29651 dspgpcgkLTVSRVTEEKCTLAWSlPQEDGGAeiTHYIVERRETSRLNWVIVEAECLTLSYVVTRLIKNNEYTFRVRAVN 29730
Cdd:COG3401     333 --------LTATAVGSSSITLSWT-ASSDADV--TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVD 401
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29731 KYGLgvpiESEP--IVARNSFTIPSQPGIPEGVGAGKEHIIIQWTKPESDGGNEIS-----NYLVDKREKKSLRWTRVNK 29803
Cdd:COG3401     402 AAGN----ESAPseEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVsaavlADGGDTGNAVPFTTTSSTV 477
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29804 DYVV-----YDTRLKVTSLMEGCDYQFRVTAVNSAGNSEPSEASNF-ISCREPSYTPGPPSAPRVVDTTKSSISLAWTKP 29877
Cdd:COG3401     478 TATTtdtttANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGApDGTPNVTGASPVTVGASTGDVLITDLVSLTTSA 557
                           490       500       510       520
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 29878 MYDGGTDIIGYVLEM--QEKDTDQWCRVHTNTTIRNNEFTVPDL 29919
Cdd:COG3401     558 SSSVSGAGLGSGNLYliTTLGGSLLTTTSTNTNDVAGVHGGTLL 601
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
22667-22749 6.25e-17

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 81.04  E-value: 6.25e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22667 NTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTT-RVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETL 22745
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 22746 NVIV 22749
Cdd:cd05894      83 FVKV 86
I-set pfam07679
Immunoglobulin I-set domain;
7011-7099 6.54e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.15  E-value: 6.54e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLG 7090
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*....
gi 1958765569  7091 TASSTARLT 7099
Cdd:pfam07679    81 EAEASAELT 89
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
31762-32012 6.60e-17

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 86.53  E-value: 6.60e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK----VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd14187       8 RYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPksllLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLE 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFErINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK-PGDNF 31916
Cdd:cd14187      88 LCRRRSLLE-LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDME--VKIGDFGLATKVEyDGERK 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDR 31996
Cdd:cd14187     165 KTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQK 240
                           250
                    ....*....|....*.
gi 1958765569 31997 LLVKERKSRMTASEAL 32012
Cdd:cd14187     241 MLQTDPTARPTINELL 256
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19901-19992 6.61e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 6.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19901 PGPPASVKINKMYADRAMLSWEPPlEDGGSEITNYIVDKRETSRPNWAQVSAT-VPITSCTVEKLIEGHEYQFRICAENK 19979
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 19980 YGVGDPIFTEPVI 19992
Cdd:cd00063      80 GGESPPSESVTVT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5703-5787 6.62e-17

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 81.01  E-value: 6.62e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5703 PSPVLVLRnGQSTTFECQVTGTPEIRVSWYLDGNE-ITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDAGTASC 5781
Cdd:smart00410     1 PPSVTVKE-GESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                     ....*.
gi 1958765569   5782 SIELKV 5787
Cdd:smart00410    80 GTTLTV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
31440-31532 6.77e-17

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 81.31  E-value: 6.77e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEI--IADGLKYRVQEfKGGYHQLIIASVTDDDATVYQVRAT 31517
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKIES-EYGVHVLHIRRVTVEDSAVYSAVAK 79
                            90
                    ....*....|....*
gi 1958765569 31518 NQGGSVSGTASLEVE 31532
Cdd:cd20951      80 NIHGEASSSASVVVE 94
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18116-18208 7.08e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 7.08e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18116 PGPPTGpINILDVTPEYMTISWQPPKDDGGsPVINYIVEKQDTRKGTWGVV-SAGSSKLKLKVPHLQKGCEYVFRVKAEN 18194
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 18195 KMGVGPPLDSIPTV 18208
Cdd:cd00063      79 GGGESPPSESVTVT 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7576-7666 7.42e-17

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 81.09  E-value: 7.42e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7576 PPSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVA 7655
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  7656 GQDESSALLTV 7666
Cdd:cd20972      81 GSDTTSAEIFV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16424-16506 7.46e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 80.74  E-value: 7.46e-17
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16424 PGPPKDLKVSDITRGSCRLSWKMPDDDGGDR-IKGYVIEKKTIDGKaWTKVNPNCGSTAFVVPDLISEQQYFFRVRAENR 16502
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  16503 FGIG 16506
Cdd:smart00060    80 AGEG 83
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
31799-32016 7.48e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 86.69  E-value: 7.48e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31799 TDQVLVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFISGLD---IFERINTSAFELnereVVSYVRQVCEALEFLH 31875
Cdd:cd05609      44 IQQVFVERDI--LTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDcatLLKNIGPLPVDM----ARMYFAETVLALEYLH 117
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31876 SQNIGHFDIRPENIIYQTRKNsiIKIIEFG--------------QARQLKPGDNF--RLLFTAPEYYAPEVHQHDVVSSA 31939
Cdd:cd05609     118 SYGIVHRDLKPDNLLITSMGH--IKLTDFGlskiglmslttnlyEGHIEKDTREFldKQVCGTPEYIAPEVILRQGYGKP 195
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31940 TDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfQEISLEAMDFIDRLLVK---ERKSRMTASEALKHPW 32016
Cdd:cd05609     196 VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGD-DALPDDAQDLITRLLQQnplERLGTGGAEEVKQHPF 274
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17822-17909 7.73e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 7.73e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17822 PGPPRDLEVSEIRKDSCYLTWKEPLDDGGSvVTNYVVERKDVATAQWSPLSTT-SKKKSHMAKHLNEGNQYLFRVAAENQ 17900
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*....
gi 1958765569 17901 YGRGPFVET 17909
Cdd:cd00063      80 GGESPPSES 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6914-6991 7.94e-17

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 80.30  E-value: 7.94e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6914 PPYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAEN 6991
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
31779-32136 8.77e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 89.69  E-value: 8.77e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31779 RCVETSSKktFMAKFVKVKGTDQ-VLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERINTSAFE--- 31854
Cdd:PTZ00267     88 RGSDPKEK--VVAKFVMLNDERQaAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEhlp 165
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31855 LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQ------LKPGDNFrllFTAPEYYAP 31928
Cdd:PTZ00267    166 FQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLM--PTGIIKLGDFGFSKQysdsvsLDVASSF---CGTPYYLAP 240
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31929 EVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYtfdeEAFQ-EISLEAMDFIDRLLVKERKSRMT 32007
Cdd:PTZ00267    241 ELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKY----DPFPcPVSSGMKALLDPLLSKNPALRPT 316
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32008 ASEALKHPWLKQrmdrVSTKVIRTLRHRryyHTLIKKDlnmvvsAARIscggaIRSQRGVSVAKVKVASIEIGPVSGQIM 32087
Cdd:PTZ00267    317 TQQLLHTEFLKY----VANLFQDIVRHS---ETISPHD------REEI-----LRQLQESGERAPPPSSIRYGVVTSDVT 378
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 32088 HaigeeGGYVkyvckienYDQSTQVTW-----YFGVRQL-----ENSEKyeityeDGVA 32136
Cdd:PTZ00267    379 H-----GGYL--------YKYSSDMRWkkryfYIGNGQLrislsENPEN------DGVA 418
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
31763-32016 9.28e-17

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 87.37  E-value: 9.28e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQ---VLVKKEISILNIARHRNILYLHE--------SFESMEE 31831
Cdd:cd07866      10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDgfpITALREIKILKKLKHPNVVPLIDmaverpdkSKRKRGS 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEF----ISGLdiferINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQA 31907
Cdd:cd07866      90 VYMVTPYmdhdLSGL-----LENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILID--NQGILKIADFGLA 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 R---------QLKPGDNFR----LLFTApEYYAPEVHQHDV-VSSATDMWSLGTLVYVLLSGiNPFLA---ETNQ-QMIE 31969
Cdd:cd07866     163 RpydgpppnpKGGGGGGTRkytnLVVTR-WYRPPELLLGERrYTTAVDIWGIGCVFAEMFTR-RPILQgksDIDQlHLIF 240
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31970 NIM-----------------NAEYTFD------EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07866     241 KLCgtpteetwpgwrslpgcEGVHSFTnyprtlEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
31762-32017 9.45e-17

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 86.28  E-value: 9.45e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTD-------QVLV----KKEISILNIARHRNIL-YLheSFESM 31829
Cdd:cd06629       2 KWVKGELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSsdradsrQKTVvdalKSEIDTLKDLDHPNIVqYL--GFEET 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIF-EFISGLDIFERINTSA-FElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQA 31907
Cdd:cd06629      80 EDYFSIFlEYVPGGSIGSCLRKYGkFE--EDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDL--EGICKISDFGIS 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLKP--GDNFRLLFTAPEYY-APEV--HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEA 31982
Cdd:cd06629     156 KKSDDiyGNNGATSMQGSVFWmAPEVihSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVPE 235
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 31983 FQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06629     236 DVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
31769-31960 9.74e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 86.51  E-value: 9.74e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIV----HRcvETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELV-----MIFEFI 31839
Cdd:cd14039       1 LGTGGFGNVclyqNQ--ETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAMEYC 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINT--SAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSII-KIIEFGQARQLKPGDNF 31916
Cdd:cd14039      79 SGGDLRKLLNKpeNCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVhKIIDLGYAKDLDQGSLC 158
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 31917 RLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFL 31960
Cdd:cd14039     159 TSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFL 202
fn3 pfam00041
Fibronectin type III domain;
19312-19396 9.82e-17

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 80.54  E-value: 9.82e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19312 DPPRKVEVTEMTKNSATLAWLPPlRDGGAKIDGYIISYREEDQPaDRWTEYSVVKDL-SLIITGLKEGKKYKFRVAARNA 19390
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSG-EPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 19391 VGVSMP 19396
Cdd:pfam00041    79 GGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
6073-6162 1.14e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 80.38  E-value: 1.14e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAG 6152
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6153 DNACSGILTV 6162
Cdd:pfam07679    81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16010-16103 1.14e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.62  E-value: 1.14e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16010 PSPPRNLAVTDIKAESCYLTWDAPLDNGGsEITHYIIDKRDASRkkSEWEEVTNTAV-ERRYGIWKLIPNGQYEFRVRAV 16088
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGS--GDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|....*
gi 1958765569 16089 NKYGTSDECKSDKVV 16103
Cdd:cd00063      78 NGGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18613-18706 1.16e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.62  E-value: 1.16e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18613 PGEPENLHIADKGKTFVYLKWRRPDYDGGsPNLSYHVERRLKGSADWERVHKGSIKETHYMVDKCVENQIYEFRVQTKNE 18692
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 18693 GGESDWVRTEEVVV 18706
Cdd:cd00063      80 GGESPPSESVTVTT 93
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
31769-32006 1.17e-16

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 87.36  E-value: 1.17e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK---VKGTDQV---LVKKEISILnIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05615      18 LGKGSFGKVMLAERKGSDELYAIKILKkdvVIQDDDVectMVEKRVLAL-QDKPPFLTQLHSCFQTVDRLYFVMEYVNGG 96
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ-LKPGDNFRLLFT 31921
Cdd:cd05615      97 DLMYHIQQVG-KFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH--IKIADFGMCKEhMVEGVTTRTFCG 173
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLLVKE 32001
Cdd:cd05615     174 TPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP----KSLSKEAVSICKGLMTKH 249

                    ....*
gi 1958765569 32002 RKSRM 32006
Cdd:cd05615     250 PAKRL 254
I-set pfam07679
Immunoglobulin I-set domain;
14212-14292 1.17e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 80.38  E-value: 1.17e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14212 LTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVN 14291
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 14292 V 14292
Cdd:pfam07679    90 V 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
13602-13690 1.22e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 1.22e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13602 PGPVRNLEVTETFDGEVSLAWEEPLTDGGsKIIGYVVERRDIKRKTWVLV-TDRADSCEFTVTGLQKGgVEYLFRVSARN 13680
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPG-TEYEFRVRAVN 78
                            90
                    ....*....|
gi 1958765569 13681 RVGTGEPVET 13690
Cdd:cd00063      79 GGGESPPSES 88
I-set pfam07679
Immunoglobulin I-set domain;
19817-19897 1.24e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 80.38  E-value: 1.24e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 19897 V 19897
Cdd:pfam07679    90 V 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
13804-13887 1.30e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.97  E-value: 1.30e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13804 PSPPVNLSASEQTQSSVQLTWEPPLKDGG-SPILGYIIERQEEGkDNWIRCNMKPvPELTYKVTGLQKGNKYLYRVSAEN 13882
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  13883 AAGVS 13887
Cdd:smart00060    79 GAGEG 83
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
31769-32006 1.36e-16

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 87.06  E-value: 1.36e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK----VKGTDQVLVKKEISILNIARHRNIL-YLHESFESMEELVMIFEFISGLD 31843
Cdd:cd05587       4 LGKGSFGKVMLAERKGTDELYAIKILKkdviIQDDDVECTMVEKRVLALSGKPPFLtQLHSCFQTMDRLYFVMEYVNGGD 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ-LKPGDNFRLLFTA 31922
Cdd:cd05587      84 LMYHIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGH--IKIADFGMCKEgIFGGKTTRTFCGT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDeeafQEISLEAMDFIDRLLVKER 32002
Cdd:cd05587     161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP----KSLSKEAVSICKGLLTKHP 236

                    ....
gi 1958765569 32003 KSRM 32006
Cdd:cd05587     237 AKRL 240
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29353-29445 1.45e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 1.45e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29353 PSAPTRPEVYYVSANAMSIRWEEPYHDGGsKIVGYWVEKKERNTILWVKENKVPCLECNYKVTGLVEGLEYQFRTYALNA 29432
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 29433 AGVSKASEASRPI 29445
Cdd:cd00063      80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
9292-9380 1.47e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.99  E-value: 1.47e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGE 9371
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDG-QPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  9372 IESNVNLQV 9380
Cdd:pfam07679    82 AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18316-18402 1.56e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 1.56e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18316 PGPPINPKLKDKTKESADLVWTKPLSDGGsPILGYVVECQKPGTTQWDRINKDElIRQCAFRVPGLIEGNEYRFRIRAAN 18395
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTP-GSETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*..
gi 1958765569 18396 IVGEGEP 18402
Cdd:cd00063      79 GGGESPP 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30740-30830 1.56e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 1.56e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30740 PNTPEGpLEYDDIQTRSVRVSWRPPADDGGaDILGYILERREVPKAAWYTIDS-RVRGTSLVVKGLKENVEYHFRVSAEN 30818
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|..
gi 1958765569 30819 QFGISKPLKSEE 30830
Cdd:cd00063      79 GGGESPPSESVT 90
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
31762-31963 1.67e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 85.82  E-value: 1.67e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTF-MAKFVKVKGTDQV--LVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd07848       2 KFEVLGVVGEGAYGVVLKCRHKETKEIVaIKKFKDSEENEEVkeTTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEY 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISG--LDIFERINTSAFElneREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNF 31916
Cdd:cd07848      82 VEKnmLELLEEMPNGVPP---EKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISH--NDVLKLCDFGFARNLSEGSNA 156
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 1958765569 31917 RLL-FTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAET 31963
Cdd:cd07848     157 NYTeYVATRWYrSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGES 205
I-set pfam07679
Immunoglobulin I-set domain;
7387-7477 1.75e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.99  E-value: 1.75e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7387 PRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDkGEVIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKNDA 7466
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  7467 GMRECSALLTV 7477
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25414-25497 1.84e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.58  E-value: 1.84e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25414 PGPPSTPEASAITKDSMVLTWTRPVDDGG-AEIEGYILEKRDKEGiRWTKCNKKTlTDLRFRVTGLTEGHSYEFRVAAEN 25492
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  25493 AAGVG 25497
Cdd:smart00060    79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
14992-15078 1.86e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 1.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14992 PGPCKDIKASDITKSSCKLTWEPPEFDGGsPILHYVLERREAGRRTYIPVMSGE-NKLSWTVKDLIPNGEYFFRVKAVNK 15070
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*...
gi 1958765569 15071 IGGGEYIE 15078
Cdd:cd00063      80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19504-19592 1.86e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 1.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19504 PGPPQPPfDISEIDADACSLSWHiPLEDGGSNITNYIVEKCDVSRGDWVTA-LASVTKTSCRVGKLIPGQEYIFRVRAEN 19582
Cdd:cd00063       1 PSPPTNL-RVTDVTSTSVTLSWT-PPEDDGGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|
gi 1958765569 19583 RFGISEPLTS 19592
Cdd:cd00063      79 GGGESPPSES 88
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
900-990 1.86e-16

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 79.77  E-value: 1.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSID---FQITFQSGIARLMIREAFAEDSGRFTCSAVN 976
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569   977 EAGTVSTSCYLAVQ 990
Cdd:cd20951      81 IHGEASSSASVVVE 94
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24725-24806 2.03e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.58  E-value: 2.03e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24725 PSPPGKVTLTDVSQTSASLMWEKPEHDGG-SRILGYVVEMQPKGTEKWSVVAESKVCSAVVSGLSSGQEYQFRVKAYNEK 24803
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  24804 GKS 24806
Cdd:smart00060    81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
22753-22845 2.07e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 2.07e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22753 PGPPTGpVKMDEVTADSVTLSWEPPKYDGGsSINNYIVEKRDTSTTAWQIVSATVA-RTTIKASRLKTGCEYQFRIAAEN 22831
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 22832 RYGKSTYLNSEPVI 22845
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27182-27272 2.13e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 2.13e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27182 PGPPSTPWVSNVTRESITVGWhEPVSNGGSAVIGYHLEMKDRNSILWQKANKMIIRTTHFKVTTISAGLIYEFRVYAENA 27261
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 27262 AGIGKPSHSSE 27272
Cdd:cd00063      80 GGESPPSESVT 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
33698-33787 2.20e-16

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 79.77  E-value: 2.20e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISV---SRSRNMYTLEIRNASVSDSGKYTVKAKN 33774
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKykiESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 33775 FRGQCSATASLTV 33787
Cdd:cd20951      81 IHGEASSSASVVV 93
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
31769-32018 2.35e-16

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 86.51  E-value: 2.35e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFG---IVHRCVETSSKKTFMAKFVKvkgtDQVLVKKEISILNIARHRNIL----------YLHESFESMEELVMI 31835
Cdd:cd05614       8 LGTGAYGkvfLVRKVSGHDANKLYAMKVLR----KAALVQKAKTVEHTRTERNVLehvrqspflvTLHYAFQTDAKLHLI 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDN 31915
Cdd:cd05614      84 LDYVSGGELFTHLYQRDH-FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH--VVLTDFGLSKEFLTEEK 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLL-FTAP-EYYAPE-VHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE----TNQQMIENIMNAEYTFDeeafQEISL 31988
Cdd:cd05614     161 ERTYsFCGTiEYMAPEiIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEgeknTQSEVSRRILKCDPPFP----SFIGP 236
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 31989 EAMDFIDRLLVKERKSRM-----TASEALKHPWLK 32018
Cdd:cd05614     237 VARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFK 271
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14296-14378 2.42e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.20  E-value: 2.42e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14296 PGPPAAFDITDVTNESCLLTWNPPRDDGG-SKITNYVVERKATDSDvWHKLSSTVKDTNFKATKLTPNKEYIFRVAAENM 14374
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  14375 YGVG 14378
Cdd:smart00060    80 AGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30344-30435 2.44e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.46  E-value: 2.44e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30344 PGPPIGpIKIDEVDATSVTISWEPPELDGGaPLSGYVVEQRDAHRPGWLPV-SESVTRPTFKFTRLTEGNEYVFRVAATN 30422
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|...
gi 1958765569 30423 RFGIGSYLQSEVI 30435
Cdd:cd00063      79 GGGESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22464-22546 2.49e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.20  E-value: 2.49e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22464 PGPPQNLKIKEVTKTSVTLTWEPPLLDGG-SKIKNYIVEKRESTRKaYSTVATNCHKTSWKIDQLQEGCSYYFRVLAENE 22542
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  22543 YGIG 22546
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20101-20185 2.57e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.20  E-value: 2.57e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20101 PGPPAFPKVYDTTRSSVSLSWGKPAFDGG-SPIIGYLVEvKRADSDHWVRCNLPEKlqKTRFEVTGLMENTEYQFRVYAV 20179
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVE-YREEGSEWKEVNVTPS--STSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  20180 NKIGYS 20185
Cdd:smart00060    78 NGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
31440-31531 2.63e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 2.63e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGlKYRVQeFKGGYHQLIIASVTDDDATVYQVRATNQ 31519
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD-RFKVT-YEGGTYTLTISNVQPDDSGKYTCVATNS 78
                            90
                    ....*....|..
gi 1958765569 31520 GGSVSGTASLEV 31531
Cdd:pfam07679    79 AGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25711-25793 2.64e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.20  E-value: 2.64e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25711 PSAPVNLTVREVKKDSVTLSWEPPLIDGGAK-VTNYIVEKRETTRKaYATITNNCTKTTFKIENLQEGCSYYFRVLASNE 25789
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  25790 YGIG 25793
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28766-28849 2.75e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 79.20  E-value: 2.75e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28766 PSAPAVVKVTDTSKTTVSLEWARPVFDGGME-IIGYIIEMCKADlGDWHKVNTEPcVKTRYTVTDLQAGEEYKFRVSAIN 28844
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEG-SEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  28845 GAGKG 28849
Cdd:smart00060    79 GAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30326-30923 2.78e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 88.91  E-value: 2.78e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30326 KNVTGTTSETIKVVILDKPGPPIGPIKIDEVDATSVTISWEPPELDGGAPLSGYVVE----QRDAHRPGWLPVSESVTRP 30401
Cdd:COG3401      11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLgtggRAGTTSGVAAVAVAAAPPT 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30402 TFKFTRLTEGNEY--VFRVAATNRFGIGSYLQSEVIECRSSISIPGPPETLQIFDISRDGMTLTWYPPEDDGGSQVTGYI 30479
Cdd:COG3401      91 ATGLTTLTGSGSVggATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVV 170
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30480 IERKEVRADRWVRVNKVPVTMTRYRSTGLIEGLEYEHRVTAINargTGKPSRPSKPTVAMDPIAPPGKPQNPRVTDTTRT 30559
Cdd:COG3401     171 SPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATD---TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPG 247
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30560 SVSLAWSVPEDEGgskVTGYLIEMQKVDQREWTKCNTTPTkiREYTLTHLPQGAEYRFRVLACNAGG-PGEPAEVpgtVK 30638
Cdd:COG3401     248 SVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTT--TSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNV---VS 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30639 VTemleyPDYELderyqegvfvrqggvirltipikgkpfpickwtkegqdvskramiatsethtelvikeadrndsgtyd 30718
Cdd:COG3401     320 VT-----TDLTP-------------------------------------------------------------------- 326
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30719 lvlenkcgkktvyikvkvigsPNTPEGpLEYDDIQTRSVRVSWRPPADdggADILGYILERREVPKAAWYTIDSRVRGTS 30798
Cdd:COG3401     327 ---------------------PAAPSG-LTATAVGSSSITLSWTASSD---ADVTGYNVYRSTSGGGTYTKIAETVTTTS 381
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30799 LVVKGLKENVEYHFRVSAENQFGISKPLKSEEPVIPKTPLNPPEPPSNPPEV-LDVTKSSVSLSWSRPKDDGGSRVTGYY 30877
Cdd:COG3401     382 YTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVpLTDVAGATAAASAASNPGVSAAVLADG 461
                           570       580       590       600
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569 30878 IERKETSTDKWVRHNKTQITTTMYTVTGLVPDAEYQFRIIAQNDVG 30923
Cdd:COG3401     462 GDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
31769-32016 2.93e-16

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 84.69  E-value: 2.93e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK------EISILNIARHRNILYLHESFESMEE--LVMIFEFIS 31840
Cdd:cd06653      10 LGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEvnalecEIQLLKNLRHDRIVQYYGCLRDPEEkkLSIFVEYMP 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK----PGDNF 31916
Cdd:cd06653      90 GGSVKDQLKAYG-ALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGN--VKLGDFGASKRIQticmSGTGI 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENImnAEYTFDEEAFQEISLEAMDFIDR 31996
Cdd:cd06653     167 KSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKI--ATQPTKPQLPDGVSDACRDFLRQ 244
                           250       260
                    ....*....|....*....|
gi 1958765569 31997 LLVKErKSRMTASEALKHPW 32016
Cdd:cd06653     245 IFVEE-KRRPTAEFLLRHPF 263
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24331-24414 3.24e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.24e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24331 PGPPKSLEVTNIAKDSMTVCWNRPDSDGG-SEIIGYIVEKRDRSGiRWIKCNkRRITDLRLRVTGLTEDHEYEFRVSAEN 24409
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  24410 AAGVG 24414
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27282-27362 3.28e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.28e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27282 PPRNVRITDISKNSVNLSWQQPAFDGG-SKITGYIVERRDlPDGRWTKASfTNVIETQFTVSGLTQNSQYEFRVFARNAV 27360
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ..
gi 1958765569  27361 GS 27362
Cdd:smart00060    81 GE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21380-21462 3.31e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.31e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21380 PGPVLNLRPTDITKDSVTLHWDLPLIDGG-SRITNYIVEKREaTRKSYSTVTTKCHKCTYKVTGLTEGCEYFFRVMAENE 21458
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  21459 YGIG 21462
Cdd:smart00060    80 AGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
33698-33774 3.46e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 78.76  E-value: 3.46e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKN 33774
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
20102-20188 3.62e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 78.61  E-value: 3.62e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20102 GPPAFPKVYDTTRSSVSLSWgKPAFDGGSPIIGYLVEVKRADS-DHWVRCNLPEklQKTRFEVTGLMENTEYQFRVYAVN 20180
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSgEPWNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*...
gi 1958765569 20181 KIGYSDPS 20188
Cdd:pfam00041    78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29752-29845 3.63e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 3.63e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29752 PSQPGIPEGVGAGKEHIIIQWTKPESDGGnEISNYLVDKREKKSLRWTRVNKDYVVyDTRLKVTSLMEGCDYQFRVTAVN 29831
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGS-ETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 29832 SAGNSEPSEASNFI 29845
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15986-16255 3.69e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 88.52  E-value: 3.69e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15986 TYTITASNRLGSVFRNVHVEVYDR---PSPPRNLAVTDIKAESCYLTWDAPLDNGgseITHYIIDKRDASrkKSEWEEVT 16062
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVTTPttpPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSG--DGPFTKVA 280
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16063 NTAvERRYGIWKLIPNGQYEFRVRAVNKYGT-SDecKSDKVVIQDPYRLPGPPGKPKVLERTKGSMLVSWTPPLDNGgsp 16141
Cdd:COG3401     281 TVT-TTSYTDTGLTNGTTYYYRVTAVDAAGNeSA--PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--- 354
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16142 ITGYWLEKREEGGAYWSRVSRApitkvgLKGVEFSVPRLIEGVKYQFRAMAINAAGIGppSEPSDPaVAGDPIYPPGPPS 16221
Cdd:COG3401     355 VTGYNVYRSTSGGGTYTKIAET------VTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEE-VSATTASAASGES 425
                           250       260       270
                    ....*....|....*....|....*....|....
gi 1958765569 16222 CPEVKDKTKSSISLAWKPPAKDGGSPIKGYIVEM 16255
Cdd:COG3401     426 LTASVDAVPLTDVAGATAAASAASNPGVSAAVLA 459
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27464-27977 3.69e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 88.52  E-value: 3.69e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27464 GSASATIRVQILDKPGPPGGPIEFKTVTAEKITLLWRPPADDGGAKITHYIV--EKRETSRVVWSMVAENLEECIITTTK 27541
Cdd:COG3401      52 PGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVggATNTGLTSSDEVPSPAVGTATTATAV 131
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27542 IIKGNEYIFRVRAVNKYGIGEPLESEPVVAKNSFVTPGPPSIPEVTKITKNSMTVVWNRPTVDGGSEINgyflekrdkks 27621
Cdd:COG3401     132 AGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIE----------- 200
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27622 lawlkvlketirdtrqkvtgltENSDYQYRVCAVNAAGmgpFSEPSDFYKAADPIDPPGPPAKIRIADSTKSSITLGWSK 27701
Cdd:COG3401     201 ----------------------PGTTYYYRVAATDTGG---ESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDP 255
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27702 PvydGGSDVTGYVVEMRQGEEEEWTIVstkGEARTTEYVVSNLKPGVNYYFQVSAVNCAGqgepitmtepvqakdileep 27781
Cdd:COG3401     256 V---TESDATGYRVYRSNSGDGPFTKV---ATVTTTSYTDTGLTNGTTYYYRVTAVDAAG-------------------- 309
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27782 eidldvalrtsviakagedvqllipfkgrppptvtwrkdeknlgsdarysiqntdSSSllvipqvtrndtgkyiltieng 27861
Cdd:COG3401     310 -------------------------------------------------------NES---------------------- 312
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27862 vgqPKSSTVSVKVLDT-PAACQKLQVKHVSLGTVTLLWDPPLidgGSPIINYVIEKRDATKRTWSIVSHKCSGTSFKVMD 27940
Cdd:COG3401     313 ---APSNVVSVTTDLTpPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTG 386
                           490       500       510
                    ....*....|....*....|....*....|....*..
gi 1958765569 27941 LSEKTPFFFRVLAENEIGIGEpcETTEPVKAAEVPAP 27977
Cdd:COG3401     387 LTPGTTYYYKVTAVDAAGNES--APSEEVSATTASAA 421
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
33074-33149 3.74e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 78.38  E-value: 3.74e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33074 RILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVEN 33149
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26790-26872 3.76e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.76e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26790 PGPPANITVREVTKETAVLSWDVPENDGG-APVKNYHIEKREASKKaWVSVTNNCSRLSYKVTNLQEGAVYYFRVSGENE 26868
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  26869 FGVG 26872
Cdd:smart00060    80 AGEG 83
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
31761-32032 3.85e-16

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 85.08  E-value: 3.85e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV---LVkkEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd06644      12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELedyMV--EIEILATCNHPYIVKLLGAFYWDGKLWIMIE 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGldifERINTSAFELN----EREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFG----QARQ 31909
Cdd:cd06644      90 FCPG----GAVDAIMLELDrgltEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD--IKLADFGvsakNVKT 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LKPGDNFrllFTAPEYYAPEVHQHDVVSSA-----TDMWSLGtLVYVLLSGINPFLAETN-QQMIENIMNAE-YTFDEEA 31982
Cdd:cd06644     164 LQRRDSF---IGTPYWMAPEVVMCETMKDTpydykADIWSLG-ITLIEMAQIEPPHHELNpMRVLLKIAKSEpPTLSQPS 239
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31983 fqEISLEAMDFIDRLLVKERKSRMTASEALKHPWLKQrmdRVSTKVIRTL 32032
Cdd:cd06644     240 --KWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSS---VTSNRPLREL 284
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22561-22642 3.87e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 3.87e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22561 PLPPGKITLMDVTRNSVSLSWEKPEHDGG-SRILGYIVEMQSKGSDKWATCATVKVTEATITGLIQGEEYSFRVSAQNEK 22639
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  22640 GIS 22642
Cdd:smart00060    81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15314-15405 3.96e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 3.96e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15314 PGPPINFVFEDIRKDSVLCKWEPPLDDGGsEIINYTLEKKDKtkPDSEWIVITSTLRN-CKYSVTKLIEGKEYLFRVRAE 15392
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREK--GSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|...
gi 1958765569 15393 NRFGPGPPCVSKP 15405
Cdd:cd00063      78 NGGGESPPSESVT 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
899-976 4.12e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 78.38  E-value: 4.12e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   899 PPTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVN 976
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15521-15607 4.12e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 4.12e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15521 RVADTSSTTIELEWEPPAfNGGGEIMGYFVDKQLVGTNEWSRCTEKMVKVRQFTVKEIREGADYKLRVSAVNAAGEGPPG 15600
Cdd:cd00063       8 RVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86

                    ....*..
gi 1958765569 15601 ETEPVTV 15607
Cdd:cd00063      87 ESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25808-25889 4.22e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.43  E-value: 4.22e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25808 PLPPGRVTLVDVTRNTATIKWEKPESDGG-SKITGYVVEMQTKGSEKWSTCTQVKTLEATISGLTAGEEYVFRVAAVNEK 25886
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  25887 GRS 25889
Cdd:smart00060    81 GEG 83
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
31766-32015 4.22e-16

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 84.25  E-value: 4.22e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31766 AEDLGRGEFG-IVHRcvetsskKTFMAKFVKVKgtdQVLVK------KEISILNIA-RHRNILYLHESFESMEELVMIFE 31837
Cdd:cd13982       6 PKVLGYGSEGtIVFR-------GTFDGRPVAVK---RLLPEffdfadREVQLLRESdEHPNVIRYFCTEKDRQFLYIALE 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 F--ISGLDIFERINTSA-FELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENII--YQTRKNSI-IKIIEFGQARQLK 31911
Cdd:cd13982      76 LcaASLQDLVESPRESKlFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILisTPNAHGNVrAMISDFGLCKKLD 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDN-FRLLFTAPEYY---APEV---HQHDVVSSATDMWSLGTLVYVLLS-GINPFlaETNQQMIENIMNAEYTFDEEAF 31983
Cdd:cd13982     156 VGRSsFSRRSGVAGTSgwiAPEMlsgSTKRRQTRAVDIFSLGCVFYYVLSgGSHPF--GDKLEREANILKGKYSLDKLLS 233
                           250       260       270
                    ....*....|....*....|....*....|...
gi 1958765569 31984 Q-EISLEAMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd13982     234 LgEHGPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
31769-32018 4.37e-16

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 85.48  E-value: 4.37e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTF----MAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05597       9 IGRGAFGEVAVVKLKSTEKVYamkiLNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDYYCGGDL 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERIntSAFE--LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQArqLKPGDNFRLLFT- 31921
Cdd:cd05597      89 LTLL--SKFEdrLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLD--RNGHIRLADFGSC--LKLREDGTVQSSv 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 ---APEYYAPEVHQ-----HDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTF----DEEafqEISLE 31989
Cdd:cd05597     163 avgTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHFsfpdDED---DVSEE 239
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 31990 AMDFIDRLL--VKERKSRMTASEALKHPWLK 32018
Cdd:cd05597     240 AKDLIRRLIcsRERRLGQNGIDDFKKHPFFE 270
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28961-29045 4.82e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.69  E-value: 4.82e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28961 PGPPGPITFKDVTRGSATLMWDAPLLDGGaRIHHYVIEKREASRRSWQVVSEK-CTRQILKVSDLTEGVPYYFRVSAENE 29039
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*.
gi 1958765569 29040 YGVGEP 29045
Cdd:cd00063      80 GGESPP 85
I-set pfam07679
Immunoglobulin I-set domain;
6446-6536 4.86e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 78.45  E-value: 4.86e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKeKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDG 6525
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK-DGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  6526 GVRENMASLTV 6536
Cdd:pfam07679    80 GEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22167-22250 4.88e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.43  E-value: 4.88e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22167 PDPPKNPEVTTITKDSMVVCWGHPDSDGG-SEIINYIVERRDKaGQRWVKCNKKAlTDLRFKVSGLTEGHEYEFRIMAEN 22245
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  22246 AAGVS 22250
Cdd:smart00060    79 GAGEG 83
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
31761-32018 5.10e-16

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 86.60  E-value: 5.10e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVH----RCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd05624      72 DDFEIIKVIGRGAFGEVAvvkmKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVM 151
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNF 31916
Cdd:cd05624     152 DYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDM--NGHIRLADFGSCLKMNDDGTV 229
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 R--LLFTAPEYYAPEVHQ--HDVVSS---ATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNaeytfDEEAFQ----- 31984
Cdd:cd05624     230 QssVAVGTPDYISPEILQamEDGMGKygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMN-----HEERFQfpshv 304
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1958765569 31985 -EISLEAMDFIDRLLV-KERKSRMTASEALK-HPWLK 32018
Cdd:cd05624     305 tDVSEEAKDLIQRLICsRERRLGQNGIEDFKkHAFFE 341
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
31771-32017 5.39e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 83.91  E-value: 5.39e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31771 RGEFGIVHRCVETSSKKTFMAKFVKVkgtDQvLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERINt 31850
Cdd:cd13995      14 RGAFGKVYLAQDTKTKKRMACKLIPV---EQ-FKPSDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKLE- 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31851 SAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiikIIEFGQARQLKPGDNF-RLLFTAPEYYAPE 31929
Cdd:cd13995      89 SCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV---LVDFGLSVQMTEDVYVpKDLRGTEIYMSPE 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31930 VHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIEN---IMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRM 32006
Cdd:cd13995     166 VILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSylyIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNHRS 245
                           250
                    ....*....|.
gi 1958765569 32007 TASEALKHPWL 32017
Cdd:cd13995     246 SAAELLKHEAL 256
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8804-8886 5.48e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 78.32  E-value: 5.48e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8804 EPLKVTVGDSASLQCQLAGTPEIGVSWYK-GDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGEVSSST 8882
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   8883 FLTV 8886
Cdd:smart00410    82 TLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26887-26968 5.54e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.04  E-value: 5.54e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26887 PSPPEKLGVTSVSKDSVSLSWLKPEHDGG-SRILHYVVEALEKGQKNWVKCAVVKTTHHVVSGLREGHEYFFRVFAENQA 26965
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  26966 GLS 26968
Cdd:smart00060    81 GEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7113-7196 5.59e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 78.32  E-value: 5.59e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7113 PVSIDVIAGESADFECHVTGAQPMRVTWSKDN-KEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCS 7191
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   7192 AQLSV 7196
Cdd:smart00410    81 TTLTV 85
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
31769-32020 5.69e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 85.65  E-value: 5.69e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI-F 31845
Cdd:PLN00034     82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRrqICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLeG 161
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINtsafelNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK----PGDNF--RLL 31919
Cdd:PLN00034    162 THIA------DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN--VKIADFGVSRILAqtmdPCNSSvgTIA 233
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFlAETNQQMIENIMNA-EYTFDEEAFQEISLEAMDFIDRLL 31998
Cdd:PLN00034    234 YMSPERINTDLNHGAYDGYAGDIWSLGVSILEFYLGRFPF-GVGRQGDWASLMCAiCMSQPPEAPATASREFRHFISCCL 312
                           250       260
                    ....*....|....*....|..
gi 1958765569 31999 VKERKSRMTASEALKHPWLKQR 32020
Cdd:PLN00034    313 QREPAKRWSAMQLLQHPFILRA 334
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26099-26183 5.91e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.31  E-value: 5.91e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26099 PGPPGTPKVVHATKSTMVVSWQVPVNDGGsQVIGYHLEYKERSSILWSKANKVLIADTQMKVSGLDEGLLYEYRVYAENI 26178
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                    ....*
gi 1958765569 26179 AGIGK 26183
Cdd:cd00063      80 GGESP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20396-20484 6.33e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.31  E-value: 6.33e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20396 PGPVVDLKVLAVTKSSCTIGWKKPRSDGGsRITGYVVDF-LTEENKWQRVMKSLSLQYST--KDLKEGKEYTFRVSAENE 20472
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYrEKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 20473 NGEGTPSEIMVV 20484
Cdd:cd00063      80 GGESPPSESVTV 91
I-set pfam07679
Immunoglobulin I-set domain;
9671-9757 6.70e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 78.07  E-value: 6.70e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9671 QFTKRIQNIVVSEHQSATFECEVSFD-DAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARlEPRG 9749
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT-NSAG 80

                    ....*...
gi 1958765569  9750 EARSTAEL 9757
Cdd:pfam07679    81 EAEASAEL 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15314-15398 6.87e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.04  E-value: 6.87e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15314 PGPPINFVFEDIRKDSVLCKWEPPLDDGG-SEIINYTLEKKDKtkpDSEWIVITSTLRNCKYSVTKLIEGKEYLFRVRAE 15392
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE---GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  15393 NRFGPG 15398
Cdd:smart00060    78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28664-28748 6.94e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.04  E-value: 6.94e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28664 PDAPGIPEPSNVTGNSITLTWTRPESDGGN-EIQHYILERREkKSTRWVKVisKRPISETRFKVTGLVEGNEYEFHVMAE 28742
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYRE-EGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  28743 NAAGVG 28748
Cdd:smart00060    78 NGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26729-27214 7.17e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 87.75  E-value: 7.17e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26729 NVSWSKPDTDLRTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTFVVKVLDSPGPPANitvreVTKETAVL 26808
Cdd:COG3401      86 AAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDG-----ANASGTTA 160
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26809 SWDVPENDGGAPVKNYHIEKREASKKAWVSVTNncsrlsYKVTNLQEGAVYYFRVSGENEFGVGVPAETKEGVKITEKPS 26888
Cdd:COG3401     161 SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLV------DGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPS 234
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26889 PPEKLGVTSVSKDSVSLSWLKPEhdgGSRILHYVVEALEKGQKNWVKCAVVKTTHHVVSGLREGHEYFFRVFAENQAGL- 26967
Cdd:COG3401     235 APTGLTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNe 311
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26968 SDPRElllPVLIKDHLEPPEIdmknfPSHTVYVRAGSNlkvdipisgkplpKVTLSRDGVPLKATMRFNTE--ITAENLT 27045
Cdd:COG3401     312 SAPSN---VVSVTTDLTPPAA-----PSGLTATAVGSS-------------SITLSWTASSDADVTGYNVYrsTSGGGTY 370
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27046 INLKESVTA--------DAGK---YEITAANSSGTTKTFINII----VLDRPGPPTGPVAISDITEESVTLKW-----EP 27105
Cdd:COG3401     371 TKIAETVTTtsytdtglTPGTtyyYKVTAVDAAGNESAPSEEVsattASAASGESLTASVDAVPLTDVAGATAaasaaSN 450
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27106 PKYDGGSHVTNYIVLKRETSTAVWTEVSATVARTMIKVMKLTTGEEYQFRIKAENRFGISDHIDSACVVVKLPYTTPGPP 27185
Cdd:COG3401     451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNV 530
                           490       500
                    ....*....|....*....|....*....
gi 1958765569 27186 STPWVSNVTrESITVGWHEPVSNGGSAVI 27214
Cdd:COG3401     531 TGASPVTVG-ASTGDVLITDLVSLTTSAS 558
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5696-5774 7.54e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 77.61  E-value: 7.54e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5696 PPQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARN 5774
Cdd:pfam13927     1 KPVITVSPSSVTV-REGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
31806-32016 7.76e-16

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 83.91  E-value: 7.76e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31806 KEISILNIARHRNILYLHESFE-SMEELVMIFEFISG--LDIFERINTSafeLNEREVVSYVRQVCEALEFL--HSQNIG 31880
Cdd:cd13990      53 REYEIHKSLDHPRIVKLYDVFEiDTDSFCTVLEYCDGndLDFYLKQHKS---IPEREARSIIMQVVSALKYLneIKPPII 129
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31881 HFDIRPENIIYQTRKNS-IIKIIEFGQARQLkPGDNFR---LLFTAPE-----YYAPEV----HQHDVVSSATDMWSLGT 31947
Cdd:cd13990     130 HYDLKPGNILLHSGNVSgEIKITDFGLSKIM-DDESYNsdgMELTSQGagtywYLPPECfvvgKTPPKISSKVDVWSVGV 208
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31948 LVYVLLSGINPFLAETNQQMI--EN-IMNA-EYTFDEEAfqEISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd13990     209 IFYQMLYGRKPFGHNQSQEAIleENtILKAtEVEFPSKP--VVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16729-16812 7.95e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 77.65  E-value: 7.95e-16
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16729 PGPPVGpIKFESISADQMTLSWLPPKDDGG-SKITNYVIEKREANRKtWVRVSSEPKECMYTIPKLLEGHEYVFRIMAQN 16807
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  16808 KYGIG 16812
Cdd:smart00060    79 GAGEG 83
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
31761-32032 8.20e-16

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 83.92  E-value: 8.20e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV---LVkkEISILNIARHRNILYLHESFESMEELVMIFE 31837
Cdd:cd06643       5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELedyMV--EIDILASCDHPNIVKLLDAFYYENNLWILIE 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFG----QARQLKPG 31913
Cdd:cd06643      83 FCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGD--IKLADFGvsakNTRTLQRR 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFrllFTAPEYYAPEVHQHDVVSS-----ATDMWSLGtLVYVLLSGINPFLAETN-QQMIENIMNAE-YTFDEEAfqEI 31986
Cdd:cd06643     161 DSF---IGTPYWMAPEVVMCETSKDrpydyKADVWSLG-VTLIEMAQIEPPHHELNpMRVLLKIAKSEpPTLAQPS--RW 234
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569 31987 SLEAMDFIDRLLVKERKSRMTASEALKHPWLKQrmdRVSTKVIRTL 32032
Cdd:cd06643     235 SPEFKDFLRKCLEKNVDARWTTSQLLQHPFVSV---LVSNKPLREL 277
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29674-30242 8.37e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 87.37  E-value: 8.37e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29674 SLPQEDGGAEITHYIVERRETSRLNWVIVEAECLTLSYVVTRLiKNNEYTFRVRAVNKYGLGVPIESEPIVARNSFTIPS 29753
Cdd:COG3401      64 GGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGA-TNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYA 142
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29754 QPGIPEGVGAGKEHIIIQWTKPESDGGNEISNYLVDKREKKSLRWTRVNKDYVVYDtrlkvtsLMEGCDYQFRVTAVNSA 29833
Cdd:COG3401     143 LGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGD-------IEPGTTYYYRVAATDTG 215
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29834 GNSEPSEASNFISCREPsytPGPPSAPRVVDTTKSSISLAWTKPmydGGTDIIGYVLEMQEKDTDQWCRVhtnTTIRNNE 29913
Cdd:COG3401     216 GESAPSNEVSVTTPTTP---PSAPTGLTATADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKV---ATVTTTS 286
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29914 FTVPDLKMGQKYSFRVAAVNAKG-MSDYSETtaeiepverleipdleladdlkktviiragaslrlmVSVSGRPSPvitw 29992
Cdd:COG3401     287 YTDTGLTNGTTYYYRVTAVDAAGnESAPSNV------------------------------------VSVTTDLTP---- 326
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29993 skkgidlanraiidntesysllivdkvnrydagkytieaenqsgkksatvlvkvydtPGPCPSVNVKEVSRDSVTITWEI 30072
Cdd:COG3401     327 ---------------------------------------------------------PAAPSGLTATAVGSSSITLSWTA 349
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30073 PTidgGAPVNNYIIEKREAAMRAFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENIYGI-GEPCETSDAVLVSEVPLVPT 30151
Cdd:COG3401     350 SS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESL 426
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30152 KLEVVDVT------KSTVTLAWEKPLYDGGSRLTGYVLEACKAGTERWMKVVTLKPTVLDH----TVISLNEGEQYLFRV 30221
Cdd:COG3401     427 TASVDAVPltdvagATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTAnlsvTTGSLVGGSGASSVT 506
                           570       580
                    ....*....|....*....|.
gi 1958765569 30222 RAQNEKGVSEPREIVTPVTVQ 30242
Cdd:COG3401     507 NSVSVIGASAAAAVGGAPDGT 527
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
31769-32015 8.41e-16

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 83.20  E-value: 8.41e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGT---DQVLVKKEISIL-NIARHRNILYLHESFESMEELVMIFEFISG--L 31842
Cdd:cd13997       8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRgpkERARALREVEAHaALGQHPNIVRYYSSWEEGGHLYIQMELCENgsL 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLlfTA 31922
Cdd:cd13997      88 QDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGT--CKIGDFGLATRLETSGDVEE--GD 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PEYYAPEVHQ-HDVVSSATDMWSLGTLVYVLLSGIN-PflaeTNQQMIENIMNAEYTFDEEAfqEISLEAMDFIDRLLVK 32000
Cdd:cd13997     164 SRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPlP----RNGQQWQQLRQGKLPLPPGL--VLSQELTRLLKVMLDP 237
                           250
                    ....*....|....*
gi 1958765569 32001 ERKSRMTASEALKHP 32015
Cdd:cd13997     238 DPTRRPTADQLLAHD 252
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
21185-21272 9.34e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.92  E-value: 9.34e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21185 PGPPSNAHVTDTTKKSASLAWGKPHYDGGlEITGYVVEHQKVGDDAWIKdTTGTALRITQFVVPDLQTKEKYNFRISAVN 21264
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKE-VEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                    ....*...
gi 1958765569 21265 DAGVGEPA 21272
Cdd:cd00063      79 GGGESPPS 86
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
31758-32017 9.54e-16

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 84.55  E-value: 9.54e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK---KEISILNIARHRNILYLHESFES-MEELV 31833
Cdd:cd07856       7 EITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKrtyRELKLLKHLRHENIISLSDIFISpLEDIY 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFIsGLDIfERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPG 31913
Cdd:cd07856      87 FVTELL-GTDL-HRLLTSR-PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNIL--VNENCDLKICDFGLARIQDPQ 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 dnfRLLFTAPEYY-APEV----HQHDVvssATDMWSLGTLVYVLLSG---------INPF------LAETNQQMIENIMn 31973
Cdd:cd07856     162 ---MTGYVSTRYYrAPEImltwQKYDV---EVDIWSAGCIFAEMLEGkplfpgkdhVNQFsiitelLGTPPDDVINTIC- 234
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31974 AEYTFD-------------EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07856     235 SENTLRfvqslpkrervpfSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
22230-22622 9.77e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 87.37  E-value: 9.77e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22230 GLTEGHEYEFRIMAENAAGVSAPSATSPFYKACDsvfKPGPPGNPRVLDTSRSSISIAWNKPiydGGSEITGYMVEIALP 22309
Cdd:COG3401     198 DIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTT---PPSAPTGLTATADTPGSVTLSWDPV---TESDATGYRVYRSNS 271
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22310 EEDEWQVVtppAGLKATSYTITNLIENQEYKIRIYAMNSEGlgepalvpgtpkaeermlppeieldadlrkvvtiracct 22389
Cdd:COG3401     272 GDGPFTKV---ATVTTTSYTDTGLTNGTTYYYRVTAVDAAG--------------------------------------- 309
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22390 lrlfvpikgrpapevkwarehgesldkasIESTSSYTLLVVGNVNrfdsgkyiltvenssgsksafvnvrvldTPGPPQN 22469
Cdd:COG3401     310 -----------------------------NESAPSNVVSVTTDLT----------------------------PPAAPSG 332
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22470 LKIKEVTKTSVTLTWEPPLldgGSKIKNYIVEKRESTRKAYSTVATNCHKTSWKIDQLQEGCSYYFRVLAENEYGI-GLP 22548
Cdd:COG3401     333 LTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAP 409
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 22549 AETAESVKASERPLPPGK--ITLMDVTRNSVSLSWEKPEHDGGSRILGYIVemqsKGSDKWATCATVKVTEATITG 22622
Cdd:COG3401     410 SEEVSATTASAASGESLTasVDAVPLTDVAGATAAASAASNPGVSAAVLAD----GGDTGNAVPFTTTSSTVTATT 481
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28893-29307 1.01e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.98  E-value: 1.01e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28893 YQGRPTPTAVWSKPDSNLSIRADIHT-TDSFSTLTVENCNRNDAGK---YTLTVENNSGRKSITFTVKVLDS---PGPPG 28965
Cdd:COG3401     158 TTASSVAGAGVVVSPDTSATAAVATTsLTVTSTTLVDGGGDIEPGTtyyYRVAATDTGGESAPSNEVSVTTPttpPSAPT 237
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28966 PITFKDVTRGSATLMWDAPLLDGGARihhYVIEKREASRRSWQVVSEKCTRQILkVSDLTEGVPYYFRVSAENEYGVGEP 29045
Cdd:COG3401     238 GLTATADTPGSVTLSWDPVTESDATG---YRVYRSNSGDGPFTKVATVTTTSYT-DTGLTNGTTYYYRVTAVDAAGNESA 313
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29046 YEmpEPIVAT---EQPAPPRRLDVVDTSKSSAVLAWlkpEHDGGSRITSYLLEMRQKGSDFWVEAGHT-KQLTFTVERLV 29121
Cdd:COG3401     314 PS--NVVSVTtdlTPPAAPSGLTATAVGSSSITLSW---TASSDADVTGYNVYRSTSGGGTYTKIAETvTTTSYTDTGLT 388
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29122 ENTEYEFRVKAKNDAGYSEPREAFSSVIIKEPQIEPTADLTGITNQLITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLK 29201
Cdd:COG3401     389 PGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAV 468
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29202 ETDRMSITTTKDRTT----LTVKDSMRGDSGRYFLTLENTAGVKTFTITVVVIGRPGPVTGPIEVSSVSAESCVLSWSEP 29277
Cdd:COG3401     469 PFTTTSSTVTATTTDtttaNLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLIT 548
                           410       420       430
                    ....*....|....*....|....*....|
gi 1958765569 29278 KDDGGTEITNYIVEKRESGTTAWQLINSSV 29307
Cdd:COG3401     549 DLVSLTTSASSSVSGAGLGSGNLYLITTLG 578
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
31760-32017 1.02e-15

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 83.04  E-value: 1.02e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYmiAEDLGRGEFGIVHRCVETSSKKTfMA----KFVKVKGTDQVLVKKEISILNIARHRNILYLHESFES--MEELV 31833
Cdd:cd13983       2 YLKF--NEVLGRGSFKTVYRAFDTEEGIE-VAwneiKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESksKKEVI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQN--IGHFDIRPENiIYQTRKNSIIKIIEFGQARQLK 31911
Cdd:cd13983      79 FITELMTSGTLKQYLKRFKR-LKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDN-IFINGNTGEVKIGDLGLATLLR 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFRLLFTaPEYYAPEVHQHDVVSSAtDMWSLGTLVYVLLSGINPFLAETN-----QQMIENIMnaeytfdEEAFQEI 31986
Cdd:cd13983     157 QSFAKSVIGT-PEFMAPEMYEEHYDEKV-DIYAFGMCLLEMATGEYPYSECTNaaqiyKKVTSGIK-------PESLSKV 227
                           250       260       270
                    ....*....|....*....|....*....|..
gi 1958765569 31987 -SLEAMDFIDRLLVKeRKSRMTASEALKHPWL 32017
Cdd:cd13983     228 kDPELKDFIEKCLKP-PDERPSARELLEHPFF 258
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
31739-31972 1.05e-15

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 84.65  E-value: 1.05e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31739 EVDETREVTMTKASHSKTKELYEKYMIAEDLGRGEFGIV-------HRCVETSSKKTFMAKFVKVKGTDQVLVKKEIsiL 31811
Cdd:PTZ00426      8 QLHKKKDSDSTKEPKRKNKMKYEDFNFIRTLGTGSFGRVilatyknEDFPPVAIKRFEKSKIIKQKQVDHVFSERKI--L 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31812 NIARHRNILYLHESFESMEELVMIFEFISGLDIFERINTSAFELNEREVVsYVRQVCEALEFLHSQNIGHFDIRPENIIY 31891
Cdd:PTZ00426     86 NYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCF-YAAQIVLIFEYLQSLNIVYRDLKPENLLL 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31892 QtrKNSIIKIIEFGQARQLKpgDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE----TNQQM 31967
Cdd:PTZ00426    165 D--KDGFIKMTDFGFAKVVD--TRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANepllIYQKI 240

                    ....*
gi 1958765569 31968 IENIM 31972
Cdd:PTZ00426    241 LEGII 245
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1038-1127 1.06e-15

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 77.54  E-value: 1.06e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVsYNKQTGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM-LVRENGRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|
gi 1958765569  1118 HGETSASASL 1127
Cdd:cd05744      80 AGENSFNAEL 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
24628-24719 1.11e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.54  E-value: 1.11e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24628 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGaKVKNYVIDKRESTRKAYANVSSKCSK-TSFKVENLTEGAIYYFRVMAENE 24706
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 24707 FGVGVPAETSDAV 24719
Cdd:cd00063      80 GGESPPSESVTVT 92
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
31758-32022 1.20e-15

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 84.71  E-value: 1.20e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEKYMIAEDLGRGEFGIVhrCVETSSKKTFMAKFVKVKGTDQVLVK-----KEISILNIARHRNILYLHESF---ESM 31829
Cdd:cd07877      14 EVPERYQNLSPVGSGAYGSV--CAAFDTKTGLRVAVKKLSRPFQSIIHakrtyRELRLLKHMKHENVIGLLDVFtpaRSL 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EEL--VMIFEFISGLDIFERINTSafELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIiyQTRKNSIIKIIEFGQA 31907
Cdd:cd07877      92 EEFndVYLVTHLMGADLNNIVKCQ--KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNL--AVNEDCELKILDFGLA 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLkpgDNFRLLFTAPEYY-APEV-----HQHDVVssatDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEE 31981
Cdd:cd07877     168 RHT---DDEMTGYVATRWYrAPEImlnwmHYNQTV----DIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAE 240
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31982 AFQEISLE---------------------------AMDFIDRLLVKERKSRMTASEALKHPWLKQRMD 32022
Cdd:cd07877     241 LLKKISSEsarnyiqsltqmpkmnfanvfiganplAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHD 308
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17524-17607 1.23e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 77.27  E-value: 1.23e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17524 PDAPEQPVVTEVTKDSALVTWNKPND--GGKPITNYILEKRETmSKRWVRVTKEPihPYTKYRVPDLLEGCQYEFRVSAE 17601
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVGYRVEYREE-GSEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  17602 NEIGIG 17607
Cdd:smart00060    78 NGAGEG 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
107-193 1.28e-15

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 77.23  E-value: 1.28e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   107 SQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGD-LYSLLIAEAYPEDSGTYSVNATNSVGRA 185
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569   186 TSTADLLV 193
Cdd:cd20973      81 TCSAELTV 88
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
31769-32016 1.29e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 82.82  E-value: 1.29e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK------EISILNIARHRNILYLHESFESMEE--LVMIFEFIS 31840
Cdd:cd06651      15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEvsalecEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 94
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK----PGDNF 31916
Cdd:cd06651      95 GGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN--VKLGDFGASKRLQticmSGTGI 171
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 RLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENImnAEYTFDEEAFQEISLEAMDFIDR 31996
Cdd:cd06651     172 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI--ATQPTNPQLPSHISEHARDFLGC 249
                           250       260
                    ....*....|....*....|
gi 1958765569 31997 LLVkERKSRMTASEALKHPW 32016
Cdd:cd06651     250 IFV-EARHRPSAEELLRHPF 268
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7584-7666 1.30e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 77.16  E-value: 1.30e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7584 KDTTATLGASVVLECRVSGSAPISVGWFLDGNE-IISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQDESSA 7662
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   7663 LLTV 7666
Cdd:smart00410    82 TLTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17424-17516 1.35e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.54  E-value: 1.35e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17424 PGPPVGPVVfDEVTKEYMVISWKPPLDDGGsEITNYIIEKKELGKDIWMPVTSASAKTT-CKVPKLLEGKDYIFRIHAEN 17502
Cdd:cd00063       1 PSPPTNLRV-TDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETsYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 17503 LYGISDPLVSDSMK 17516
Cdd:cd00063      79 GGGESPPSESVTVT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6547-6629 1.37e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 77.16  E-value: 1.37e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6547 GSMTVTVGETCSLECKVAGTPELSVEWYKDG-KLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTA 6625
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   6626 VVDV 6629
Cdd:smart00410    82 TLTV 85
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
31758-32016 1.37e-15

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 83.43  E-value: 1.37e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEK-YMIAEdlgrGEFGIVHRCVETSSKKTFMAKFVKVKGTDQ---VLVKKEISILNIARHRNILYLHESF--ESMEE 31831
Cdd:cd07843       5 DEYEKlNRIEE----GTYGVVYRARDKKTGEIVALKKLKMEKEKEgfpITSLREINILLKLQHPNIVTVKEVVvgSNLDK 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISgLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRknSIIKIIEFGQARQL- 31910
Cdd:cd07843      81 IYMVMEYVE-HDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNR--GILKICDFGLAREYg 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNFRLLFTAPEYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGiNPFLA---ETNQqmIENIMNAEYTFDEEA---- 31982
Cdd:cd07843     158 SPLKPYTQLVVTLWYRAPELlLGAKEYSTAIDMWSVGCIFAELLTK-KPLFPgksEIDQ--LNKIFKLLGTPTEKIwpgf 234
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31983 ----------------------FQEISL--EAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07843     235 selpgakkktftkypynqlrkkFPALSLsdNGFDLLNRLLTYDPAKRISAEDALKHPY 292
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
899-989 1.46e-15

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 77.29  E-value: 1.46e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDfQITFQSGIARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd20976      80 GQVSCSAWVTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14992-15074 1.47e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.88  E-value: 1.47e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14992 PGPCKDIKASDITKSSCKLTWEPPEFDGG-SPILHYVLERREAGRRtYIPVMSGENKLSWTVKDLIPNGEYFFRVKAVNK 15070
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  15071 IGGG 15074
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
24835-24913 1.64e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.91  E-value: 1.64e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 24835 VQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVIV 24913
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
31763-32014 1.69e-15

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 82.73  E-value: 1.69e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV-LVKKEISILNIARHRNILYLHESfESME------ELVMI 31835
Cdd:cd13986       2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVkEAMREIENYRLFNHPNILRLLDS-QIVKeaggkkEVYLL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISG---LDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQN---IGHFDIRPENIIYqTRKNSIIkIIEFG---- 31905
Cdd:cd13986      81 LPYYKRgslQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLL-SEDDEPI-LMDLGsmnp 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31906 -----------QARQLKPGDNFRLLFTAPEYYAPEVHQhdVVSSATDMWSLGTLVYVLLSGINPFlaetnqQMIEN---- 31970
Cdd:cd13986     159 arieiegrreaLALQDWAAEHCTMPYRAPELFDVKSHC--TIDEKTDIWSLGCTLYALMYGESPF------ERIFQkgds 230
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 1958765569 31971 ----IMNAEYTFDEEAfqEISLEAMDFIDRLLVKERKSRMTASEALKH 32014
Cdd:cd13986     231 lalaVLSGNYSFPDNS--RYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
I-set pfam07679
Immunoglobulin I-set domain;
3019-3102 1.81e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.91  E-value: 1.81e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3019 EFRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVA----GG 3093
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  3094 NMSTANLFV 3102
Cdd:pfam07679    82 AEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27679-27763 1.91e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.50  E-value: 1.91e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27679 PGPPAKIRIADSTKSSITLGWSKPVYDGG-SDVTGYVVEMRQgEEEEWTIVSTKGeaRTTEYVVSNLKPGVNYYFQVSAV 27757
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  27758 NCAGQG 27763
Cdd:smart00060    78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20000-20083 1.97e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.50  E-value: 1.97e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20000 PGRCDPPVISNITKDHMTVSWKAPADDGG-SPITGYLVEKRETQAvNWTKVNRKPvIERTLKATGLQEGTEYEFRVTAIN 20078
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  20079 KAGPG 20083
Cdd:smart00060    79 GAGEG 83
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
31758-32022 2.00e-15

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 83.95  E-value: 2.00e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKfvKVKGTDQVLVK-----KEISILNIARHRNILYLHESFE---SM 31829
Cdd:cd07878      12 EVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVK--KLSRPFQSLIHarrtyRELRLLKHMKHENVIGLLDVFTpatSI 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EEL--VMIFEFISGLDIFERINTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIiyQTRKNSIIKIIEFGQA 31907
Cdd:cd07878      90 ENFneVYLVTNLMGADLNNIVKCQK--LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV--AVNEDCELRILDFGLA 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQlkpGDNFRLLFTAPEYY-APEV-----HQHDVVssatDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEE 31981
Cdd:cd07878     166 RQ---ADDEMTGYVATRWYrAPEImlnwmHYNQTV----DIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPE 238
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31982 AFQEISLE---------------------------AMDFIDRLLVKERKSRMTASEALKHPWLKQRMD 32022
Cdd:cd07878     239 VLKKISSEharkyiqslphmpqqdlkkifrganplAIDLLEKMLVLDSDKRISASEALAHPYFSQYHD 306
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16217-16302 2.01e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.50  E-value: 2.01e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16217 PGPPSCPEVKDKTKSSISLAWKPPAKDGG-SPIKGYIVEMQEEGTtDWKKVNEPDkllTACECVVPNLKELRKYRFRVKA 16295
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP---SSTSYTLTGLKPGTEYEFRVRA 76

                     ....*..
gi 1958765569  16296 VNEAGES 16302
Cdd:smart00060    77 VNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23546-23628 2.07e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.50  E-value: 2.07e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23546 PSPPVNLKVTEITKDSVSITWEPPLLDGG-SKIKNYIVEKREaTRKSYAAVVTNCHKNSWKIDQLQEGCSYYFRVTAENE 23624
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  23625 YGIG 23628
Cdd:smart00060    80 AGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
18429-18510 2.09e-15

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 76.47  E-value: 2.09e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18429 VITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAqgSAIV 18508
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEK--SATI 78

                    ..
gi 1958765569 18509 NV 18510
Cdd:cd05748      79 NV 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19009-19098 2.15e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.50  E-value: 2.15e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19009 PGPPTNFKVVDTTKNSITLAWGKPVYDGG-APIIGYVVEMRPKiadaspDEGWKRCNAAAQlvRMEFTVTSLDENQEYEF 19087
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE------GSEWKEVNVTPS--STSYTLTGLKPGTEYEF 72
                             90
                     ....*....|.
gi 1958765569  19088 RVCAQNQVGIG 19098
Cdd:smart00060    73 RVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
20588-20680 2.18e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.77  E-value: 2.18e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20588 PGIPTGpIKFDEVTAEAMTLKWGPPKDDGGsEITNYVLEKRDSVNNKWVTCAS-AVQKTTFRVTRLHEGIEYTFRVSAEN 20666
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 20667 KYGVGEGLKSEPIV 20680
Cdd:cd00063      79 GGGESPPSESVTVT 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6932-7001 2.38e-15

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 75.83  E-value: 2.38e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6932 VSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTAASKTV 7001
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
fn3 pfam00041
Fibronectin type III domain;
19212-19296 2.61e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 76.30  E-value: 2.61e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19212 GPVSDLKVSDVTKTSCHVSWAPPEnDGGSPVTHYIVEKREA---ERKTWSTVTPEvkKTSFNVTNLVPGNEYFFRVTAVN 19288
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnsgEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*...
gi 1958765569 19289 EYGPGVPT 19296
Cdd:pfam00041    78 GGGEGPPS 85
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
31769-31973 2.79e-15

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 82.93  E-value: 2.79e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGivhrcvetsskKTFMAKFvkvKGTDQV----LVKKEI--------------SILNIA-RHRNILYLHESFESM 31829
Cdd:cd05591       3 LGKGSFG-----------KVMLAER---KGTDEVyaikVLKKDVilqdddvdctmtekRILALAaKHPFLTALHSCFQTK 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGLDIFERINtSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ 31909
Cdd:cd05591      69 DRLFFVMEYVNGGDLMFQIQ-RARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGH--CKLADFGMCKE 145
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31910 -LKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMN 31973
Cdd:cd05591     146 gILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH 210
I-set pfam07679
Immunoglobulin I-set domain;
18026-18112 2.83e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.53  E-value: 2.83e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18026 VKLIEGLVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKT 18105
Cdd:pfam07679     4 TQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAE 83

                    ....*..
gi 1958765569 18106 VAVHLTV 18112
Cdd:pfam07679    84 ASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7209-7290 2.90e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 76.39  E-value: 2.90e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7209 SKVAKQGESIQLECKISGSPEIKVVWFRNDSE-LHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVGHASCSTA 7287
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   7288 LKV 7290
Cdd:smart00410    83 LTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29854-29938 2.93e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.11  E-value: 2.93e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29854 PGPPSAPRVVDTTKSSISLAWTKPMYDGGTD-IIGYVLEMQEKDtDQWCRVHTNTTirNNEFTVPDLKMGQKYSFRVAAV 29932
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEG-SEWKEVNVTPS--STSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  29933 NAKGMS 29938
Cdd:smart00060    78 NGAGEG 83
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
31763-31977 2.98e-15

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 81.78  E-value: 2.98e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMA---------KFVKVKGTDQVLVKKEISILNIA----RHRNILYLHESFESM 31829
Cdd:cd08528       2 YAVLELLGSGAFGCVYKVRKKSNGQTLLAlkeinmtnpAFGRTEQERDKSVGDIISEVNIIkeqlRHPNIVRYYKTFLEN 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGLDIFERINT---SAFELNEREVVSYVRQVCEALEFLHSQN-IGHFDIRPENIIYQTrkNSIIKIIEFG 31905
Cdd:cd08528      82 DRLYIVMELIEGAPLGEHFSSlkeKNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGE--DDKVTITDFG 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31906 QARQlKPGDNFRLLFTAPE--YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYT 31977
Cdd:cd08528     160 LAKQ-KGPESSKMTSVVGTilYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYE 232
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14395-14478 3.11e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.11  E-value: 3.11e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14395 PGPPTRLEPSDITKDAVTLTWCEPDDDGG-SPITGYWVERlDPDTDKWVRCNKmPVKDTTYRVKGLTNKKKYRFRVLAEN 14473
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEY-REEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  14474 LAGPG 14478
Cdd:smart00060    79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27082-27175 3.15e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.38  E-value: 3.15e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27082 PGPPTGPVaISDITEESVTLKWEPPKYDGGsHVTNYIVLKRETSTAVWTEVSATVA-RTMIKVMKLTTGEEYQFRIKAEN 27160
Cdd:cd00063       1 PSPPTNLR-VTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1958765569 27161 RFGISDHIDSACVVV 27175
Cdd:cd00063      79 GGGESPPSESVTVTT 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1038-1130 3.20e-15

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 76.31  E-value: 3.20e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLT-TGYRYKVSYNKQTGECRLVISMTFADDAGEYTIVIRN 1116
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDpSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  1117 KHGETSASASLLEE 1130
Cdd:cd20951      81 IHGEASSSASVVVE 94
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18809-18891 3.23e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 76.11  E-value: 3.23e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18809 PGPVRNLKIADVSSDRCTIRWDPPEDDGG-CEIQNYILEKCEsKRMVWSTYSANVLTPGATVTRLIEGNEYIFRVRAENK 18887
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  18888 IGTG 18891
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
1249-1337 3.28e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.14  E-value: 3.28e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFlQDGRASLRIPVVLPEDEGIYTAFASNIKGN 1328
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTY-EGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569  1329 AICSGKLYV 1337
Cdd:pfam07679    82 AEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4299-4381 3.29e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 76.00  E-value: 3.29e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4299 EPLEVALGHLAKFTCEIQGAPNVRFQWFK-AGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYGSVSCTA 4377
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   4378 TLTV 4381
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
13805-13890 3.30e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.91  E-value: 3.30e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13805 SPPVNLSASEQTQSSVQLTWEPPlKDGGSPILGYIIERQEEGK-DNWIRCNMKPvPELTYKVTGLQKGNKYLYRVSAENA 13883
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSgEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 13884 AGVSDPS 13890
Cdd:pfam00041    79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
31634-31715 3.50e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.73  E-value: 3.50e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31634 PDPPRGVKVSDVSRDSVNLTWTEPASDGG-SKVTNYIVEKCaTTAERWLRV-GQARETRYTVVNLFGKTSYQFRVIAENK 31711
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYR-EEGSEWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  31712 FGLS 31715
Cdd:smart00060    80 AGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
23149-23241 3.72e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.00  E-value: 3.72e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23149 PGPPEGPVaISGVTAEKCMLAWKPPlQDGGSDIINYIVERRETSRLVWTLVD-ANVQTLSCKVTKLLEGNEYIFRIMAVN 23227
Cdd:cd00063       1 PSPPTNLR-VTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 23228 KYGVGEPLESEPLI 23241
Cdd:cd00063      79 GGGESPPSESVTVT 92
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
31769-32014 3.73e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 81.63  E-value: 3.73e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKgTDQVLVKKEISIL--------NIARHRNILYLHESFESMEELVMIF-EFI 31839
Cdd:cd06652      10 LGQGAFGRVYLCYDADTGRELAVKQVQFD-PESPETSKEVNALeceiqllkNLLHERIVQYYGCLRDPQERTLSIFmEYM 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK----PGDN 31915
Cdd:cd06652      89 PGGSIKDQLKSYG-ALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGN--VKLGDFGASKRLQticlSGTG 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENImnAEYTFDEEAFQEISLEAMDFID 31995
Cdd:cd06652     166 MKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKI--ATQPTNPQLPAHVSDHCRDFLK 243
                           250
                    ....*....|....*....
gi 1958765569 31996 RLLVkERKSRMTASEALKH 32014
Cdd:cd06652     244 RIFV-EAKLRPSADELLRH 261
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28368-28447 3.74e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.73  E-value: 3.74e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28368 DPPGTPDYIDVTRETITLKWNPPLRDGG-SKIVAYSIEKRQGSDRWVRCNfTDVSECQYTVSGLSPGDRYEFRIIARNAV 28446
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     .
gi 1958765569  28447 G 28447
Cdd:smart00060    81 G 81
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18491-18878 3.97e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.44  E-value: 3.97e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18491 YIISAKNSSGHAQGSAIVNVLDR---PGPCQNLKVSNVTKENCTISWEnplDNGGSEITNFIVEYRKPNQKGWSIVASDV 18567
Cdd:COG3401     207 YRVAATDTGGESAPSNEVSVTTPttpPSAPTGLTATADTPGSVTLSWD---PVTESDATGYRVYRSNSGDGPFTKVATVT 283
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18568 TKRLIKANLLANNEYYFRVCAENKVGVG----PTIETKTPILAinpidrPGEPENLHIADKGKTFVYLKWRRPDydgGSP 18643
Cdd:COG3401     284 TTSYTDTGLTNGTTYYYRVTAVDAAGNEsapsNVVSVTTDLTP------PAAPSGLTATAVGSSSITLSWTASS---DAD 354
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18644 NLSYHVERRLKGSADWERVHKgSIKETHYMVDKCVENQIYEFRVQTKNEGG-ESDWVRTEEVVVKEDLQKPVLDL-KLSG 18721
Cdd:COG3401     355 VTGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTAsVDAV 433
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18722 VLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATD--LTRSPRVKIDTSAE---SSKFSLTKAKRSDGGKYVVTATNPAGS 18796
Cdd:COG3401     434 PLTDVAGATAAASAASNPGVSAAVLADGGDTGNAvpFTTTSSTVTATTTDtttANLSVTTGSLVGGSGASSVTNSVSVIG 513
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18797 FVAYA-TVNVLDKPGPVRNLKIADVSSDRCTIRWDPPEDDGGCEIQNYILEKCESKRMVWSTYSANVLTPGATVTRLIEG 18875
Cdd:COG3401     514 ASAAAaVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVA 593

                    ...
gi 1958765569 18876 NEY 18878
Cdd:COG3401     594 GVH 596
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
21437-21837 3.97e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.44  E-value: 3.97e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21437 TYKVTGLTEGCEYFFRVMAENEYGIGEPTETTEPVRASEAPLPPDSLNIMDITKNTVSLAWPKPrhdGGSKITGYVIEAQ 21516
Cdd:COG3401     193 VDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPV---TESDATGYRVYRS 269
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21517 RKGSDQWTHISTVKGLECVVRNLTEGEEYTFQVMAVNSAG-RSAPREsrpvivkeqtmlpeldlrgiyqklviaragdni 21595
Cdd:COG3401     270 NSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSN--------------------------------- 316
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21596 kveipvlgrpkpTVTwkkgdqilkqtqrVNVENTAtstilninecvrsdsgaypltakntvgevgdvitiqvhdiPGPPT 21675
Cdd:COG3401     317 ------------VVS-------------VTTDLTP----------------------------------------PAAPS 331
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21676 GpIKFDEVSSDFVTFSWEPPEndgGVPISNYVVEMRQTDSTTWVELATTVIRTTYKATRLTTGVEYQFRVKAQNRYGVGp 21755
Cdd:COG3401     332 G-LTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE- 406
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21756 GITSASVVANYPFKVPGPPGTPQVTAVTKDSmTISWHEPLSDGGSPILGYHIERKERNGILWQTVSKALVPGNIFKSTGL 21835
Cdd:COG3401     407 SAPSEEVSATTASAASGESLTASVDAVPLTD-VAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTT 485

                    ..
gi 1958765569 21836 TD 21837
Cdd:COG3401     486 TA 487
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1417-1507 4.02e-15

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 75.91  E-value: 4.02e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:cd20990      81 GQNSFNLELVV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31235-31328 4.06e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.00  E-value: 4.06e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31235 PDKPTGpIVIEALLKNSVVISWKAPADDGGSwITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQN 31314
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 31315 TFGISEPLEVASVV 31328
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23835-23918 4.08e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.73  E-value: 4.08e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23835 PDPPKGpVKFDEVSAESITLSWNPPLYTGG-CQITNYIVQKRDTTTTvWDVVSATVARTTLKVTKLKTGTEYQFRIFAEN 23913
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  23914 RYGQS 23918
Cdd:smart00060    79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9296-9380 4.36e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 75.62  E-value: 4.36e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9296 PQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGEIESN 9375
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   9376 VNLQV 9380
Cdd:smart00410    81 TTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15290-15621 4.37e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.05  E-value: 4.37e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15290 QYMIKVENDHGVAKAPCTVSVLDT---PGPPINFVFEDIRKDSVLCKWEPPLDDGgseIINYTLEKKdkTKPDSEWIVIT 15366
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVTTPttpPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRS--NSGDGPFTKVA 280
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15367 STLRNcKYSVTKLIEGKEYLFRVRAENRFG-PGPPcvSKPLLAKDPFEPPDAPDKPIVDDVTSNSMVVKWNEPKDNGspI 15445
Cdd:COG3401     281 TVTTT-SYTDTGLTNGTTYYYRVTAVDAAGnESAP--SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--V 355
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15446 LGYWLEKREVNSTHWSRVNKaLLSSLKTKVDGLLEGLTYVFRVCAENAAGPGkfSPPSDPKTARDPISPPGPPVPRVADT 15525
Cdd:COG3401     356 TGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASGESLTASVDA 432
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15526 ------SSTTIELEWEPPAFNGGGEIMGYFVDKQLVGTNEWSRCTEKMVKVRQFTVKEIREGADYKLRVSAVNAAGEGPP 15599
Cdd:COG3401     433 vpltdvAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVI 512
                           330       340
                    ....*....|....*....|..
gi 1958765569 15600 GETEPVTVAEPQEPPTVELDVS 15621
Cdd:COG3401     513 GASAAAAVGGAPDGTPNVTGAS 534
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30545-30628 4.59e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.73  E-value: 4.59e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30545 PGKPQNPRVTDTTRTSVSLAWSVPEDEGG-SKVTGYLIEMQKVDqREWTKCNTTPTKiREYTLTHLPQGAEYRFRVLACN 30623
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSS-TSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  30624 AGGPG 30628
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
6824-6909 4.75e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 4.75e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6824 FVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAGRD 6903
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*.
gi 1958765569  6904 SCDALV 6909
Cdd:pfam07679    83 EASAEL 88
I-set pfam07679
Immunoglobulin I-set domain;
6166-6255 4.84e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 4.84e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6166 PSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTNDVG 6245
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  6246 SDSCTTMLLV 6255
Cdd:pfam07679    81 EAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
14498-14581 4.97e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.53  E-value: 4.97e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14498 PPGKPTVKDIGKTSLVLNWTKPEhDGGAKIESYVIEMLKTGT-DDWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKAG 14576
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....*
gi 1958765569 14577 ESEPS 14581
Cdd:pfam00041    81 EGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
19703-19797 5.08e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 75.61  E-value: 5.08e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19703 DPPGKPEVVDVTKNSASLIWARPKHDGGsKIIGYFVEACKLPGDKWVRCNTTPHQIPleEYTATGLEENAQYQFRAIAKT 19782
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSET--SYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1958765569 19783 AVNISQPSEPSDPVT 19797
Cdd:cd00063      79 GGGESPPSESVTVTT 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4591-4659 5.18e-15

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 75.06  E-value: 5.18e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4591 ARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCST 4659
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
14969-15236 5.19e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.05  E-value: 5.19e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14969 YTITLENKLGSATASINVKVIG---LPGPCKDIKASDITKSSCKLTWEPPEFDGgspILHYVLERREAGRRTYIPVmSGE 15045
Cdd:COG3401     207 YRVAATDTGGESAPSNEVSVTTpttPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKV-ATV 282
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15046 NKLSWTVKDLIPNGEYFFRVKAVNkiGGGEYIELKNPVIAQDPKQPPDPPVDVEVHNPTAKAMTITWKPPLydgGSKIMG 15125
Cdd:COG3401     283 TTTSYTDTGLTNGTTYYYRVTAVD--AAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTG 357
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15126 YIIEKLAKGEDRWKRCNEhLVPVLTYTAKGLEEGKEYQFRVRAENAAGIgEPSRATPPTKAVDPIDAPKVILRTSLEVKR 15205
Cdd:COG3401     358 YNVYRSTSGGGTYTKIAE-TVTTTSYTDTGLTPGTTYYYKVTAVDAAGN-ESAPSEEVSATTASAASGESLTASVDAVPL 435
                           250       260       270
                    ....*....|....*....|....*....|.
gi 1958765569 15206 GDEIALDATISGSPYPTITWIKDENVIVPEE 15236
Cdd:COG3401     436 TDVAGATAAASAASNPGVSAAVLADGGDTGN 466
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23643-23724 5.80e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 75.34  E-value: 5.80e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23643 PQPPGKITVDDVTRNSVSLSWTKPEHDGG-SKIIQYIVEMQAKNTDKWSECARVKSLEAVITSLTQGEEYLFRVIAVNEK 23721
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  23722 GRS 23724
Cdd:smart00060    81 GEG 83
I-set pfam07679
Immunoglobulin I-set domain;
8706-8790 5.82e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.37  E-value: 5.82e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8706 FVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKD 8785
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*
gi 1958765569  8786 SCSAQ 8790
Cdd:pfam07679    83 EASAE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
29452-29548 5.88e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 75.61  E-value: 5.88e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29452 DPPGRPEVTDVTRSTVSLVWSAPmYDGGSKVVGYIIERKpvsEVGDGRWLKCNYTIVSDNFFTVTALSEGDTYEFRVLAK 29531
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYR---EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|....*..
gi 1958765569 29532 NAAGiISKGSESTGPVT 29548
Cdd:cd00063      78 NGGG-ESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
13704-13789 5.93e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.14  E-value: 5.93e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13704 GPPLNVTITDVNRFGVSLTWEPPEyDGGAEITNYVIELRDKTSIRWDTAMTVRAEDLSATVTDVVEGQEYSFRVRAQNRI 13783
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 13784 GVGKPS 13789
Cdd:pfam00041    80 GEGPPS 85
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
31761-32017 6.14e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 81.77  E-value: 6.14e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQ---VLVKKEISILNIARHRNILYLHE----SFESMEEL- 31832
Cdd:cd07864       7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfpITAIREIKILRQLNHRSVVNLKEivtdKQDALDFKk 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31833 -----VMIFEFISGlDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQA 31907
Cdd:cd07864      87 dkgafYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ--IKLADFGLA 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 R-----QLKPGDN--FRLLFTAPEYYAPEvhqhDVVSSATDMWSLGTLVYVLLSGINPFLAetNQQMIE----------- 31969
Cdd:cd07864     164 RlynseESRPYTNkvITLWYRPPELLLGE----ERYGPAIDVWSCGCILGELFTKKPIFQA--NQELAQlelisrlcgsp 237
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31970 --------------NIMNAEYTFD---EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07864     238 cpavwpdviklpyfNTMKPKKQYRrrlREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14100-14182 6.71e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.96  E-value: 6.71e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14100 PDPPENVKWRDRTANSIFLTWDPPKNDGG-SRIKGYIVEKCPRGSDkWVACGEPVPDTKMEVTGLEEGKWYAYRVKALNR 14178
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  14179 QGAS 14182
Cdd:smart00060    80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
27792-27874 7.01e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.37  E-value: 7.01e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27792 SVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQpKSSTVS 27871
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE-AEASAE 87

                    ...
gi 1958765569 27872 VKV 27874
Cdd:pfam07679    88 LTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
18514-18604 7.21e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 75.23  E-value: 7.21e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18514 PGPCQNLKVSNVTKENCTISWENPLDNGGsEITNFIVEYRKPNQKGWSIVASDVTKR---LIKaNLLANNEYYFRVCAEN 18590
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSEtsyTLT-GLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 18591 KVGVGPTIETKTPI 18604
Cdd:cd00063      79 GGGESPPSESVTVT 92
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
31763-31962 7.33e-15

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 80.84  E-value: 7.33e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV------KGTDQVLvkKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd08228       4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIfemmdaKARQDCV--KEIDLLKQLNHPNVIKYLDSFIEDNELNIVL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFE---LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPG 31913
Cdd:cd08228      82 ELADAGDLSQMIKYFKKQkrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITA--TGVVKLGDLGLGRFFSSK 159
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DN-FRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE 31962
Cdd:cd08228     160 TTaAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26000-26082 7.40e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.96  E-value: 7.40e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26000 PGPPGPIRIDEVSCDNVSISWTPPEYDGG-CQISNYIVEKRETtSTTWQVVSQAVARTSIKIVRLTTGSEYQFRVCAENR 26078
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  26079 YGKS 26082
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29058-29139 7.55e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.96  E-value: 7.55e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29058 PAPPRRLDVVDTSKSSAVLAWLKPEHDGG-SRITSYLLEMRQKGSDFWVEAGHTKQLTFTVERLVENTEYEFRVKAKNDA 29136
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  29137 GYS 29139
Cdd:smart00060    81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27082-27165 7.70e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.96  E-value: 7.70e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27082 PGPPTGPVaISDITEESVTLKWEPPKYDGG-SHVTNYIVLKRETSTAvWTEVSATVARTMIKVMKLTTGEEYQFRIKAEN 27160
Cdd:smart00060     1 PSPPSNLR-VTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  27161 RFGIS 27165
Cdd:smart00060    79 GAGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
33901-33982 7.86e-15

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 74.93  E-value: 7.86e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33901 ISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQsqeQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDSATV 33980
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLK---ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATI 78

                    ..
gi 1958765569 33981 NI 33982
Cdd:cd05748      79 NV 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28169-28261 8.03e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 75.23  E-value: 8.03e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28169 PSKPKGpIRFDEIKADSAIMSWDIPEDDGGgEITCYSIEKREASQTNWKMVCSSVA-RTTFKVSNLVKDSEYQFRVRAEN 28247
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 28248 RYGVSEPLVSNVIV 28261
Cdd:cd00063      79 GGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25314-25397 8.16e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.96  E-value: 8.16e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25314 PGPPEGpLKVTGVTAEKCYLAWNPPLQDGGAS-ISHYIIEKRETSRlSWTQVSTEVQALNYKVTKLLPGNEYIFRVMAVN 25392
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  25393 KYGVG 25397
Cdd:smart00060    79 GAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
26580-27117 8.46e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 84.28  E-value: 8.46e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26580 PSDTSPLVRAEDPVFLPSPPSKPKIVDSGKTTITIGWVKPLFDGGAPITGYTVEYKKSEETDWKVAIQSFRGTEYTMSGL 26659
Cdd:COG3401     118 PSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGG 197
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26660 TT--GAEYVFRVRSLNKVGASDPSDItdpqvakereeepafdvdsemrktltvkagssftmtvpfrgrpipnVSWSKPDT 26737
Cdd:COG3401     198 DIepGTTYYYRVAATDTGGESAPSNE----------------------------------------------VSVTTPTT 231
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26738 dlrtrayidstdsrtsltienanrndsgkytltiqnvlsaasmtfvvkvldSPGPPANITVREVTKETAVLSWDVPENDG 26817
Cdd:COG3401     232 ---------------------------------------------------PPSAPTGLTATADTPGSVTLSWDPVTESD 260
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26818 gapVKNYHIEKREASKKAWVSVTNNcSRLSYKVTNLQEGAVYYFRVSGENEFGV-GVPAETKEGVKITEKPSPPEKLGVT 26896
Cdd:COG3401     261 ---ATGYRVYRSNSGDGPFTKVATV-TTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPSGLTAT 336
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26897 SVSKDSVSLSWlkpEHDGGSRILHYVVEALEKGQKNWVKCA-VVKTTHHVVSGLREGHEYFFRVFAENQAGL-SDPRELL 26974
Cdd:COG3401     337 AVGSSSITLSW---TASSDADVTGYNVYRSTSGGGTYTKIAeTVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEV 413
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26975 ----LPVLIKDHLEPPEIDMKNFPSHTVYVRAGSNlkVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKE 27050
Cdd:COG3401     414 sattASAASGESLTASVDAVPLTDVAGATAAASAA--SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSV 491
                           490       500       510       520       530       540       550
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27051 SVTADAGKYEITAANSSGTTKTFINIIVLDRPGPPTGPVA---ISDITEESVTLKWEPPKYDGGSHVTNY 27117
Cdd:COG3401     492 TTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTgasPVTVGASTGDVLITDLVSLTTSASSSV 561
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
15919-16006 9.37e-15

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 74.55  E-value: 9.37e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15919 TIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIeKPTDALNITKEEVSrseakTELSIPKAVREDKGTYTITASNRLGSV 15998
Cdd:cd05748       1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPL-KETGRVQIETTASS-----TSLVIKNAKRSDSGKYTLTLKNSAGEK 74

                    ....*...
gi 1958765569 15999 FRNVHVEV 16006
Cdd:cd05748      75 SATINVKV 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16524-16612 9.44e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 9.44e-15
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16524 PDLPIKLKIGLITKNTVHLSWKPPKNDGG-SPVTHYIVEclawdpTGKKKEAWRQCNRrDVEELEFTVEDLVEGGEYEFR 16602
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVE------YREEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFR 73
                             90
                     ....*....|
gi 1958765569  16603 VKAVNEAGVS 16612
Cdd:smart00060    74 VRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30850-30925 9.44e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 9.44e-15
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  30850 VLDVTKSSVSLSWSRPKDDGGSRVTGYYIERKETSTDKWVRHNKTQITTTmYTVTGLVPDAEYQFRIIAQNDVGLS 30925
Cdd:smart00060     9 VTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTS-YTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26495-26578 1.00e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 1.00e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26495 PSPPTSLEITSVTKDSMTLCWSRPETDGG-SDISGYIIERREKNSlRWMRVNKKPVyDLRVKSTGLREGCEYEYRVFAEN 26573
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPS-STSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  26574 AAGLS 26578
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21671-21754 1.01e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 1.01e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21671 PGPPTGpIKFDEVSSDFVTFSWEPPENDGGV-PISNYVVEMRQTDSTtWVELATTVIRTTYKATRLTTGVEYQFRVKAQN 21749
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  21750 RYGVG 21754
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
17626-17712 1.04e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 74.76  E-value: 1.04e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17626 SPPINPEAIDTTCNSVDLTWQPPRhDGGSKILGYIVEYQKVGDEEWrrANHTPESCPETKYKVTGLRDGQTYKFRVLAVN 17705
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEP--WNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 17706 EAGESDP 17712
Cdd:pfam00041    78 GGGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
3577-3667 1.04e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 1.04e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIiHNPDGSGTFIVNDPQRGDSGLYICKAENLW 3656
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV-TYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  3657 GTSTCTAELLV 3667
Cdd:pfam07679    80 GEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6268-6349 1.07e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 74.46  E-value: 1.07e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6268 SKIVKAGDSARLECKITGSPEIRVVWYRNEHE-LTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTK 6346
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   6347 VIV 6349
Cdd:smart00410    83 LTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22268-22352 1.11e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 1.11e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22268 PGPPGNPRVLDTSRSSISIAWNKPIYDGG-SEITGYMVEIAlPEEDEWQVVTPPAglKATSYTITNLIENQEYKIRIYAM 22346
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYR-EEGSEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  22347 NSEGLG 22352
Cdd:smart00060    78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19901-19983 1.15e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 1.15e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19901 PGPPASVKINKMYADRAMLSWEPPLEDGG-SEITNYIVDKRETSrPNWAQVSATVPITSCTVEKLIEGHEYQFRICAENK 19979
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  19980 YGVG 19983
Cdd:smart00060    80 AGEG 83
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
31761-32026 1.15e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 80.82  E-value: 1.15e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV--LVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd07873       2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEY 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGlDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK-PGDNFR 31917
Cdd:cd07873      82 LDK-DLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE--LKLADFGLARAKSiPTKTYS 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDV-VSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEI---------- 31986
Cdd:cd07873     159 NEVVTLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGIlsneefksyn 238
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31987 ----------------SLEAMDFIDRLLVKERKSRMTASEALKHPWLKQRMDRVST 32026
Cdd:cd07873     239 ypkyradalhnhaprlDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHSLGERIHK 294
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
900-989 1.15e-14

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 74.84  E-value: 1.15e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQI-ESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVrPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd05744      81 GENSFNAELVV 91
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
31761-32019 1.15e-14

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 81.60  E-value: 1.15e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGT--DQVLVkkEISILNIARHR------NILYLHESFESMEEL 31832
Cdd:cd14226      13 DRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAflNQAQI--EVRLLELMNKHdtenkyYIVRLKRHFMFRNHL 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31833 VMIFEFIS-GL-DIFERINTSAFELNEreVVSYVRQVCEALEFLHSQ--NIGHFDIRPENIIYQTRKNSIIKIIEFGQAR 31908
Cdd:cd14226      91 CLVFELLSyNLyDLLRNTNFRGVSLNL--TRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCNPKRSAIKIIDFGSSC 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31909 QLkpgdNFRLL-FTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGiNPFLAETNQQ----------------MIEN 31970
Cdd:cd14226     169 QL----GQRIYqYIQSRFYrSPEVLLGLPYDLAIDMWSLGCILVEMHTG-EPLFSGANEVdqmnkivevlgmppvhMLDQ 243
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31971 IMNAEYTFD-----------------EEAFQEISLEAM---------------------------DFIDRLLVKERKSRM 32006
Cdd:cd14226     244 APKARKFFEklpdgtyylkktkdgkkYKPPGSRKLHEIlgvetggpggrragepghtvedylkfkDLILRMLDYDPKTRI 323
                           330
                    ....*....|...
gi 1958765569 32007 TASEALKHPWLKQ 32019
Cdd:cd14226     324 TPAEALQHSFFKR 336
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17229-17312 1.22e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.19  E-value: 1.22e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17229 PERPEDLEVKEVTKNTVTLTWNPPKYDGG-SEIINYVLESRLIGTEkfHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVN 17307
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE--WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  17308 IVGQG 17312
Cdd:smart00060    79 GAGEG 83
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
31757-32037 1.28e-14

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 80.12  E-value: 1.28e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYmiaEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd06641       3 EELFTKL---EKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIedIQQEITVLSQCDSPYVTKYYGSYLKDTKLWI 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISG---LDIFErintsAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLK 31911
Cdd:cd06641      80 IMEYLGGgsaLDLLE-----PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLS--EHGEVKLADFGVAGQLT 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFRLLFTA-PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFqeiSLEA 31990
Cdd:cd06641     153 DTQIKRN*FVGtPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNY---SKPL 229
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWLKQRMDRVSTKVIRTLRHRRY 32037
Cdd:cd06641     230 KEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRW 276
I-set pfam07679
Immunoglobulin I-set domain;
4667-4753 1.35e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 1.35e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4667 PSFIKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEVG 4746
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                    ....*..
gi 1958765569  4747 KCGCVAT 4753
Cdd:pfam07679    81 EAEASAE 87
I-set pfam07679
Immunoglobulin I-set domain;
24147-24227 1.36e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 1.36e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24147 IVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNVK 24226
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 24227 V 24227
Cdd:pfam07679    90 V 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6541-6616 1.43e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 74.14  E-value: 1.43e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6541 VIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQN 6616
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
30050-30141 1.50e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.46  E-value: 1.50e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30050 PGPCPSVNVKEVSRDSVTITWEIPTIDGGaPVNNYIIEKREAAMRAFKTVTTKCSKTL-YRISGLVEGTMYYFRVLPENI 30128
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETsYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|...
gi 1958765569 30129 YGIGEPCETSDAV 30141
Cdd:cd00063      80 GGESPPSESVTVT 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
28085-28152 1.51e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 74.16  E-value: 1.51e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 28085 ISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDN 28152
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKN 69
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
31769-31959 1.62e-14

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 80.61  E-value: 1.62e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVEtssKKTFMAKFVKVKGTDQVL-----VKKEISILNIARHRNILYLhesFESMEEL-----VMIFEF 31838
Cdd:cd13988       1 LGQGATANVFRGRH---KKTGDLYAVKVFNNLSFMrpldvQMREFEVLKKLNHKNIVKL---FAIEEELttrhkVLVMEL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERIN--TSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKN--SIIKIIEFGQARQLKPGD 31914
Cdd:cd13988      75 CPCGSLYTVLEepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDgqSVYKLTDFGAARELEDDE 154
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31915 NFRLLFTAPEYYAPEVHQHDVV--------SSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd13988     155 QFVSLYGTEEYLHPDMYERAVLrkdhqkkyGATVDLWSIGVTFYHAATGSLPF 207
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20396-20476 1.71e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 1.71e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20396 PGPVVDLKVLAVTKSSCTIGWKKPRSDGG-SRITGYVVDFLTEENKWQRVMKSLS-LQYSTKDLKEGKEYTFRVSAENEN 20473
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSsTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  20474 GEG 20476
Cdd:smart00060    81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22067-22150 1.76e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 1.76e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22067 PGPPEGpLAVSDVTSEKCVLSWLPPLDDGGAK-IDHYIVQKRETSRlAWTNVATEVQVTKLKVTKLLKGNEYIFRVMAVN 22145
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  22146 KYGVG 22150
Cdd:smart00060    79 GAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7855-7932 1.94e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 73.75  E-value: 1.94e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7855 PPYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAEN 7932
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21771-21854 1.94e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 1.94e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21771 PGPPGTPQVTAVTKDSMTISWHEPLSDGG-SPILGYHIERKERNGiLWQTVSKAlVPGNIFKSTGLTDGIAYEFRVIAEN 21849
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  21850 MAGKS 21854
Cdd:smart00060    79 GAGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
17340-17420 1.95e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 73.78  E-value: 1.95e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17340 LTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFCQVN 17419
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 17420 V 17420
Cdd:cd05748      82 V 82
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
31757-32037 1.96e-14

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 79.72  E-value: 1.96e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYmiaEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd06642       3 EELFTKL---ERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIedIQQEITVLSQCDSPYITRYYGSYLKGTKLWI 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGD 31914
Cdd:cd06642      80 IMEYLGGGSALDLLKPGPLE--ETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD--VKLADFGVAGQLTDTQ 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTA-PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENI-MNAEYTFDEEAFQEISleamD 31992
Cdd:cd06642     156 IKRNTFVGtPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIpKNSPPTLEGQHSKPFK----E 231
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWLKQRMDRVSTKVIRTLRHRRY 32037
Cdd:cd06642     232 FVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRYKRW 276
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
31767-31962 2.00e-14

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 79.35  E-value: 2.00e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHR---CVETSSKKTfMAKFVKVKGTDQVLvKKEISILNIaRHRNILYL--HESFESMEEL-VMIFEFIS 31840
Cdd:cd13979       9 EPLGSGGFGSVYKatyKGETVAVKI-VRRRRKNRASRQSF-WAELNAARL-RHENIVRVlaAETGTDFASLgLIIMEYCG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRL-- 31918
Cdd:cd13979      86 NGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILIS--EQGVCKLCDFGCSVKLGEGNEVGTpr 163
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569 31919 --LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE 31962
Cdd:cd13979     164 shIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGL 209
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15415-15497 2.04e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 2.04e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15415 PDAPDKPIVDDVTSNSMVVKWNEPKDNG--SPILGYWLEKREVNSThWSRVNKAlLSSLKTKVDGLLEGLTYVFRVCAEN 15492
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGSE-WKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  15493 AAGPG 15497
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20985-21067 2.10e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 2.10e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20985 PGPPGPIEISNVSAEKATLTWTPPLEDGG-SPIKAYVLEKRETSRLlWTVVSEDIQACRHVVTKLIQGNEYLFRVSAVNH 21063
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  21064 YGKG 21067
Cdd:smart00060    80 AGEG 83
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
31757-32037 2.10e-14

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 79.71  E-value: 2.10e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYmiaEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd06640       3 EELFTKL---ERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIedIQQEITVLSQCDSPYVTKYYGSYLKGTKLWI 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGD 31914
Cdd:cd06640      80 IMEYLGGGSALDLLRAGPFD--EFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGD--VKLADFGVAGQLTDTQ 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTA-PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPflaETNQQMIENIMNAEYTFDEEAFQEISLEAMDF 31993
Cdd:cd06640     156 IKRNTFVGtPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP---NSDMHPMRVLFLIPKNNPPTLVGDFSKPFKEF 232
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 31994 IDRLLVKERKSRMTASEALKHPWLKQRMDRVSTKVIRTLRHRRY 32037
Cdd:cd06640     233 IDACLNKDPSFRPTAKELLKHKFIVKNAKKTSYLTELIDRFKRW 276
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30943-31026 2.27e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.27e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30943 PSQPGELEILSISKDSVILQWEKPECDGG-KEILGYWVEYRQSGDSaWKKSNKERiKDRQFTIGGLLEATEYEFRVFAEN 31021
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  31022 ETGLS 31026
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
27282-27361 2.39e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.60  E-value: 2.39e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27282 PPRNVRITDISKNSVNLSWQqPAFDGGSKITGYIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAVG 27361
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21091-21167 2.41e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.41e-14
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  21091 EISNVTKNTATVSWKRPIDDGG-SEITGYHVERREKKGlRWVRATKTPvSDLRCKVTGLQEGNTYEFRVSAENRAGIG 21167
Cdd:smart00060     8 RVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30444-30527 2.41e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.41e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30444 PGPPETLQIFDISRDGMTLTWYPPEDDGG-SQVTGYIIERKEVRaDRWVRVNkVPVTMTRYRSTGLIEGLEYEHRVTAIN 30522
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  30523 ARGTG 30527
Cdd:smart00060    79 GAGEG 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4387-4474 2.42e-14

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 73.99  E-value: 2.42e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPS---PDCRITDADNKHSLELSNLTVQDRGVYSCKASN 4463
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSsipGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|.
gi 1958765569  4464 KFGADICQAEL 4474
Cdd:cd20951      81 IHGEASSSASV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30344-30427 2.45e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.45e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30344 PGPPIGpIKIDEVDATSVTISWEPPELDGG-APLSGYVVEQRDAHrPGWLPVSESVTRPTFKFTRLTEGNEYVFRVAATN 30422
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  30423 RFGIG 30427
Cdd:smart00060    79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33704-33787 2.47e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 73.69  E-value: 2.47e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33704 PRSQNINEGQNVLFSCEISGEPSPEIEWFKNNL-PISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQCSAT 33782
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  33783 ASLTV 33787
Cdd:smart00410    81 TTLTV 85
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
31758-32022 2.61e-14

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 80.42  E-value: 2.61e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEKYMIAEDLGRGEFGIV--HRCVETSSK---KTFMAKF---VKVKGTdqvlvKKEISILNIARHRNILYL------H 31823
Cdd:cd07851      12 EVPDRYQNLSPVGSGAYGQVcsAFDTKTGRKvaiKKLSRPFqsaIHAKRT-----YRELRLLKHMKHENVIGLldvftpA 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31824 ESFESMEELVMIFEFIsGLDIFERINTSAfeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIiyQTRKNSIIKIIE 31903
Cdd:cd07851      87 SSLEDFQDVYLVTHLM-GADLNNIVKCQK--LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNL--AVNEDCELKILD 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31904 FGQARQLkpgDNFRLLFTAPEYY-APEV-----HQHDVVssatDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYT 31977
Cdd:cd07851     162 FGLARHT---DDEMTGYVATRWYrAPEImlnwmHYNQTV----DIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGT 234
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31978 FDEEAFQEISLE---------------------------AMDFIDRLLVKERKSRMTASEALKHPWLKQRMD 32022
Cdd:cd07851     235 PDEELLKKISSEsarnyiqslpqmpkkdfkevfsganplAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHD 306
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29653-29735 2.68e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.68e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29653 PGPCGKLTVSRVTEEKCTLAWSLPQEDGG-AEITHYIVERRETSRlNWVIVEAECLTLSYVVTRLIKNNEYTFRVRAVNK 29731
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  29732 YGLG 29735
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21477-21558 2.71e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.71e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21477 PLPPDSLNIMDITKNTVSLAWPKPRHDGG-SKITGYVIEAQRKGSDQWTHISTVKGLECVVRNLTEGEEYTFQVMAVNSA 21555
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  21556 GRS 21558
Cdd:smart00060    81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18116-18199 2.76e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 2.76e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18116 PGPPTGpINILDVTPEYMTISWQPPKDDGG-SPVINYIVEKQDTrKGTWGVVSAGSSKLKLKVPHLQKGCEYVFRVKAEN 18194
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  18195 KMGVG 18199
Cdd:smart00060    79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
26395-26487 2.85e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 73.68  E-value: 2.85e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26395 PGPPAGpLEINGLTAEKCSLSWGRPQEDGGaDIDYYIVEKRETSRLAWTICEAEL-RTTSCKVTKLLKGNEYIFRVTGVN 26473
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 26474 KYGVGEPLESVAVK 26487
Cdd:cd00063      79 GGGESPPSESVTVT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8997-9078 2.86e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 73.31  E-value: 2.86e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8997 PVDAVVGESADLECHVTGTQPIKVTWAKDNRE-IRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQ 9075
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   9076 LNI 9078
Cdd:smart00410    83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
16830-16919 2.96e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 2.96e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16830 GAPDKPTVSSVTRNSMTVNWEEPEyDGGSPVTGY---WLEMKDTTSKRWKRVNRDPIkamtlgvSYKVTGLIEGSDYQFR 16906
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYeveYRPKNSGEPWNEITVPGTTT-------SVTLTGLKPGTEYEVR 72
                            90
                    ....*....|...
gi 1958765569 16907 VYAINAAGVGPAS 16919
Cdd:pfam00041    73 VQAVNGGGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
19155-19731 2.99e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 82.36  E-value: 2.99e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19155 VGIDNVVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVKVLDTPGPVSDLKVSDVTkTSCHVSWAPP 19234
Cdd:COG3401      69 TGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAAT-AGTYALGAGL 147
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19235 ENDGGSPVTHY---IVEKREAERKTWSTVTPEVKKTSFNVT---------NLVPGNEYFFRVTAVNEYGPGVPTDVpkpV 19302
Cdd:COG3401     148 YGVDGANASGTtasSVAGAGVVVSPDTSATAAVATTSLTVTsttlvdgggDIEPGTTYYYRVAATDTGGESAPSNE---V 224
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19303 LASDPLSEPDPPRKVEVTEMTKNSATLAWLPPLRDGgakIDGYIIsYREEDqPADRWTEYSVVKDLSLIITGLKEGKKYK 19382
Cdd:COG3401     225 SVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRV-YRSNS-GDGPFTKVATVTTTSYTDTGLTNGTTYY 299
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19383 FRVAARNAVGvsmpreaegvyeakeqllppkilmpeqitikagkklrveahvygkpnpickwkkgeddvvtsshlaIHKA 19462
Cdd:COG3401     300 YRVTAVDAAG------------------------------------------------------------------NESA 313
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19463 DSSSVLIIKDVTrkdsgyysltaenssgtdtqkikvtvmdAPGPPQPpFDISEIDADACSLSWHiplEDGGSNITNYIVE 19542
Cdd:COG3401     314 PSNVVSVTTDLT----------------------------PPAAPSG-LTATAVGSSSITLSWT---ASSDADVTGYNVY 361
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19543 KCDVSRGDWVTALASVTKTSCRVGKLIPGQEYIFRVRAENRFGISEPLTSPKMLAKFPfdVPSEPKNARVTKVNKDCIFV 19622
Cdd:COG3401     362 RSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTAS--AASGESLTASVDAVPLTDVA 439
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19623 AWDRPDSDGGSPITGYLIERKERNSllwvKANDTIVRSTEYPCAGLVEGLEYSFRIYALNKAGSSPPSKPTEYVTARMPV 19702
Cdd:COG3401     440 GATAAASAASNPGVSAAVLADGGDT----GNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGAS 515
                           570       580
                    ....*....|....*....|....*....
gi 1958765569 19703 DPPGKPEVVDVTKNSASLIWARPKHDGGS 19731
Cdd:COG3401     516 AAAAVGGAPDGTPNVTGASPVTVGASTGD 544
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23249-23332 3.10e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 3.10e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23249 PDAPKAPEVTAVTKDSMIVVWERPASDGG-SEILGYVLEKRDKEGiRWTRCHKRlIGELRLRVTGLLENHNYEFRVSAEN 23327
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  23328 AAGLS 23332
Cdd:smart00060    79 GAGEG 83
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
31759-32017 3.22e-14

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 80.05  E-value: 3.22e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMA-KFVKVKGTDQVLVKKEISILNIARHRN------ILYLHESFESMEE 31831
Cdd:cd14214      11 LQERYEIVGDLGEGTFGKVVECLDHARGKSQVAlKIIRNVGKYREAARLEINVLKKIKEKDkenkflCVLMSDWFNFHGH 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFIsGLDIFERINTSAFE---LNEREVVSYvrQVCEALEFLHSQNIGHFDIRPENIIY----------------- 31891
Cdd:cd14214      91 MCIAFELL-GKNTFEFLKENNFQpypLPHIRHMAY--QLCHALKFLHENQLTHTDLKPENILFvnsefdtlyneskscee 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31892 QTRKNSIIKIIEFGQARqlKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ---MI 31968
Cdd:cd14214     168 KSVKNTSIRVADFGSAT--FDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREhlvMM 245
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31969 ENIM------------------NAEYTFDEEA----------------FQEISLE---AMDFIDRLLVKERKSRMTASEA 32011
Cdd:cd14214     246 EKILgpipshmihrtrkqkyfyKGSLVWDENSsdgryvsenckplmsyMLGDSLEhtqLFDLLRRMLEFDPALRITLKEA 325

                    ....*.
gi 1958765569 32012 LKHPWL 32017
Cdd:cd14214     326 LLHPFF 331
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
16940-17025 3.33e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 73.30  E-value: 3.33e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16940 KVTDWTKSSVDLEWSPPlKDGGSKITGYIVEYKEEGKEEWEKGKDKEVRGTKLVVTGLKEGAFYKFRVRAVNIAGVGEPG 17019
Cdd:cd00063       8 RVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86

                    ....*.
gi 1958765569 17020 EVTDII 17025
Cdd:cd00063      87 ESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
19998-20086 3.36e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 3.36e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19998 DPPGRcdpPVISNITKDHMTVSWKAPaDDGGSPITGYLVEKRETQAVNWTKVNRKPVIERTLKATGLQEGTEYEFRVTAI 20077
Cdd:pfam00041     1 SAPSN---LTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 20078 NKAGPGKPS 20086
Cdd:pfam00041    77 NGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22753-22836 3.38e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 3.38e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22753 PGPPTGpVKMDEVTADSVTLSWEPPKYDGGSS-INNYIVEKRDTSTTaWQIVSATVARTTIKASRLKTGCEYQFRIAAEN 22831
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  22832 RYGKS 22836
Cdd:smart00060    79 GAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
20271-20814 3.46e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 82.36  E-value: 3.46e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20271 YDAGKYILTLENSCGKKEYTIVVKVLDTPGPPVNVTVKEISKDSAYITWDPPIIDGGSPIINYVVEKRDAERKSWSTVTT 20350
Cdd:COG3401      99 GSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATA 178
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20351 ECPKTSFRVS---------NLEEGKSYFFRVFAENEYGIGDPGETRDAVKASETPGPVVDLKVLAVTKSSCTIGWkkpRS 20421
Cdd:COG3401     179 AVATTSLTVTsttlvdgggDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW---DP 255
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20422 DGGSRITGYVVD-FLTEENKWQRVMKSLSLQYSTKDLKEGKEYTFRVSAENENG-EGTPSEIMVVAKDdvvapdldlkdl 20499
Cdd:COG3401     256 VTESDATGYRVYrSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTD------------ 323
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20500 pdlcylakensnfrlkipiKGKPAPsvswkkgedPLatdtrvsvestavnttlvvydcqksdagkytitlkNVAGTKEGT 20579
Cdd:COG3401     324 -------------------LTPPAA---------PS-----------------------------------GLTATAVGS 340
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20580 LSIkvvgkpgiptgpikfdevtaeamTLKWGPPKDDGgseITNYVLEKRDSVNNKWVTCASAVQKTTFRVTRLHEGIEYT 20659
Cdd:COG3401     341 SSI-----------------------TLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20660 FRVSAENKYGVgEGLKSEPIVAkHPFDVPDAPPPPNIVDVRHDSVSLTWTDPKKTGGSPITGYHIEFKERNSLLWKRANK 20739
Cdd:COG3401     395 YKVTAVDAAGN-ESAPSEEVSA-TTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTT 472
                           490       500       510       520       530       540       550
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 20740 TPIrmkdFKVTGLTEGLEYEFRVMAINLAGVGKPSLPSEPVVALDPIDPPGKPEVISVTRNSVTLIWTEPKYDGG 20814
Cdd:COG3401     473 TSS----TVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTG 543
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
31053-31132 3.61e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.92  E-value: 3.61e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31053 DVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELV-QSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSK 31131
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     .
gi 1958765569  31132 L 31132
Cdd:smart00410    83 L 83
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
31754-32017 3.63e-14

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 80.83  E-value: 3.63e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31754 SKTKELY---EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK----VKGTDQVLVKKEISILNIARHRNILYLHESF 31826
Cdd:cd05623      62 SKVKQMRlhkEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNkwemLKRAETACFREERDVLVNGDSQWITTLHYAF 141
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31827 ESMEELVMIFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQ 31906
Cdd:cd05623     142 QDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDM--NGHIRLADFGS 219
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARQLKPGDNFR--LLFTAPEYYAPEVHQ-----HDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFD 31979
Cdd:cd05623     220 CLKLMEDGTVQssVAVGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQ 299
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 1958765569 31980 -EEAFQEISLEAMDFIDRLLV-KERKSRMTASEALK-HPWL 32017
Cdd:cd05623     300 fPTQVTDVSENAKDLIRRLICsREHRLGQNGIEDFKnHPFF 340
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25116-25195 3.66e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 3.66e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25116 DPPGRPEAIIITRNSVTLKWKKPTYDGG-SKITGYIVEKKDlPDGRWMKASfTNVVETEFTVTGLVEDQRYEFRVIARNA 25194
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     .
gi 1958765569  25195 A 25195
Cdd:smart00060    80 A 80
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
31855-32014 3.92e-14

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 78.99  E-value: 3.92e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31855 LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIkIIEFGQARQL-KPGDNFRLLFTAPEYYAPevhqh 31933
Cdd:cd13974     129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRKIT-ITNFCLGKHLvSEDDLLKDQRGSPAYISP----- 202
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31934 DVVS------SATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfqEISLEAMDFIDRLLVKERKSRMT 32007
Cdd:cd13974     203 DVLSgkpylgKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDG--RVSENTVCLIRKLLVLNPQKRLT 280

                    ....*..
gi 1958765569 32008 ASEALKH 32014
Cdd:cd13974     281 ASEVLDS 287
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27811-28075 3.97e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 81.97  E-value: 3.97e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27811 PPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKY---ILTIENGVGQPKSSTVSVKVLDT-PAACQKLQV 27886
Cdd:COG3401     162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYyyrVAATDTGGESAPSNEVSVTTPTTpPSAPTGLTA 241
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27887 KHVSLGTVTLLWDPPlidGGSPIINYVIEKRDATKRTWSIVShKCSGTSFKVMDLSEKTPFFFRVLAENEIGI-GEPCET 27965
Cdd:COG3401     242 TADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVA-TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNV 317
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27966 TEPVKAAEVPAPIRDLSMKDSTKTSVVLSWTKPDfdgGSIITDYLVERKGKGEQAWSH-AGISKTCEIEIGQLKEQSVLE 28044
Cdd:COG3401     318 VSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKiAETVTTTSYTDTGLTPGTTYY 394
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1958765569 28045 FRVSARNEKG----QSDPVTIGPLTVKELVITPEV 28075
Cdd:COG3401     395 YKVTAVDAAGnesaPSEEVSATTASAASGESLTAS 429
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22952-23032 3.99e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 3.99e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22952 DPPGRPEAIIVTRNSVTLQWKKPTYDGG-SKITGYVVEKKElPDGRWMKASFTNiIDTQFEVTGLIEDHRYEFRVIARNA 23030
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ..
gi 1958765569  23031 AG 23032
Cdd:smart00060    80 AG 81
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
31769-32034 4.04e-14

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 79.67  E-value: 4.04e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK---VKGTDQVL-VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05598       9 IGVGAFGEVSLVRKKDTNALYAMKTLRkkdVLKRNQVAhVKAERDILAEADNEWVVKLYYSFQDKENLYFVMDYIPGGDL 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FER-INTSAFElnerEVVS--YVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGqarqLKPGdnFRL--- 31918
Cdd:cd05598      89 MSLlIKKGIFE----EDLArfYIAELVCAIESVHKMGFIHRDIKPDNILID--RDGHIKLTDFG----LCTG--FRWthd 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 --------LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEA 31990
Cdd:cd05598     157 skyylahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPHEANLSPEA 236
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31991 MDFIDRLL--VKERKSRMTASEALKHPWLK----QRMDRVSTKVIRTLRH 32034
Cdd:cd05598     237 KDLILRLCcdAEDRLGRNGADEIKAHPFFAgidwEKLRKQKAPYIPTIRH 286
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
31769-32019 4.11e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 78.54  E-value: 4.11e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVkGTDQVLVKKEISILNIARHRNILYL---HESFESMEELVMIFEFISG--LD 31843
Cdd:cd06605       9 LGEGNGGVVSKVRHRPSGQIMAVKVIRL-EIDEALQKQILRELDVLHKCNSPYIvgfYGAFYSEGDISICMEYMDGgsLD 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERintSAFELNEREVVSYVRQVCEALEFLHSQ-NIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKpgDNFRLLFTA 31922
Cdd:cd06605      88 KILK---EVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQ--VKLCDFGVSGQLV--DSLAKTFVG 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQ----EISLEAMDFIDRL 31997
Cdd:cd06605     161 TRSYmAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIFELLSYIVDEPPPLlpsgKFSPDFQDFVSQC 240
                           250       260
                    ....*....|....*....|..
gi 1958765569 31998 LVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd06605     241 LQKDPTERPSYKELMEHPFIKR 262
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
31763-32017 4.14e-14

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 77.98  E-value: 4.14e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14164       2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVdRRRASPDFVQKflpRELSILRRVNHPNIVQMFECIEVANGRLYIVME 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTsafelNEREVVSYVR----QVCEALEFLHSQNIGHFDIRPENIIYqTRKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd14164      82 AAATDLLQKIQE-----VHHIPKDLARdmfaQMVGAVNYLHDMNIVHRDLKCENILL-SADDRKIKIADFGFARFVEDYP 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPE-YYAPEV---HQHDvvSSATDMWSLGTLVYVLLSGINPFlAETNQQMIEnimNAEYTFDEEAFQEISLEA 31990
Cdd:cd14164     156 ELSTTFCGSRaYTPPEVilgTPYD--PKKYDVWSLGVVLYVMVTGTMPF-DETNVRRLR---LQQRGVLYPSGVALEEPC 229
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31991 MDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14164     230 RALIRTLLQFNPSTRPSIQQVAGNSWL 256
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
3198-3288 4.20e-14

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 73.00  E-value: 4.20e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3198 PPQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDY 3277
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  3278 GVATTSASLSV 3288
Cdd:cd20972      81 GSDTTSAEIFV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28961-29043 4.28e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 4.28e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28961 PGPPGPITFKDVTRGSATLMWDAPLLDGG-ARIHHYVIEKREASRRsWQVVSEKCTRQILKVSDLTEGVPYYFRVSAENE 29039
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  29040 YGVG 29043
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17922-18003 4.28e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 4.28e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17922 PGPPKDLHHVDVDKTEVSLVWNKPDRDGG-SPITGYLVEYQEEGAKDWIKFKTVKNLECVVTGLQQGKTYRFRVKAENII 18000
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  18001 GLG 18003
Cdd:smart00060    81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24917-25000 4.45e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 4.45e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24917 PGPPVGpVKFDEVSADFVVISWEPPAYTGG-CQISNYIVEKRDTTTtNWQMVSATVARTTIKVSKLKTGTEYQFRIFAEN 24995
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  24996 RYGKS 25000
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
9085-9175 4.46e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 73.06  E-value: 4.46e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLSeTIEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATNDA 9164
Cdd:pfam07679     1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  9165 GSALCTSSIVI 9175
Cdd:pfam07679    80 GEAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
26597-26681 4.63e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.83  E-value: 4.63e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26597 SPPSKPKIVDSGKTTITIGWvKPLFDGGAPITGYTVEYKKSEETDWKVAIQSFRGT-EYTMSGLTTGAEYVFRVRSLNKV 26675
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 26676 GASDPS 26681
Cdd:pfam00041    80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28269-28352 5.15e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 5.15e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28269 PGPPGKPVIYNVTSDGMSLTWDAPVYDGG-SEVTGFHVEKKERNSiLWQRVNTSPiSGREYRATGLIEGLDYQFRVYAEN 28347
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  28348 SAGLS 28352
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
18713-18805 5.16e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.68  E-value: 5.16e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18713 PVLDLKLSGVlTVKAGDTIRLEAGVRGKPFPEVAWTKDKdaTDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATN 18792
Cdd:pfam07679     1 PKFTQKPKDV-EVQEGESARFTCTVTGTPDPEVSWFKDG--QPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 18793 PAGSFVAYATVNV 18805
Cdd:pfam07679    78 SAGEAEASAELTV 90
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
31763-32035 5.17e-14

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 78.61  E-value: 5.17e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILN-IARHRNILYLHESFESM------EELVMI 31835
Cdd:cd06637       8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKkYSHHRNIATYYGAFIKKnppgmdDQLWLV 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERI-NTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd06637      88 MEFCGAGSVTDLIkNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDRTV 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPEYY-APEVHQHDVVSSAT-----DMWSLGTLVYVLLSGINPFLaeTNQQMIENIMNAEYTFDEEAFQEISL 31988
Cdd:cd06637     166 GRRNTFIGTPYWmAPEVIACDENPDATydfksDLWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNPAPRLKSKKWSK 243
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31989 EAMDFIDRLLVKERKSRMTASEALKHPWLK----QRMDRVSTK--VIRTLRHR 32035
Cdd:cd06637     244 KFQSFIESCLVKNHSQRPSTEQLMKHPFIRdqpnERQVRIQLKdhIDRTKKKR 296
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25515-25599 5.20e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 5.20e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25515 PGPPSNPKVTDTSRSSVSLAWNKPIYDGG-APVRGYVIELKEaAADEWTTCTPPSglQGKQFTVTKLKENTEYNFRICAF 25593
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  25594 NTEGVG 25599
Cdd:smart00060    78 NGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
8141-8218 5.21e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.68  E-value: 5.21e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8141 PRFIKKLdQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:pfam07679     1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29253-29336 5.35e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 5.35e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29253 PGPVTGpIEVSSVSAESCVLSWSEPKDDGGT-EITNYIVEKRESGTTaWQLINSSVKRTQIKVTHLTKYKEYCFRVSSEN 29331
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  29332 RFGVS 29336
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24231-24314 5.35e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 5.35e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24231 PGPPEGpVQVTGVTSEKCTLAWSPPLQDGG-SDISHYVVEKRETSRlAWTVVASEVVTNSLKVTKLLEGNEYIFRIMAVN 24309
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  24310 KYGVG 24314
Cdd:smart00060    79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5984-6066 5.39e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.54  E-value: 5.39e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5984 KSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQ-IVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDA 6062
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   6063 YLRV 6066
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
25810-25891 5.41e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 5.41e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25810 PPGRVTLVDVTRNTATIKWEKPEsDGGSKITGYVVEMQTKGSEKWSTCTQVK--TLEATISGLTAGEEYVFRVAAVNEKG 25887
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPgtTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 25888 RSDP 25891
Cdd:pfam00041    81 EGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17822-17904 5.51e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 5.51e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17822 PGPPRDLEVSEIRKDSCYLTWKEPLDDGG-SVVTNYVVERKDVATaQWSPLSTTSKKKSHMAKHLNEGNQYLFRVAAENQ 17900
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  17901 YGRG 17904
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26596-26678 5.51e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.65  E-value: 5.51e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26596 PSPPSKPKIVDSGKTTITIGWVKPLFDGG-APITGYTVEYKkSEETDWKVAIQSFRGTEYTMSGLTTGAEYVFRVRSLNK 26674
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYR-EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  26675 VGAS 26678
Cdd:smart00060    80 AGEG 83
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
31769-32019 5.68e-14

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 79.79  E-value: 5.68e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVET-SSKKTFMAKFVKVKgtdQVLVK-----KEISILNIARHRNILYL-------HESFesMEELVMI 31835
Cdd:cd07853       8 IGYGAFGVVWSVTDPrDGKRVALKKMPNVF---QNLVSckrvfRELKMLCFFKHDNVLSAldilqppHIDP--FEEIYVV 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFI-SGLdifERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGD 31914
Cdd:cd07853      83 TELMqSDL---HKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNS--NCVLKICDFGLARVEEPDE 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 nfRLLFTA---PEYY-APEV---HQHdvVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENI--------MNAEYTFD 31979
Cdd:cd07853     158 --SKHMTQevvTQYYrAPEIlmgSRH--YTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLItdllgtpsLEAMRSAC 233
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31980 EEAFQEI--------------------SLEAMDFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd07853     234 EGARAHIlrgphkppslpvlytlssqaTHEAVHLLCRMLVFDPDKRISAADALAHPYLDE 293
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8797-8887 5.70e-14

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 72.84  E-value: 5.70e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTT---CKMHFKNNVATLVFTQVDSNDSGEYICRAEN 8873
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  8874 SVGEVSSSTFLTVQ 8887
Cdd:cd20951      81 IHGEASSSASVVVE 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6454-6536 5.77e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.54  E-value: 5.77e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6454 SLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDGGVRENMAS 6533
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   6534 LTV 6536
Cdd:smart00410    83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
28665-28751 5.85e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 5.85e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28665 DAPGIPEPSNVTGNSITLTWTRPEsDGGNEIQHYILERREKKSTRWVKVISkRPISETRFKVTGLVEGNEYEFHVMAENA 28744
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEIT-VPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 28745 AGVGPAS 28751
Cdd:pfam00041    79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20688-20771 5.90e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.26  E-value: 5.90e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20688 PDAPPPPNIVDVRHDSVSLTWTDPKKTGG-SPITGYHIEFKERNSLlWKRANKTPIRMKdFKVTGLTEGLEYEFRVMAIN 20766
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTS-YTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  20767 LAGVG 20771
Cdd:smart00060    79 GAGEG 83
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
31757-32125 6.00e-14

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 81.07  E-value: 6.00e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG---TDQVLVKKEISILNIARHRNILYLHESF------- 31826
Cdd:PTZ00283     28 KEQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGmseADKNRAQAEVCCLLNCDFFSIVKCHEDFakkdprn 107
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31827 -ESMEELVMIFEFISGLDIFERINTSA---FELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKII 31902
Cdd:PTZ00283    108 pENVLMIALVLDYANAGDLRQEIKSRAktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS--NGLVKLG 185
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31903 EFGQARQLK---PGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYtfd 31979
Cdd:PTZ00283    186 DFGFSKMYAatvSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRY--- 262
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31980 EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLKQRMDRVSTKVIRTLRHRRYYHTLIKKDLNMVVSAARISCGG 32059
Cdd:PTZ00283    263 DPLPPSISPEMQEIVTALLSSDPKRRPSSSKLLNMPICKLFISGLLEIVQTQPGFSGPLRDTISRQIQQTKQLLQVERRR 342
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 32060 AIRSQRGVSVAKVKVASIE----IGPVSGQIMHaigeeGGYVKyvckienyDQSTQVTW---YFGVR-QLENSE 32125
Cdd:PTZ00283    343 IVRQMEESLSTAASTTILEgatpLTTLGGLTLY-----EGIVK--------KQSSDLSWkrrYLCIRgELEKGE 403
fn3 pfam00041
Fibronectin type III domain;
30546-30630 6.02e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 6.02e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30546 GKPQNPRVTDTTRTSVSLAWSVPEDeGGSKVTGYLIEMQKVD-QREWTKCNTTPTKIReYTLTHLPQGAEYRFRVLACNA 30624
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNsGEPWNEITVPGTTTS-VTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 30625 GGPGEP 30630
Cdd:pfam00041    79 GGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27878-27967 6.14e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.53  E-value: 6.14e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27878 PAACQKLQVKHVSLGTVTLLWDPPLiDGGSPIINYVIEKRDATKRTWSIVSHK-CSGTSFKVMDLSEKTPFFFRVLAENE 27956
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|.
gi 1958765569 27957 IGIGEPCETTE 27967
Cdd:cd00063      80 GGESPPSESVT 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
15630-15705 6.27e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 72.24  E-value: 6.27e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 15630 AGKTLRIPAVVTGRPVPTKVWTIEEGELD-KERVVIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAAARVEV 15705
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4572-4650 6.55e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 72.21  E-value: 6.55e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4572 PPSFVKKvDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATN 4650
Cdd:pfam13927     1 KPVITVS-PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
13703-13786 6.57e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.26  E-value: 6.57e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13703 PGPPLNVTITDVNRFGVSLTWEPPEYDGG-AEITNYVIELRDKTSiRWDTAmTVRAEDLSATVTDVVEGQEYSFRVRAQN 13781
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  13782 RIGVG 13786
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
21092-21170 6.64e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 6.64e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 21092 ISNVTKNTATVSWKRPiDDGGSEITGYHVERREKKGLRWVRATKTPVSDLRCKVTGLQEGNTYEFRVSAENRAGIGPPS 21170
Cdd:pfam00041     8 VTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24628-24710 6.76e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.26  E-value: 6.76e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24628 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEF 24707
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  24708 GVG 24710
Cdd:smart00060    81 GEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16077-16517 6.88e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 81.20  E-value: 6.88e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16077 PNGQYEFRVRAVNKYGTSDECKSDKVVIQDPYRLPGPP---GKPKVLERTKGSMLVSWTPPLDNGGSPITGYWLEKREEG 16153
Cdd:COG3401      89 PTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATtatAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGV 168
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16154 GAYWSRVSRAPITKVGLKGVEFSVP----RLIEGVKYQFRAMAINAAGIgppSEPSDPAVAGDPIYPPGPPSCPEVKDKT 16229
Cdd:COG3401     169 VVSPDTSATAAVATTSLTVTSTTLVdgggDIEPGTTYYYRVAATDTGGE---SAPSNEVSVTTPTTPPSAPTGLTATADT 245
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16230 KSSISLAWKPPAKDGgspIKGYIVEMQEEGTTDWKKVNEpdklLTACECVVPNLKELRKYRFRVKAVNEAG-ESEPSDTt 16308
Cdd:COG3401     246 PGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT----VTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNV- 317
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16309 geipatdiqevpevfidigaqdclickagsqiripavikgrptpksswefdgkakkamkdgihdipedaqletaenSSVI 16388
Cdd:COG3401     318 ----------------------------------------------------------------------------VSVT 321
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16389 VIPEctrahsgkysitaknkagqktancrvkvmdAPGPPKDLKVSDITRGSCRLSWKMPDDDGgdrIKGYVIEKKTIDGK 16468
Cdd:COG3401     322 TDLT------------------------------PPAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGG 368
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16469 AWTKVNPNCGSTAFVVPDLISEQQYFFRVRAENRFGI-GPPAETIQRTTA 16517
Cdd:COG3401     369 TYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTA 418
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
32306-32396 7.03e-14

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 72.62  E-value: 7.03e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGlDYYALHIRDTLPEDTGYYRVTATNTA 32385
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEG-DLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569 32386 GSTSCQAHLQV 32396
Cdd:cd20972      81 GSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9190-9271 7.36e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.15  E-value: 7.36e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9190 PVTASEGDFLQLSCHVQGSEPIRIQWLR-AGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSDTSKCK 9268
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   9269 VTI 9271
Cdd:smart00410    83 LTV 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
104-193 7.38e-14

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 72.39  E-value: 7.38e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSL--DFQISQEGDLYSLLIAEAYPEDSGTYSVNATNS 181
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569   182 VGRATSTADLLV 193
Cdd:cd20974      81 SGQATSTAELLV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6922-7000 7.73e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.15  E-value: 7.73e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6922 EPLEASVGDSVSLQCQVAGTPEITVSWFK-GDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTAASKT 7000
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18908-18991 8.22e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.88  E-value: 8.22e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18908 PGRPDPPEVTKVSKEEMTVVWNAPEYDGGKS-ITGYYLEKKEKHAvRWVPVNKSAiPERRLKVQNLLPGHEYQFRVKAEN 18986
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  18987 EVGIG 18991
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
23065-23145 8.31e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.29  E-value: 8.31e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23065 VVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNVK 23144
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 23145 V 23145
Cdd:pfam07679    90 V 90
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
31762-32016 8.31e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 77.86  E-value: 8.31e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd07839       1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSsalREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGlDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLK-PGDNFR 31917
Cdd:cd07839      81 CDQ-DLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLL--INKNGELKLADFGLARAFGiPVRCYS 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETN-QQMIENIMNAEYTFDEEAFQEIS-------- 31987
Cdd:cd07839     158 AEVVTLWYRPPDVlFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDvDDQLKRIFRLLGTPTEESWPGVSklpdykpy 237
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569 31988 -----------------LEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07839     238 pmypattslvnvvpklnSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
15709-15798 8.39e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.14  E-value: 8.39e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15709 PGPVLDLKPVVTNRKMCLLNWSDPADDGGsEITGFIIERKDAKMHTWRQ--PIETERSKCDITGLIEGQEYKFRVIAKNK 15786
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|..
gi 1958765569 15787 FGCGPPVEIGPI 15798
Cdd:cd00063      80 GGESPPSESVTV 91
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
31803-32015 8.40e-14

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 77.01  E-value: 8.40e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31803 LVKKEISILNIARHRNIL-YLHESFESMEE----LVMI-FEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHS 31876
Cdd:cd14012      44 LLEKELESLKKLRHPNLVsYLAFSIERRGRsdgwKVYLlTEYAPGGSLSELLDSVGS-VPLDTARRWTLQLLEALEYLHR 122
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31877 QNIGHFDIRPENI-IYQTRKNSIIKIIEFGQARQLKPGDNFRLLFTAPE--YYAPEVHQHDV-VSSATDMWSLGTLVYVL 31952
Cdd:cd14012     123 NGVVHKSLHAGNVlLDRDAGTGIVKLTDYSLGKTLLDMCSRGSLDEFKQtyWLPPELAQGSKsPTRKTDVWDLGLLFLQM 202
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31953 LSGINPFLAETNQQMIENIMNAEYTFDeeafqeisleamDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd14012     203 LFGLDVLEKYTSPNPVLVSLDLSASLQ------------DFLSKCLSLDPKKRPTALELLPHE 253
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13-97 8.60e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.15  E-value: 8.60e-14
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     13 QSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTlPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATST 92
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569     93 AELLV 97
Cdd:smart00410    81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
2756-2839 8.81e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.29  E-value: 8.81e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2756 KIIKKPKDVTALENATVAFEVSVSHDTVP-VKWFHKNVEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVV----GQ 2830
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2831 LECKAKLFV 2839
Cdd:pfam07679    82 AEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
17525-17610 9.34e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.06  E-value: 9.34e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17525 DAPEQPVVTEVTKDSALVTWNKPNDGGKPITNYILEKRETMSKRWVRVTKEPIHPYTkYRVPDLLEGCQYEFRVSAENEI 17604
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTS-VTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 17605 GIGDPS 17610
Cdd:pfam00041    80 GEGPPS 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
31154-31229 9.91e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 71.85  E-value: 9.91e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31154 VGSTLRLHVMYIGRPVPAMTWYHGQKLLQNSESITIENTEHYTHLVMKNVQRKtHAGKYKVQLSNVFGTVDAILDV 31229
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRS-DSGKYTLTLKNSAGEKSATINV 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
13602-13685 1.10e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 1.10e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13602 PGPVRNLEVTETFDGEVSLAWEEPLTDGG-SKIIGYVVERRDiKRKTWVLVTDRADSCEFTVTGLQKgGVEYLFRVSARN 13680
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKP-GTEYEFRVRAVN 78

                     ....*
gi 1958765569  13681 RVGTG 13685
Cdd:smart00060    79 GAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
21145-21521 1.13e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.43  E-value: 1.13e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21145 VTGLQEGNTYEFRVSAENRAGIGPPSdasNPVLMKDVAYPPGPPSNAHVTDTTKKSASLAWgKPHYDGGLeiTGYVVEHQ 21224
Cdd:COG3401     196 GGDIEPGTTYYYRVAATDTGGESAPS---NEVSVTTPTTPPSAPTGLTATADTPGSVTLSW-DPVTESDA--TGYRVYRS 269
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21225 KVGDDAWIKDTTGTAlriTQFVVPDLQTKEKYNFRISAVNDAGvgepavipnveiveketapdfeldaelrrtlvvragl 21304
Cdd:COG3401     270 NSGDGPFTKVATVTT---TSYTDTGLTNGTTYYYRVTAVDAAG------------------------------------- 309
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21305 sirifvpIKGRPAPEVTWTKDNInlkhranientesftlliipecnrydtgkfvmtienpagkksgfvnvrvldTPGPVL 21384
Cdd:COG3401     310 -------NESAPSNVVSVTTDLT---------------------------------------------------PPAAPS 331
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21385 NLRPTDITKDSVTLHWDLPLidgGSRITNYIVEKREATRKSYSTVTTKCHKCTYKVTGLTEGCEYFFRVMAENEYGI-GE 21463
Cdd:COG3401     332 GLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSA 408
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21464 PTE--TTEPVRASEAPLPPDSLNIMDITKNTVSLAWPKPRHDGGSKITGYVIEAQRKGSD 21521
Cdd:COG3401     409 PSEevSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAV 468
I-set pfam07679
Immunoglobulin I-set domain;
2038-2128 1.15e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.90  E-value: 1.15e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIeRSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIA 2117
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPL-RSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  2118 GETSSHAFLLV 2128
Cdd:pfam07679    80 GEAEASAELTV 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
7480-7561 1.16e-13

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 72.00  E-value: 1.16e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7480 PARIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSV 7559
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  7560 GK 7561
Cdd:cd05747      83 GK 84
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
31439-31531 1.26e-13

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 71.85  E-value: 1.26e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31439 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEiIADGLKYRVQEfKGGYHQLIIASVTDDDATVYQVRATN 31518
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKE-LQNSPDIQIHQ-EGDLHSLIIAEAFEEDTGRYSCLATN 78
                            90
                    ....*....|...
gi 1958765569 31519 QGGSVSGTASLEV 31531
Cdd:cd20972      79 SVGSDTTSAEIFV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15807-15890 1.27e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 1.27e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15807 PTSPERLTYTERTKSTITLDWKEPRSDGG-SPIQGYIIEKRRHDkPDFERVNKRlCPTTSFLVDNLDEHQMYEFRVKAVN 15885
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  15886 DIGES 15890
Cdd:smart00060    79 GAGEG 83
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
21587-21667 1.31e-13

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 71.41  E-value: 1.31e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQ-RVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITI 21665
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 21666 QV 21667
Cdd:cd05894      85 KV 86
fn3 pfam00041
Fibronectin type III domain;
28767-28849 1.33e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 71.29  E-value: 1.33e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28767 SAPAVVKVTDTSKTTVSLEWARPvFDGGMEIIGYIIEMCKADLGDWHKVNTEPCVKTRYTVTDLQAGEEYKFRVSAINGA 28846
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ...
gi 1958765569 28847 GKG 28849
Cdd:pfam00041    80 GEG 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20787-20867 1.38e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 1.38e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20787 DPPGKPEVISVTRNSVTLIWTEPKYDGG-HKLTGYIVEKRDlPSKSWMKANhVNVPDCAFTVTDLVEGGKYEFRIRAKNT 20865
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ..
gi 1958765569  20866 AG 20867
Cdd:smart00060    80 AG 81
fn3 pfam00041
Fibronectin type III domain;
30850-30928 1.39e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 71.29  E-value: 1.39e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 30850 VLDVTKSSVSLSWSRPkDDGGSRVTGYYIERKETSTDKWVRHNKTQITTTMYTVTGLVPDAEYQFRIIAQNDVGLSETS 30928
Cdd:pfam00041     8 VTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7199-7290 1.42e-13

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 71.46  E-value: 1.42e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7199 PPKFIKKLDTSKVAkQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNG 7278
Cdd:cd20972       1 PPQFIQKLRSQEVA-EGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  7279 VGHASCSTALKV 7290
Cdd:cd20972      80 VGSDTTSAEIFV 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7577-7666 1.44e-13

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 71.65  E-value: 1.44e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRK-LKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKcQPSFADNvcTLTLSSLEPSDTGAYTCVAANVA 7655
Cdd:cd20978       1 PKFIQKpEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPME-RATVEDG--TLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  7656 GQDESSALLTV 7666
Cdd:cd20978      78 GDIYTETLLHV 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
20588-20671 1.46e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 1.46e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20588 PGIPTGpIKFDEVTAEAMTLKWGPPKDDGG-SEITNYVLEKRDSvNNKWVTCASAVQKTTFRVTRLHEGIEYTFRVSAEN 20666
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  20667 KYGVG 20671
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23935-24018 1.56e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.56e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23935 PGPPGTPFVTAVSKDSMVVQWHEP-INNGGSPVIGYHLERKERNSiLWTKVNKTIIhDTQFKALNLEEGIEYEFRVYAEN 24013
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYRVEYREEGS-EWKEVNVTPS-STSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  24014 IVGVG 24018
Cdd:smart00060    79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12983-13047 1.57e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 71.38  E-value: 1.57e-13
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  12983 NLEVSEGDTIKLVCEVS-KPGAEVTWYK-GDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCR 13047
Cdd:smart00410     3 SVTVKEGESVTLSCEASgSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCA 69
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
31761-32017 1.58e-13

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 76.96  E-value: 1.58e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISIL-NIARHRNILYLHESFESM------EELV 31833
Cdd:cd06608       6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILrKFSNHPNIATFYGAFIKKdppggdDQLW 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISG---LDIFERINTSAFELNErEVVSYV-RQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQ 31909
Cdd:cd06608      86 LVMEYCGGgsvTDLVKGLRKKGKRLKE-EWIAYIlRETLRGLAYLHENKVIHRDIKGQNILLT--EEAEVKLVDFGVSAQ 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LKPGDNFRLLFTAPEYY-APEV----HQHDVV-SSATDMWSLGTLVYVLLSGINPfLAETN--QQMIENIMNAEYTFDEE 31981
Cdd:cd06608     163 LDSTLGRRNTFIGTPYWmAPEViacdQQPDASyDARCDVWSLGITAIELADGKPP-LCDMHpmRALFKIPRNPPPTLKSP 241
                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 1958765569 31982 AfqEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06608     242 E--KWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27478-27570 1.64e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 71.37  E-value: 1.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27478 PGPPGGpIEFKTVTAEKITLLWRPPADDGGaKITHYIVEKRETSRVVWSMVA-ENLEECIITTTKIIKGNEYIFRVRAVN 27556
Cdd:cd00063       1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....
gi 1958765569 27557 KYGIGEPLESEPVV 27570
Cdd:cd00063      79 GGGESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
27680-27765 1.64e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 71.29  E-value: 1.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27680 GPPAKIRIADSTKSSITLGWSKPVyDGGSDVTGYVVEMRQ-GEEEEWTIVSTKGEarTTEYVVSNLKPGVNYYFQVSAVN 27758
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPkNSGEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 27759 CAGQGEP 27765
Cdd:pfam00041    78 GGGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16111-16199 1.66e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.66e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16111 PGPPGKPKVLERTKGSMLVSWTPPL-DNGGSPITGYWLEKREEGGAyWSRVSRAPITKvglkgvEFSVPRLIEGVKYQFR 16189
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPdDGITGYIVGYRVEYREEGSE-WKEVNVTPSST------SYTLTGLKPGTEYEFR 73
                             90
                     ....*....|
gi 1958765569  16190 AMAINAAGIG 16199
Cdd:smart00060    74 VRAVNGAGEG 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7874-7942 1.73e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 70.82  E-value: 1.73e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7874 TLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSAV 7942
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8517-8594 1.75e-13

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 71.06  E-value: 1.75e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8517 PPSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATN 8594
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
31337-31420 1.76e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.76e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31337 PSVPGKPTITAVTKDSCVVAWKPPASDGGAKIRNYYLEKREKKQNKWIAVTTEEiRETVFSVQNLIEGLEYEFRVKCENL 31416
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  31417 GGES 31420
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17424-17507 1.76e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.76e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17424 PGPPVGPVVfDEVTKEYMVISWKPPLDDGG-SEITNYIIEKKELGKDiWMPVTSASAKTTCKVPKLLEGKDYIFRIHAEN 17502
Cdd:smart00060     1 PSPPSNLRV-TDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  17503 LYGIS 17507
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19504-19587 1.79e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.79e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19504 PGPPqPPFDISEIDADACSLSWHIPLEDGG-SNITNYIVEKCDVSrGDWVTALASVTKTSCRVGKLIPGQEYIFRVRAEN 19582
Cdd:smart00060     1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  19583 RFGIS 19587
Cdd:smart00060    79 GAGEG 83
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
20513-20584 1.82e-13

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 71.02  E-value: 1.82e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 20513 RLKIPIKGKPAPSVSWKKGEDPL-ATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKV 20584
Cdd:cd05894      14 RLDVPISGEPAPTVTWSRGDKAFtATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24432-24516 1.85e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.11  E-value: 1.85e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24432 PGPPTNVHIVDTTKNSITLAWGKPIYDGG-SDILGYVVEICKADeEEWQIVTPQTglRVTRFEISKLIEHQEYKIRVCAL 24510
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  24511 NKVGLG 24516
Cdd:smart00060    78 NGAGEG 83
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
31765-31959 1.85e-13

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 78.14  E-value: 1.85e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHRCVETSSKKTFMakfVKVKGTDQV----LVKKE-------ISILNIARH--------RNILYLHES 31825
Cdd:cd05617       8 ISQGLGLQDFDLIRVIGRGSYAKVLL---VRLKKNDQIyamkVVKKElvhddedIDWVQTEKHvfeqassnPFLVGLHSC 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31826 FESMEELVMIFEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFG 31905
Cdd:cd05617      85 FQTTSRLFLVIEYVNGGDLMFHMQRQR-KLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLD--ADGHIKLTDYG 161
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31906 QARQ-LKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd05617     162 MCKEgLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
31769-32012 1.94e-13

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 76.54  E-value: 1.94e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVeTSSKKTFMAKFVKVKgTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd14066       1 IGSGGFGTVYKGV-LENGTVVAVKRLNEM-NCAASKKeflTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERI--NTSAFELNEREVVSYVRQVCEALEFLHSQN---IGHFDIRPENIIYQTRKNSiiKIIEFGQARQLKPGDNFR--- 31917
Cdd:cd14066      79 DRLhcHKGSPPLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEP--KLTDFGLARLIPPSESVSkts 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMnaeytfdEEAFQEISLEAMDFIDRL 31997
Cdd:cd14066     157 AVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLV-------EWVESKGKEELEDILDKR 229
                           250
                    ....*....|....*
gi 1958765569 31998 LVKERKSRMTASEAL 32012
Cdd:cd14066     230 LVDDDGVEEEEVEAL 244
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
31763-32017 1.95e-13

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 77.44  E-value: 1.95e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIV--HRCVETSSKKTFMAKFVKVKGTDQVLVKK---EISILNIAR-HRNILYLHES---FESMEELV 31833
Cdd:cd07857       2 YELIKELGQGAYGIVcsARNAETSEEETVAIKKITNVFSKKILAKRalrELKLLRHFRgHKNITCLYDMdivFPGNFNEL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINtSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPG 31913
Cdd:cd07857      82 YLYEELMEADLHQIIR-SGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA--DCELKICDFGLARGFSEN 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 ----DNFRLLFTAPEYY-APEVH-QHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEI- 31986
Cdd:cd07857     159 pgenAGFMTEYVATRWYrAPEIMlSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPDEETLSRIg 238
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31987 --------------------------SLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07857     239 spkaqnyirslpnipkkpfesifpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
31762-31960 2.05e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 76.65  E-value: 2.05e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMiaEDLGRGEFGIVHRC-VETSSKKTFMAKFVKVKGTDQVLV-----KKEISILNIARHRNILYLHESFESMEELVM- 31834
Cdd:cd05038       7 KFI--KQLGEGHFGSVELCrYDPLGDNTGEQVAVKSLQPSGEEQhmsdfKREIEILRTLDHEYIVKYKGVCESPGRRSLr 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 -IFEFIS--GLDIFERINtsAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLK 31911
Cdd:cd05038      85 lIMEYLPsgSLRDYLQRH--RDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVE--SEDLVKISDFGLAKVLP 160
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31912 PGDNFrllFTAPE-------YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFL 31960
Cdd:cd05038     161 EDKEY---YYVKEpgespifWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ 213
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
19480-20137 2.13e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 79.66  E-value: 2.13e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19480 YYSLTAENSSGTDTQKIKVTVMDAPGPPQPPFDISEIDADACSLSWhiPLEDGGSNITNYIVEKCDVSRGDWVTALASVT 19559
Cdd:COG3401      20 NTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGG--GLGTGGRAGTTSGVAAVAVAAAPPTATGLTTL 97
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19560 KTSCRVGKLIPGQEYIFRVRAENRFGISEPLTSPKMLAKFPFDVPSEPKNARVTKVNKDCIFVAWDRPDSDGGSPITGYL 19639
Cdd:COG3401      98 TGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSAT 177
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19640 IErkernslLWVKANDTIVRSTEYPCAGLVEGLEYSFRIYALNKAGSSPPSKPTEYVTARMPVDPPGKPEVVDVTKNSAS 19719
Cdd:COG3401     178 AA-------VATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVT 250
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19720 LIWARPKHDGgskIIGYFVEACKLPGDKWVRCNTTPHQipleEYTATGLEENAQYQFRAIAKTAVNIsqPSEPSDPVTIL 19799
Cdd:COG3401     251 LSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTTT----SYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVT 321
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19800 AENVPPrielsvemkslltvkagtnvcldatvfgkpmptvswkkdstpikqtegvkmamkrnlctlelfsvnrkdsgdyt 19879
Cdd:COG3401     322 TDLTPP-------------------------------------------------------------------------- 327
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19880 itaenssgsksatiklkvldkpGPPASVKINKMYADRAMLSWEPPLedgGSEITNYIVDKRETSRPNWAQVSATVPITSC 19959
Cdd:COG3401     328 ----------------------AAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAETVTTTSY 382
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19960 TVEKLIEGHEYQFRICAENKYGVGDPIFTEPVIAKNPYDPPGRCDPPVISNITKDhmTVSWKAPADDGGSPITGYLVEKR 20039
Cdd:COG3401     383 TDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTD--VAGATAAASAASNPGVSAAVLAD 460
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20040 ETQAVNWTKVNRkpviERTLKATGLQEGTEYEFRVTAINKAGPGKPSDASKAVYAQDPLYPPGPPAFPKVYDTTRSSVSL 20119
Cdd:COG3401     461 GGDTGNAVPFTT----TSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPV 536
                           650
                    ....*....|....*...
gi 1958765569 20120 SWGKPAFDGGSPIIGYLV 20137
Cdd:COG3401     537 TVGASTGDVLITDLVSLT 554
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28169-28252 2.20e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.72  E-value: 2.20e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28169 PSKPKGpIRFDEIKADSAIMSWDIPEDDGG-GEITCYSIEKREASqTNWKMVCSSVARTTFKVSNLVKDSEYQFRVRAEN 28247
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  28248 RYGVS 28252
Cdd:smart00060    79 GAGEG 83
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
31769-32012 2.20e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 76.18  E-value: 2.20e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK--KEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFE 31846
Cdd:cd13996      14 LGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKvlREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTLRD 93
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31847 RIN--TSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsIIKIIEFGQARQLKPGDNFRLLFTAPE 31924
Cdd:cd13996      94 WIDrrNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDL-QVKIGDFGLATSIGNQKRELNNLNNNN 172
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31925 ---------------YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINpflaeTNQQMIENIMNA-EYTFDEEAFQEISL 31988
Cdd:cd13996     173 ngntsnnsvgigtplYASPEQLDGENYNEKADIYSLGIILFEMLHPFK-----TAMERSTILTDLrNGILPESFKAKHPK 247
                           250       260
                    ....*....|....*....|....
gi 1958765569 31989 EAmDFIDRLLVKERKSRMTASEAL 32012
Cdd:cd13996     248 EA-DLIQSLLSKNPEERPSAEQLL 270
I-set pfam07679
Immunoglobulin I-set domain;
9581-9663 2.36e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 70.75  E-value: 2.36e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9581 PAWERHLQDVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTCK----HE 9655
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVatnsAG 80

                    ....*...
gi 1958765569  9656 DLETSAEL 9663
Cdd:pfam07679    81 EAEASAEL 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4387-4476 2.43e-13

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 70.99  E-value: 2.43e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSP-SPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKF 4465
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  4466 GADICQAELTI 4476
Cdd:cd05744      81 GENSFNAELVV 91
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
31759-32017 2.44e-13

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 77.36  E-value: 2.44e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMA-KFVKVKGTDQVLVKKEISILNIARHRN------ILYLHESFESMEE 31831
Cdd:cd14215      10 LQERYEIVSTLGEGTFGRVVQCIDHRRGGARVAlKIIKNVEKYKEAARLEINVLEKINEKDpenknlCVQMFDWFDYHGH 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFI--SGLDIFERINTSAFELNEREVVSYvrQVCEALEFLHSQNIGHFDIRPENIIY-----------------Q 31892
Cdd:cd14215      90 MCISFELLglSTFDFLKENNYLPYPIHQVRHMAF--QVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrdeR 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31893 TRKNSIIKIIEFGQARqlKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQ---MIE 31969
Cdd:cd14215     168 SVKSTAIRVVDFGSAT--FDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREhlaMME 245
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31970 NIM------------------NAEYTFDEEAF-------------QEISLEA------MDFIDRLLVKERKSRMTASEAL 32012
Cdd:cd14215     246 RILgpipsrmirktrkqkyfyHGRLDWDENTSagryvrenckplrRYLTSEAeehhqlFDLIESMLEYEPSKRLTLAAAL 325

                    ....*
gi 1958765569 32013 KHPWL 32017
Cdd:cd14215     326 KHPFF 330
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
31062-31130 2.51e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 70.05  E-value: 2.51e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31062 AQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSS 31130
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8796-8873 2.56e-13

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 70.29  E-value: 2.56e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8796 PPYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAEN 8873
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8814-8883 2.59e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 70.05  E-value: 2.59e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8814 ASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGEVSSSTF 8883
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
1253-1337 2.64e-13

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 70.68  E-value: 2.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1253 IKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICS 1332
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                    ....*
gi 1958765569  1333 GKLYV 1337
Cdd:cd20973      84 AELTV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7487-7570 2.74e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.61  E-value: 2.74e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7487 PEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRE-LSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGKSSCT 7565
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   7566 VSVHV 7570
Cdd:smart00410    81 TTLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
32306-32396 2.76e-13

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 70.60  E-value: 2.76e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGP-HIEIVHEGlDYYALHIRDTLPEDTGYYRVTATNT 32384
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSaHKMLVREN-GRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569 32385 AGSTSCQAHLQV 32396
Cdd:cd05744      80 AGENSFNAELVV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7863-7945 2.77e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.61  E-value: 2.77e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7863 EHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPA-YKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSA 7941
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   7942 VLVI 7945
Cdd:smart00410    82 TLTV 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
31044-31134 2.78e-13

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 70.69  E-value: 2.78e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31044 APGVRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEV 31123
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569 31124 GEVETSSKLLL 31134
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5716-5783 2.83e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 70.05  E-value: 2.83e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5716 TFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDA-GTASCSI 5783
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31763-32017 2.84e-13

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 75.78  E-value: 2.84e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTD------------QVLVKKEISilniARHRNILYLHESFESM 31829
Cdd:cd14100       2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVeKDRVSEwgelpngtrvpmEIVLLKKVG----SGFRGVIRLLDWFERP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGL-DIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiIKIIEFGQAR 31908
Cdd:cd14100      78 DSFVLVLERPEPVqDLFDFI-TERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGE-LKLIDFGSGA 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31909 QLKpgDNFRLLFTAPEYYAP----EVHQHDVVSSAtdMWSLGTLVYVLLSGINPFlaetnqQMIENIMNAEYTFDeeafQ 31984
Cdd:cd14100     156 LLK--DTVYTDFDGTRVYSPpewiRFHRYHGRSAA--VWSLGILLYDMVCGDIPF------EHDEEIIRGQVFFR----Q 221
                           250       260       270
                    ....*....|....*....|....*....|...
gi 1958765569 31985 EISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14100     222 RVSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
1430-1507 2.88e-13

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 70.68  E-value: 2.88e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1430 EGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRAGKSTISVTLTV 1507
Cdd:cd20973      11 EGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
22853-22936 2.92e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.34  E-value: 2.92e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22853 PGPPGTPFVTLASKDSMEVQWHEPVSDGG-SRVIGYHLERKERNSiLWVKLNKTPiPQTKFKTTGLEEGIEYEFRVSAEN 22931
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  22932 IVGIG 22936
Cdd:smart00060    79 GAGEG 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
906-989 2.94e-13

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 70.68  E-value: 2.94e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   906 LKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITF-QSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTS 984
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                    ....*
gi 1958765569   985 CYLAV 989
Cdd:cd20973      84 AELTV 88
fn3 pfam00041
Fibronectin type III domain;
16218-16305 3.01e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 3.01e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16218 GPPSCPEVKDKTKSSISLAWKPPaKDGGSPIKGYIVEMQEEGTTD-WKKVNEPdklLTACECVVPNLKELRKYRFRVKAV 16296
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVP---GTTTSVTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 16297 NEAGESEPS 16305
Cdd:pfam00041    77 NGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14696-14779 3.03e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.34  E-value: 3.03e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14696 PGPPYALTVVDVTKRHVDLKWEPPKNDGGR-PIQRYIIEKKEKlGTRWVKAgKTSGPDCNFRVTDVIEGTEVQFQVRAEN 14774
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  14775 EAGVG 14779
Cdd:smart00060    79 GAGEG 83
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
31761-32018 3.13e-13

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 77.58  E-value: 3.13e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTF-MAKFVKVK--GTDQVL-VKKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd05629       1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYaMKTLLKSEmfKKDQLAhVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFER-INTSAFelNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFG---------- 31905
Cdd:cd05629      81 EFLPGGDLMTMlIKYDTF--SEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH--IKLSDFGlstgfhkqhd 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31906 --------QARQLKPGD--------------------------NFRLL----FTAPEYYAPEVHQHDVVSSATDMWSLGT 31947
Cdd:cd05629     157 sayyqkllQGKSNKNRIdnrnsvavdsinltmsskdqiatwkkNRRLMaystVGTPDYIAPEIFLQQGYGQECDWWSLGA 236
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31948 LVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLV--KERKSRMTASEALKHPWLK 32018
Cdd:cd05629     237 IMFECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLITnaENRLGRGGAHEIKSHPFFR 309
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
31761-32017 3.15e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 76.20  E-value: 3.15e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV--LVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd07871       5 ETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGApcTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEY 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGlDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQAR-QLKPGDNFR 31917
Cdd:cd07871      85 LDS-DLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE--LKLADFGLARaKSVPTKTYS 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEVHQHDV-VSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEIS--------- 31987
Cdd:cd07871     162 NEVVTLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTsneefrsyl 241
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 1958765569 31988 -----------------LEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07871     242 fpqyraqplinhaprldTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
fn3 pfam00041
Fibronectin type III domain;
18217-18301 3.19e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 3.19e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18217 SPPGKPVVTDITENAATVSWTLPKsDGGSPITGYYVERREITG----KWVRVNKTPIadlKFRVTGLYEGNTYEFRVFAE 18292
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgepwNEITVPGTTT---SVTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 18293 NLAGLSNPS 18301
Cdd:pfam00041    77 NGGGEGPPS 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
900-989 3.36e-13

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 70.57  E-value: 3.36e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQ--SGIARLMIREAFAEDSGRFTCSAVNE 977
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQdnCGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569   978 AGTVSTSCYLAV 989
Cdd:cd05892      81 AGVVSCNARLDV 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17124-17331 3.42e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 78.89  E-value: 3.42e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17124 VLDVPGPVGIPFLSDNLTNDSCKLTWFSPeDDGGSPITNYVIQKREADRRAWTPVTYTVTRQNATVQGLIQ-GKSYFFRI 17202
Cdd:COG3401     131 VAGGAATAGTYALGAGLYGVDGANASGTT-ASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEpGTTYYYRV 209
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17203 AAENSIGMGPFVETPNALVirdPITVPERPEDLEVKEVTKNTVTLTWNPPKYDGgseIINYVLESRLIGTEKFHKVTNDN 17282
Cdd:COG3401     210 AATDTGGESAPSNEVSVTT---PTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT 283
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 1958765569 17283 LLSrkYTVKGLKEGDTYEYRVSAVNivGQGKPSFCTKPITCKDELAPPT 17331
Cdd:COG3401     284 TTS--YTDTGLTNGTTYYYRVTAVD--AAGNESAPSNVVSVTTDLTPPA 328
fn3 pfam00041
Fibronectin type III domain;
14001-14084 3.52e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.14  E-value: 3.52e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14001 SAPKELKFSDVTKDSVHLTWEPPdDDGGSPLTGYVVEKRDMSR-KTWTKVMDFVTDLEFTVPDLVQGKEYLFKVCARNKC 14079
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 14080 GPGEP 14084
Cdd:pfam00041    80 GEGPP 84
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
31762-32018 3.55e-13

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 77.13  E-value: 3.55e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKfvKVKGTDQVLVK---KEISILNIARHRNILYLHESFES-----MEELV 31833
Cdd:cd07854       6 RYMDLRPLGCGSNGLVFSAVDSDCDKRVAVK--KIVLTDPQSVKhalREIKIIRRLDHDNIVKVYEVLGPsgsdlTEDVG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINTSAFELNEREVVS--YVR----QVCEALEFLHSQNIGHFDIRPENIIYQTrKNSIIKIIEFGQA 31907
Cdd:cd07854      84 SLTELNSVYIVQEYMETDLANVLEQGPLSeeHARlfmyQLLRGLKYIHSANVLHRDLKPANVFINT-EDLVLKIGDFGLA 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLKP----GDNFRLLFTAPEYYAPEVHQH-DVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEA 31982
Cdd:cd07854     163 RIVDPhyshKGYLSEGLVTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPVVREED 242
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31983 FQEI--------------------------SLEAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd07854     243 RNELlnvipsfvrndggeprrplrdllpgvNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28519-29061 3.63e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 78.89  E-value: 3.63e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28519 ITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEITVKVQDTPGKVVGPIRFT--NITGEKMTLWWEAPLNDGCAPV 28596
Cdd:COG3401      21 TAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTsgVAAVAVAAAPPTATGLTTLTGS 100
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28597 THYIIEKRETSRLAWALIEDHCEAQSYTAIKLITGNEYQFRVSAVNKFGVGRPLESDPVVAQIQYTIPDAPGIPEPSNVT 28676
Cdd:COG3401     101 GSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAV 180
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28677 GNSITLTWTRPESDGGNEIQHyilerrekkstrwvkviskrpisetrfkvtglveGNEYEFHVMAENAAGVGPASGISRL 28756
Cdd:COG3401     181 ATTSLTVTSTTLVDGGGDIEP----------------------------------GTTYYYRVAATDTGGESAPSNEVSV 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28757 IKcrePVNPPSAPAVVKVTDTSKTTVSLEWaRPVFDGGmeIIGYIIEMCKADLGDWHKVNTEPcvKTRYTVTDLQAGEEY 28836
Cdd:COG3401     227 TT---PTTPPSAPTGLTATADTPGSVTLSW-DPVTESD--ATGYRVYRSNSGDGPFTKVATVT--TTSYTDTGLTNGTTY 298
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28837 KFRVSAINGAGK--GDSCEVTGTikavdrlsapeldidanfkqthivragasirlfiayqgrPTPTAvwskpdsnlsira 28914
Cdd:COG3401     299 YYRVTAVDAAGNesAPSNVVSVT---------------------------------------TDLTP------------- 326
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28915 dihttdsfstltvencnrndagkytltvennsgrksitftvkvldsPGPPGPITFKDVTRGSATLMWDAPLldgGARIHH 28994
Cdd:COG3401     327 ----------------------------------------------PAAPSGLTATAVGSSSITLSWTASS---DADVTG 357
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 28995 YVIEKREASRRSWQVVSEKCTRQILKVSDLTEGVPYYFRVSAENEYGVGEPYemPEPIVATEQPAPP 29061
Cdd:COG3401     358 YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAP--SEEVSATTASAAS 422
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4967-5035 3.68e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 69.67  E-value: 3.68e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4967 RLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSRGA 5035
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
31762-32017 3.84e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 75.92  E-value: 3.84e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd07861       1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPStaiREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISgLDIFERINT--SAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLK-PGDN 31915
Cdd:cd07861      81 LS-MDLKKYLDSlpKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLID--NKGVIKLADFGLARAFGiPVRV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPEVHQHDV-VSSATDMWSLGTlVYVLLSGINPFL---AETNQQM----------------IENIMNAE 31975
Cdd:cd07861     158 YTHEVVTLWYRAPEVLLGSPrYSTPVDIWSIGT-IFAEMATKKPLFhgdSEIDQLFrifrilgtptediwpgVTSLPDYK 236
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*....
gi 1958765569 31976 YTFDE-------EAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07861     237 NTFPKwkkgslrTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
14797-14881 4.31e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.95  E-value: 4.31e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14797 PSPPLDLHVTDAGRKHIAIAWKPPEK-NGGSPIIGYHVEMCPVGTEkWMRVNSRPiKDLKFKVeEGVVPDKEYVLRVRAV 14875
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDdGITGYIVGYRVEYREEGSE-WKEVNVTP-SSTSYTL-TGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  14876 NAVGVS 14881
Cdd:smart00060    78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23350-23434 4.57e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.95  E-value: 4.57e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23350 PGPPNNPKVMDVTRSSVFLSWTKPIYDGG-CEIQGYIVEKCDVSvGEWTMCTPPTgiNKTNLEVEKLLEKHEYNFRICAI 23428
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  23429 NKAGVG 23434
Cdd:smart00060    78 NGAGEG 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5697-5787 4.62e-13

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 70.22  E-value: 4.62e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVLRnGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGIsFVD--GLATFQISNARVENSGTYVCEARN 5774
Cdd:cd05744       1 PHFLQAPGDLEVQE-GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM-LVRenGRHSLIIEPVTKRDAGIYTCIARN 78
                            90
                    ....*....|...
gi 1958765569  5775 DAGTASCSIELKV 5787
Cdd:cd05744      79 RAGENSFNAELVV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9677-9758 4.74e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.84  E-value: 4.74e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9677 QNIVVSEHQSATFECEVS-FDDAIVTWYK-GPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEpRGEARST 9754
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNS-SGSASSG 80

                     ....
gi 1958765569   9755 AELY 9758
Cdd:smart00410    81 TTLT 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8048-8137 4.80e-13

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 70.22  E-value: 4.80e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVEN-TATLTVLKVAKGDAGQYTCYASNVA 8126
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  8127 GKDSCSAQLGV 8137
Cdd:cd05744      81 GENSFNAELVV 91
fn3 pfam00041
Fibronectin type III domain;
20300-20383 4.99e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 4.99e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20300 GPPVNVTVKEISKDSAYITWDPPIiDGGSPIINYVVEKRDAER-KSWSTVTTECPKTSFRVSNLEEGKSYFFRVFAENEY 20378
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 20379 GIGDP 20383
Cdd:pfam00041    80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
25415-25500 5.04e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 5.04e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25415 GPPSTPEASAITKDSMVLTWTRPvDDGGAEIEGYILEKRDKEGIRWTKCNKKTLTDLRFRVTGLTEGHSYEFRVAAENAA 25494
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 25495 GVGEPS 25500
Cdd:pfam00041    80 GEGPPS 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
3304-3391 5.08e-13

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 69.92  E-value: 5.08e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3304 PPAIVTPLQDAVTSEGRPARFQCQVSGTDL-KVSWYCRDKKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAV 3382
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTpVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....*....
gi 1958765569  3383 GQVSSTATL 3391
Cdd:cd20972      81 GSDTTSAEI 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
31455-31531 5.12e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.84  E-value: 5.12e-13
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  31455 SNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVqEFKGGYHQLIIASVTDDDATVYQVRATNQGGSVSGTASLEV 31531
Cdd:smart00410    10 ESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSV-SRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
917-984 5.28e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 69.28  E-value: 5.28e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   917 VTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTS 984
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6558-6626 5.33e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 69.28  E-value: 5.33e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6558 SLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAV 6626
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
31762-32017 5.34e-13

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 76.11  E-value: 5.34e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAkfVKVKGTDQVLVK---KEISIL---NIA-----RHrnILYLHESFESME 31830
Cdd:cd14135       1 RYRVYGYLGKGVFSNVVRARDLARGNQEVA--IKIIRNNELMHKaglKELEILkklNDAdpddkKH--CIRLLRHFEHKN 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 ELVMIFEFISG-----LDIFER---INTSAfelnereVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsIIKII 31902
Cdd:cd14135      77 HLCLVFESLSMnlrevLKKYGKnvgLNIKA-------VRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKN-TLKLC 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31903 EFGQArqLKPGDNFRLLFTAPEYY-APEV---HQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIM------ 31972
Cdd:cd14135     149 DFGSA--SDIGENEITPYLVSRFYrAPEIilgLPYD---YPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMdlkgkf 223
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31973 ------NAEYT---FDEEA---FQEIS--------------------------------------LEAMDFIDRLLVKER 32002
Cdd:cd14135     224 pkkmlrKGQFKdqhFDENLnfiYREVDkvtkkevrrvmsdikptkdlktlligkqrlpdedrkklLQLKDLLDKCLMLDP 303
                           330
                    ....*....|....*
gi 1958765569 32003 KSRMTASEALKHPWL 32017
Cdd:cd14135     304 EKRITPNEALQHPFI 318
I-set pfam07679
Immunoglobulin I-set domain;
19417-19500 5.40e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 5.40e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19417 PEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKI 19496
Cdd:pfam07679     7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASA 86

                    ....
gi 1958765569 19497 KVTV 19500
Cdd:pfam07679    87 ELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
13521-13598 5.56e-13

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 69.54  E-value: 5.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13521 LVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTK---TVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKAEGFINLQ 13597
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETgrvQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 13598 V 13598
Cdd:cd05748      82 V 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5994-6059 5.76e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 69.28  E-value: 5.76e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5994 VTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSS 6059
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
fn3 pfam00041
Fibronectin type III domain;
15809-15893 5.78e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 5.78e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15809 SPERLTYTERTKSTITLDWKEPRsDGGSPIQGYIIEKRRHDKPD--FERVNKRlcPTTSFLVDNLDEHQMYEFRVKAVND 15886
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEpwNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 15887 IGESEPS 15893
Cdd:pfam00041    79 GGEGPPS 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6539-6620 5.81e-13

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 70.08  E-value: 5.81e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6539 PAVIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNV 6618
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  6619 GK 6620
Cdd:cd05747      83 GK 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7218-7287 5.82e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 69.28  E-value: 5.82e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7218 IQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVGHASCSTA 7287
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
23149-23232 5.83e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.57  E-value: 5.83e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23149 PGPPEGPVaISGVTAEKCMLAWKPPLQDGG-SDIINYIVERRETSRlVWTLVDANVQTLSCKVTKLLEGNEYIFRIMAVN 23227
Cdd:smart00060     1 PSPPSNLR-VTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  23228 KYGVG 23232
Cdd:smart00060    79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
5322-5411 5.83e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 5.83e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5322 PSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAG 5401
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  5402 IQRCSALLSV 5411
Cdd:pfam07679    81 EAEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4292-4381 5.96e-13

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 69.76  E-value: 5.96e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESD---KCSIRSSNYISSLEILRTQVVDCGEYTCKASN 4368
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569  4369 EYGSVSCTATLTV 4381
Cdd:cd20951      81 IHGEASSSASVVV 93
fn3 pfam00041
Fibronectin type III domain;
22269-22354 6.01e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 6.01e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22269 GPPGNPRVLDTSRSSISIAWNKPiYDGGSEITGYMVEIALP-EEDEWQVVTPPAGlkATSYTITNLIENQEYKIRIYAMN 22347
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnSGEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 22348 SEGLGEP 22354
Cdd:pfam00041    78 GGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
17128-17216 6.06e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 69.83  E-value: 6.06e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17128 PGPVGIPFLSDNlTNDSCKLTWFSPEDDGGsPITNYVIQKREADRRAWTPVTYTVTRQN-ATVQGLIQGKSYFFRIAAEN 17206
Cdd:cd00063       1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETsYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|
gi 1958765569 17207 SIGMGPFVET 17216
Cdd:cd00063      79 GGGESPPSES 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
13922-13996 6.25e-13

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 69.54  E-value: 6.25e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 13922 NPIKILVPSTGYPRPKATWTFGDQVLEAGDRVKIKTISAYAELIISPSERPDKGIYTLTLENPVKSISGEIDVNV 13996
Cdd:cd05748       8 ESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
I-set pfam07679
Immunoglobulin I-set domain;
20900-20981 6.49e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.59  E-value: 6.49e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20900 LTVKAGDSIVLSaISILGKPLPKSSWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEHVKV 20979
Cdd:pfam07679    10 VEVQEGESARFT-CTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569 20980 SV 20981
Cdd:pfam07679    89 TV 90
I-set pfam07679
Immunoglobulin I-set domain;
29569-29649 6.56e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.59  E-value: 6.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29569 VTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMVK 29648
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 29649 V 29649
Cdd:pfam07679    90 V 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
33418-33504 6.72e-13

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 69.69  E-value: 6.72e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33418 IVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSV 33497
Cdd:cd05747       6 ILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQ 85

                    ....*..
gi 1958765569 33498 SSSCKLT 33504
Cdd:cd05747      86 EAQFTLT 92
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
31763-31962 7.11e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 75.45  E-value: 7.11e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRC------VETSSKKTFMAKFVKVKGTDQVLvkKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd08229      26 FRIEKKIGRGQFSEVYRAtclldgVPVALKKVQIFDLMDAKARADCI--KEIDLLKQLNHPNVIKYYASFIEDNELNIVL 103
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFE---LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPG 31913
Cdd:cd08229     104 ELADAGDLSRMIKHFKKQkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITA--TGVVKLGDLGLGRFFSSK 181
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DN-FRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAE 31962
Cdd:cd08229     182 TTaAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
31769-32015 7.18e-13

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 74.94  E-value: 7.18e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVhrC---VETSSK----KTFMAKFVKVKGTDQV-LVKKEIsiLNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd05607      10 LGKGGFGEV--CavqVKNTGQmyacKKLDKKRLKKKSGEKMaLLEKEI--LEKVNSPFIVSLAYAFETKTHLCLVMSLMN 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDI-FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiiKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd05607      86 GGDLkYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNC--RLSDLGLAVEVKEGKPITQR 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFL----AETNQQMIENIMNAEYTFDEEAFQEislEAMDFID 31995
Cdd:cd05607     164 AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRdhkeKVSKEELKRRTLEDEVKFEHQNFTE---EAKDICR 240
                           250       260
                    ....*....|....*....|
gi 1958765569 31996 RLLVKERKSRMTASEALKHP 32015
Cdd:cd05607     241 LFLAKKPENRLGSRTNDDDP 260
I-set pfam07679
Immunoglobulin I-set domain;
12976-13047 7.23e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.59  E-value: 7.23e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12976 VFTKNLANLEVSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCR 13047
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV 74
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3591-3667 7.48e-13

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 69.53  E-value: 7.48e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  3591 GIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIIHNPDGSGTFIVNDPQRGDSGLYICKAENLWGTSTCTAELLV 3667
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
fn3 pfam00041
Fibronectin type III domain;
24726-24808 8.29e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 8.29e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24726 SPPGKVTLTDVSQTSASLMWEKPEhDGGSRILGYVVEMQPKGTE---KWSVVAESKVcSAVVSGLSSGQEYQFRVKAYNE 24802
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGepwNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 24803 KGKSDP 24808
Cdd:pfam00041    79 GGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
25017-25100 8.53e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 8.53e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25017 PGPPGTPFVTSVSKDQMLVQWHEPVNDGG-SKVIGYHLEQKEKNSiLWVKLNKIPiQDTKFKTTGLDEGLEYEFRVSAEN 25095
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  25096 IVGIG 25100
Cdd:smart00060    79 GAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24592-25292 8.56e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 77.74  E-value: 8.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24592 LSIDNCDRNDAGKYILKLENSSGSKSAFVTVKVLDTPGPPQNLAVKEVRK--DSVLLVWEPPIIDGGAKVKNYVIDKRES 24669
Cdd:COG3401      11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGlsSGGGLGTGGRAGTTSGVAAVAVAAAPPT 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24670 TRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEFGVGVPAETSDAVKASEPPSPPGKVTLTDVSQTSASlmwekpe 24749
Cdd:COG3401      91 ATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSV------- 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24750 hdGGSRILGYVVEMQPKGTEKWSVVAESKVCSAVVSGLSSGQEYQFRVKAYNEKGKSDPrvlgvpviakdltiqpsfklp 24829
Cdd:COG3401     164 --AGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP--------------------- 220
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24830 fntysvqagedlkieipvigrprpkiswvkdgeplrqttrvnveetatstilhikesskddFGKYSVTATNNAgtatenl 24909
Cdd:COG3401     221 -------------------------------------------------------------SNEVSVTTPTTP------- 232
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24910 svivlekPGPPVGpVKFDEVSADFVVISWEPPAYTGgcqISNYIVEKRDTTTTNWQMVsATVARTTIKVSKLKTGTEYQF 24989
Cdd:COG3401     233 -------PSAPTG-LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKV-ATVTTTSYTDTGLTNGTTYYY 300
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24990 RIFAENRYGKSTPlDSKPVVVQYPFKEPGPPGTPFVTSVSKDQMLVQWhEPVNDGGskVIGYHLEQKEKNSILWVKLNKi 25069
Cdd:COG3401     301 RVTAVDAAGNESA-PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAE- 375
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25070 PIQDTKFKTTGLDEGLEYEFRVSAENIVGI--GKPSKVSECYVARDPCDPPGRPEAIIITRNSVTLKWkkPTYDGGSKIT 25147
Cdd:COG3401     376 TVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA--AASAASNPGV 453
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25148 GYIVEKKDLPDGRWMKASFTNVVETEFTVTG-----LVEDQRYEFRVIARNAADNFSEPSESSGAITARDEIDAPNASLD 25222
Cdd:COG3401     454 SAAVLADGGDTGNAVPFTTTSSTVTATTTDTttanlSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGA 533
                           650       660       670       680       690       700       710
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25223 PKYrDVIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKSTLQKTTLTvKDCIRTDGGQYT 25292
Cdd:COG3401     534 SPV-TVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT-NDVAGVHGGTLL 601
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4770-4849 8.67e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.07  E-value: 8.67e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4770 TALAGQTVTLQAAVRGSEPISVMWMK-GQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEAGSQTSVGELI 4848
Cdd:smart00410     5 TVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84

                     .
gi 1958765569   4849 V 4849
Cdd:smart00410    85 V 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30743-30823 8.69e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 8.69e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30743 PEGPLEYDDIQTRSVRVSWRPPADDGG-ADILGYILERREVpKAAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFG 30821
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81

                     ..
gi 1958765569  30822 IS 30823
Cdd:smart00060    82 EG 83
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
15577-15888 8.74e-13

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 78.06  E-value: 8.74e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15577 EIREGADYKLRVSAVNaagegppGET----EPVTVAEPQEPPTVEL--DVSVKGGIQIMAGKTLRIPAVVTGRPVPTKVW 15650
Cdd:COG4733     407 DVLAGRRIGGRVSSVD-------GRVvtldRPVTMEAGDRYLRVRLpdGTSVARTVQSVAGRTLTVSTAYSETPEAGAVW 479
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15651 TIEEGELDKERVVIENVGtkseliiknalRKDHGRYVITATNSCGSKFAAARVEVFDVPGPVLDLKPVVTNRKMCLLN-- 15728
Cdd:COG4733     480 AFGPDELETQLFRVVSIE-----------ENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSESLSVVAqg 548
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15729 ---------WSDPADDGGSEITgfiiERKDAKmhTWRQPIETERSKCDITGLIEGQeYKFRVIAKNKFG-CGPPVEIGPI 15798
Cdd:COG4733     549 tavttltvsWDAPAGAVAYEVE----WRRDDG--NWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGvSSAWAASSET 621
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15799 LAVDPLGPPTSPERLTYTERTKStITLDWKEPRsdgGSPIQGYIIekRRHDKPDFE--RVNKRLCPTTSFLVDNLDEHQM 15876
Cdd:COG4733     622 TVTGKTAPPPAPTGLTATGGLGG-ITLSWSFPV---DADTLRTEI--RYSTTGDWAsaTVAQALYPGNTYTLAGLKAGQT 695
                           330
                    ....*....|..
gi 1958765569 15877 YEFRVKAVNDIG 15888
Cdd:COG4733     696 YYYRARAVDRSG 707
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18316-18400 8.78e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 8.78e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18316 PGPPINPKLKDKTKESADLVWTKPLSDGG-SPILGYVVEcQKPGTTQWDRINKDEliRQCAFRVPGLIEGNEYRFRIRAA 18394
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVE-YREEGSEWKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  18395 NIVGEG 18400
Cdd:smart00060    78 NGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
29966-30046 8.87e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.21  E-value: 8.87e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29966 KTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLA--NRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVL 30043
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 30044 VKV 30046
Cdd:pfam07679    88 LTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7576-7653 9.20e-13

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 68.75  E-value: 9.20e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7576 PPSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAAN 7653
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18514-18595 9.22e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 9.22e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18514 PGPCQNLKVSNVTKENCTISWENPL-DNGGSEITNFIVEYRKPNQKGWSIVASDVTKRLIKANLLANNEYYFRVCAENKV 18592
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  18593 GVG 18595
Cdd:smart00060    81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27578-27661 9.31e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 9.31e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27578 PGPPSIPEVTKITKNSMTVVWNRPTVDGG-SEINGYFLEKRDKKSlAWLKVlKETIRDTRQKVTGLTENSDYQYRVCAVN 27656
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  27657 AAGMG 27661
Cdd:smart00060    79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26198-26277 9.49e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.18  E-value: 9.49e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26198 DPPGQPEVTNITRKSVSLKWSKPRYDGGAK-ITGYIVERRElPDGRWLKCNfTNVQETYFEVTELTEDQRYEFRVFARNA 26276
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYRE-EGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     .
gi 1958765569  26277 A 26277
Cdd:smart00060    80 A 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
27975-28066 9.58e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 69.45  E-value: 9.58e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27975 PAPIRDLSMKDSTKTSVVLSWTKPDFDGGSiITDYLVERKGKGEQAWSHA--GISKTCEIEIGQLKEQSVLEFRVSARNE 28052
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1958765569 28053 KGQSDPVTIGPLTV 28066
Cdd:cd00063      80 GGESPPSESVTVTT 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
111-193 9.74e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.07  E-value: 9.74e-13
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    111 QSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAE-IQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTA 189
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569    190 DLLV 193
Cdd:smart00410    82 TLTV 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5696-5787 9.76e-13

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 69.15  E-value: 9.76e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5696 PPQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARND 5775
Cdd:cd20972       1 PPQFIQKLRSQEV-AEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  5776 AGTASCSIELKV 5787
Cdd:cd20972      80 VGSDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
25516-25601 9.88e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 9.88e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25516 GPPSNPKVTDTSRSSVSLAWNKPiYDGGAPVRGYVIELKEA-AADEWTTCTPPSGLqgKQFTVTKLKENTEYNFRICAFN 25594
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnSGEPWNEITVPGTT--TSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 25595 TEGVGEP 25601
Cdd:pfam00041    78 GGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
14101-14185 9.88e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 9.88e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14101 DPPENVKWRDRTANSIFLTWDPPKnDGGSRIKGYIVEKCPRGS-DKWVACGEPVPDTKMEVTGLEEGKWYAYRVKALNRQ 14179
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 14180 GASKPS 14185
Cdd:pfam00041    80 GEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
27792-27874 1.01e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.07  E-value: 1.01e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27792 SVIAKAGEDVQLLIPFKGRPPPTVTWRKD-EKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQpKSSTV 27870
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQgGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS-ASSGT 81

                     ....
gi 1958765569  27871 SVKV 27874
Cdd:smart00410    82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
7670-7759 1.02e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.21  E-value: 1.02e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7670 PSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTNDAG 7749
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  7750 SASCTTHLFV 7759
Cdd:pfam07679    81 EAEASAELTV 90
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
31769-32017 1.02e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 76.20  E-value: 1.02e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGT---DQVL-VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05626       9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDVlnrNQVAhVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGDM 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FER-INTSAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFG------------------ 31905
Cdd:cd05626      89 MSLlIRMEVFP--EVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDL--DGHIKLTDFGlctgfrwthnskyyqkgs 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31906 QARQ--LKPGD------NFRL----------------------LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSG 31955
Cdd:cd05626     165 HIRQdsMEPSDlwddvsNCRCgdrlktleqratkqhqrclahsLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVG 244
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31956 INPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLL--VKERKSRMTASEALKHPWL 32017
Cdd:cd05626     245 QPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCcsAEERLGRNGADDIKAHPFF 308
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6-97 1.04e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 69.37  E-value: 1.04e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPGVQISFS-DGRARLMIPAVTKANSGRYSLRATN 84
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESeYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569    85 GSGQATSTAELLV 97
Cdd:cd20951      81 IHGEASSSASVVV 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15097-15175 1.05e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 1.05e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15097 DVEVHNPTAKAMTITWKPPLYDGG-SKIMGYIIEKLAKGeDRWKRCNEHlVPVLTYTAKGLEEGKEYQFRVRAENAAGIG 15175
Cdd:smart00060     6 NLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
23753-23828 1.07e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.21  E-value: 1.07e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 23753 VQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIE 23828
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1801-1890 1.08e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 69.37  E-value: 1.08e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRV----RYDGIHYLDIVDCKSYDTGEVKVTAEN 1876
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKykieSEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  1877 PEGVTEHKVKLEIQ 1890
Cdd:cd20951      81 IHGEASSSASVVVE 94
fn3 pfam00041
Fibronectin type III domain;
17232-17315 1.10e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 1.10e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17232 PEDLEVKEVTKNTVTLTWNPPKyDGGSEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQ 17311
Cdd:pfam00041     3 PSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                    ....
gi 1958765569 17312 GKPS 17315
Cdd:pfam00041    82 GPPS 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7199-7277 1.12e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 68.75  E-value: 1.12e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7199 PPKFIKKLdTSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHN 7277
Cdd:pfam13927     1 KPVITVSP-SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8610-8687 1.19e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 68.36  E-value: 1.19e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8610 PPSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSN 8687
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
31766-31971 1.19e-12

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 73.89  E-value: 1.19e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31766 AEDLGRGEFGIVHRcvETSSKKTFMA-KFVKVKGTDQVLVK--KEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd05085       1 GELLGKGNFGEVYK--GTLKDKTPVAvKTCKEDLPQELKIKflSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPG--DNFRLLF 31920
Cdd:cd05085      79 DFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCL--VGENNALKISDFGMSRQEDDGvySSSGLKQ 156
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31921 TAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05085     157 IPIKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGMTNQQAREQV 208
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
16640-16725 1.20e-12

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 68.77  E-value: 1.20e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16640 VEEGTDVNIVAKIKGVPFPTLTWfkappKKPDSkePVVYDTHVNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTASK 16719
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTW-----SKDGQ--PLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSA 76

                    ....*.
gi 1958765569 16720 EMRLNV 16725
Cdd:cd05748      77 TINVKV 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5154-5222 1.21e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 68.12  E-value: 1.21e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5154 QLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTSI 5222
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
31759-32017 1.23e-12

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 75.27  E-value: 1.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMA-KFVKVKGTDQVLVKKEISILN-------IARHRNILYLhESFESME 31830
Cdd:cd14213      10 LRARYEIVDTLGEGAFGKVVECIDHKMGGMHVAvKIVKNVDRYREAARSEIQVLEhlnttdpNSTFRCVQML-EWFDHHG 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 ELVMIFEFIsGLDIFERINTSAF---ELNEREVVSYvrQVCEALEFLHSQNIGHFDIRPENIIY---------------- 31891
Cdd:cd14213      89 HVCIVFELL-GLSTYDFIKENSFlpfPIDHIRNMAY--QICKSVNFLHHNKLTHTDLKPENILFvqsdyvvkynpkmkrd 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31892 -QTRKNSIIKIIEFGQARQlkPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLV--YVL-------------LSG 31955
Cdd:cd14213     166 eRTLKNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieYYLgftvfqthdskehLAM 243
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31956 INPFLAETNQQMIENIMNAEY------TFDEEA------------FQEISL-------EAMDFIDRLLVKERKSRMTASE 32010
Cdd:cd14213     244 MERILGPLPKHMIQKTRKRKYfhhdqlDWDEHSsagryvrrrckpLKEFMLsqdvdheQLFDLIQKMLEYDPAKRITLDE 323

                    ....*..
gi 1958765569 32011 ALKHPWL 32017
Cdd:cd14213     324 ALKHPFF 330
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26099-26182 1.25e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 1.25e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26099 PGPPGTPKVVHATKSTMVVSWQVPVNDGG-SQVIGYHLEYKERSSiLWSKANkVLIADTQMKVSGLDEGLLYEYRVYAEN 26177
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  26178 IAGIG 26182
Cdd:smart00060    79 GAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29980-30579 1.25e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 77.35  E-value: 1.25e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29980 VSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDKVNRY----DAGKYTIEAENQSGKKSATVLVKVYDTPGPCPS 30055
Cdd:COG3401      62 SSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGgatnTGLTSSDEVPSPAVGTATTATAVAGGAATAGTY 141
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30056 VNVKEVSRDSVTITWEIPTIDGGAPVNNYIIEKREAAMRAFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENIYGIGEPC 30135
Cdd:COG3401     142 ALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPS 221
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30136 ETSDAVLVSEVPLVPTKLEVVDVTKSTVTLAWEKPlydGGSRLTGYVLEACKAGTERWMKVVTLKPTVLDHTviSLNEGE 30215
Cdd:COG3401     222 NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVATVTTTSYTDT--GLTNGT 296
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30216 QYLFRVRAQNEKGV-SEPREIVTpvtvqdlrvlptidlstmpqktihvpagrpielvipitgrppptaswffagsklres 30294
Cdd:COG3401     297 TYYYRVTAVDAAGNeSAPSNVVS--------------------------------------------------------- 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30295 erVTVEThtkvakltirettirdtgeymlelknvtgttsetikvvilDKPGPPIGpIKIDEVDATSVTISWEPPEldgGA 30374
Cdd:COG3401     320 --VTTDL----------------------------------------TPPAAPSG-LTATAVGSSSITLSWTASS---DA 353
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30375 PLSGYVVEQRDAHRPGWLPVSESVTRPTFKFTRLTEGNEYVFRVAATNRFGIGSYLQSEV-----IECRSSISIPGPPET 30449
Cdd:COG3401     354 DVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVsattaSAASGESLTASVDAV 433
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30450 LQIFDISRDGMTLTWYPPEDDGGSQVTGYIIERKEVRADRWVRVNKVPVTMTRYRSTGLIEGLEY-----EHRVTAINAR 30524
Cdd:COG3401     434 PLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGgsgasSVTNSVSVIG 513
                           570       580       590       600       610
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 30525 GTGKPSRPSKPTVAMDPIAPPGKPQNPRVTDTTRTSVSLAWSVPEDEGGSKVTGY 30579
Cdd:COG3401     514 ASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGS 568
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29452-29536 1.26e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 1.26e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29452 DPPGRPEVTDVTRSTVSLVWSAPMYDGGskvVGYIIERKPVSEVGDGRWLKCNyTIVSDNFFTVTALSEGDTYEFRVLAK 29531
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYRVEYREEGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*
gi 1958765569  29532 NAAGI 29536
Cdd:smart00060    78 NGAGE 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8797-8886 1.34e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 68.68  E-value: 1.34e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNN-VATLVFTQVDSNDSGEYICRAENSV 8875
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  8876 GEVSSSTFLTV 8886
Cdd:cd05744      81 GENSFNAELVV 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
9-97 1.36e-12

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 68.76  E-value: 1.36e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     9 TQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTlpGVQISF-SDGRARLMIPAVTKANSGRYSLRATNGSG 87
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESR--RFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLG 78
                            90
                    ....*....|
gi 1958765569    88 QATSTAELLV 97
Cdd:cd20973      79 EATCSAELTV 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29353-29436 1.36e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.41  E-value: 1.36e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29353 PSAPTRPEVYYVSANAMSIRWEEPYHDGG-SKIVGYWVEKKERNTiLWVKENkVPCLECNYKVTGLVEGLEYQFRTYALN 29431
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  29432 AAGVS 29436
Cdd:smart00060    79 GAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8234-8311 1.37e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 68.36  E-value: 1.37e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8234 PPVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATN 8311
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
29567-29649 1.38e-12

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 68.78  E-value: 1.38e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29567 DLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQY-TGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSV 29645
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLeQGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDV 88

                    ....
gi 1958765569 29646 MVKV 29649
Cdd:cd05891      89 TVSV 92
I-set pfam07679
Immunoglobulin I-set domain;
12175-12258 1.39e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.82  E-value: 1.39e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12175 PYFTVKLHDKTGVEKDEIILKCEVSKDVP--VKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC----DCG 12248
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSAG 80
                            90
                    ....*....|
gi 1958765569 12249 TDTTKANVTV 12258
Cdd:pfam07679    81 EAEASAELTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6-97 1.40e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 68.68  E-value: 1.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVIStstlPGVQISF---SDGRARLMIPAVTKANSGRYSLRA 82
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVR----PDSAHKMlvrENGRHSLIIEPVTKRDAGIYTCIA 76
                            90
                    ....*....|....*
gi 1958765569    83 TNGSGQATSTAELLV 97
Cdd:cd05744      77 RNRAGENSFNAELVV 91
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8892-8982 1.41e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 68.76  E-value: 1.41e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8892 PPSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPI 8971
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8972 GSASSSAKLIL 8982
Cdd:cd20972      81 GSDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
23547-23630 1.42e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 1.42e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23547 SPPVNLKVTEITKDSVSITWEPPlLDGGSKIKNYIVEKREATRKSYAAVVTNC-HKNSWKIDQLQEGCSYYFRVTAENEY 23625
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPgTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 23626 GIGLP 23630
Cdd:pfam00041    80 GEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30050-30132 1.43e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.41  E-value: 1.43e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30050 PGPCPSVNVKEVSRDSVTITWEIPTIDGG-APVNNYIIEKREAAMRaFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENI 30128
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  30129 YGIG 30132
Cdd:smart00060    80 AGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5978-6053 1.44e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 68.36  E-value: 1.44e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5978 QIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVEN 6053
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8047-8124 1.54e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 68.36  E-value: 1.54e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8047 PPFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASN 8124
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
31767-31971 1.59e-12

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 73.53  E-value: 1.59e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK-------KEISILNIARHRNILYLHESFESmEELVMIFEFI 31839
Cdd:cd05040       1 EKLGDGSFGVVRRGEWTTPSGKVIQVAVKCLKSDVLSQPnamddflKEVNAMHSLDHPNLIRLYGVVLS-SPLMMVTELA 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKnsIIKIIEFGQARQLKPGD----- 31914
Cdd:cd05040      80 PLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKD--KVKIGDFGLMRALPQNEdhyvm 157
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 --NFRLLFTapeYYAPEVHQHDVVSSATDMWSLG-TLVYVLLSGINPFLAETNQQMIENI 31971
Cdd:cd05040     158 qeHRKVPFA---WCAPESLKTRKFSHASDVWMFGvTLWEMFTYGEEPWLGLNGSQILEKI 214
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5883-5960 1.60e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.98  E-value: 1.60e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5883 PPSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKN 5960
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
9181-9258 1.62e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.98  E-value: 1.62e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9181 PPVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASN 9258
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
24034-24114 1.62e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.41  E-value: 1.62e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24034 DPPGTPEAIIVKRNEITLQWTKPVYDGG-SMITGYIVEKRDlPEGRWMKASfTNVIETQFTVSGLTEDQRYEFRVIAKNA 24112
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ..
gi 1958765569  24113 AG 24114
Cdd:smart00060    80 AG 81
fn3 pfam00041
Fibronectin type III domain;
15416-15500 1.64e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.21  E-value: 1.64e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15416 DAPDKPIVDDVTSNSMVVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKALLSSLKTKVDGLLEGLTYVFRVCAENAAG 15495
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....*
gi 1958765569 15496 PGKFS 15500
Cdd:pfam00041    81 EGPPS 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
33422-33505 1.68e-12

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 68.37  E-value: 1.68e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33422 LRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFI-LEILKTETSDGGLYSCTVANSAGSVSSS 33500
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCsLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                    ....*
gi 1958765569 33501 CKLTI 33505
Cdd:cd20973      84 AELTV 88
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
31758-32017 1.74e-12

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 74.71  E-value: 1.74e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEKYMIAEDLGRGEFGIVhrCVETSS---KKTFMAKFVKV--KGTDQVLVKKEISILNIARHRNILYLHE-----SFE 31827
Cdd:cd07858       2 EVDTKYVPIKPIGRGAYGIV--CSAKNSetnEKVAIKKIANAfdNRIDAKRTLREIKLLRHLDHENVIAIKDimpppHRE 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31828 SMEELVMIFEFISgLDIfERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQA 31907
Cdd:cd07858      80 AFNDVYIVYELMD-TDL-HQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNA--NCDLKICDFGLA 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLKPGDNFRLLFTAPE-YYAPEVHQH-DVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQE 31985
Cdd:cd07858     156 RTTSEKGDFMTEYVVTRwYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEEDLGF 235
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31986 ISLE---------------------------AMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07858     236 IRNEkarryirslpytprqsfarlfphanplAIDLLEKMLVFDPSKRITVEEALAHPYL 294
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7855-7945 1.75e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 68.38  E-value: 1.75e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7855 PPYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSV 7934
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  7935 GAVASSAVLVI 7945
Cdd:cd20972      81 GSDTTSAEIFV 91
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31763-32017 1.77e-12

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 73.45  E-value: 1.77e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFV-KVKGTD-----QVLVKKEISILNI--ARHRNILYLHESFESMEELVM 31834
Cdd:cd14102       2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVvKERVTEwgtlnGVMVPLEIVLLKKvgSGFRGVIKLLDWYERPDGFLI 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGL-DIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRkNSIIKIIEFGQARQLKpg 31913
Cdd:cd14102      82 VMERPEPVkDLFDFI-TEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLR-TGELKLIDFGSGALLK-- 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFRLLFTAPEYYAPE--VHQHDVVSSATDMWSLGTLVYVLLSGINPFlaetnqQMIENIMNAEYTFDeeafQEISLEAM 31991
Cdd:cd14102     158 DTVYTDFDGTRVYSPPewIRYHRYHGRSATVWSLGVLLYDMVCGDIPF------EQDEEILRGRLYFR----RRVSPECQ 227
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31992 DFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14102     228 QLIKWCLSLRPSDRPTLEQIFDHPWM 253
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6-84 1.86e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.98  E-value: 1.86e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPgvQISFSDGRARLMIPAVTKANSGRYSLRATN 84
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTR--SRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
31762-32018 1.86e-12

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 74.82  E-value: 1.86e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVET-SSKKTFMAKFVKV--KGTDQVLVKKEISILNIARHRNI-----LYLHESFESMEELV 31833
Cdd:cd07859       1 RYKIQEVIGKGSYGVVCSAIDThTGEKVAIKKINDVfeHVSDATRILREIKLLRLLRHPDIveikhIMLPPSRREFKDIY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGlDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQL--- 31910
Cdd:cd07859      81 VVFELMES-DLHQVIKAND-DLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNIL--ANADCKLKICDFGLARVAfnd 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNFRLLFTAPEYY-APEV--HQHDVVSSATDMWSLGTLVYVLLSG---------------INPFLAETNQQMIENIM 31972
Cdd:cd07859     157 TPTAIFWTDYVATRWYrAPELcgSFFSKYTPAIDIWSIGCIFAEVLTGkplfpgknvvhqldlITDLLGTPSPETISRVR 236
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31973 NAE-------------YTFDEEaFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd07859     237 NEKarrylssmrkkqpVPFSQK-FPNADPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
I-set pfam07679
Immunoglobulin I-set domain;
1682-1754 1.90e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.44  E-value: 1.90e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  1682 FECRLTpiGDPTMVVEWLHDGKPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:pfam07679    20 FTCTVT--GTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
31769-32018 1.90e-12

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 75.09  E-value: 1.90e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK---VKGTDQVL-VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05627      10 IGRGAFGEVRLVQKKDTGHIYAMKILRkadMLEKEQVAhIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDM 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK------------- 31911
Cdd:cd05627      90 MTLLMKKD-TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGH--VKLSDFGLCTGLKkahrtefyrnlth 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 --PGD-----------------NFRLL----FTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMI 31968
Cdd:cd05627     167 npPSDfsfqnmnskrkaetwkkNRRQLaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETY 246
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31969 ENIMNAEYTFDEEAFQEISLEAMDFIDRLLV--KERKSRMTASEALKHPWLK 32018
Cdd:cd05627     247 RKVMNWKETLVFPPEVPISEKAKDLILRFCTdaENRIGSNGVEEIKSHPFFE 298
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
900-989 1.91e-12

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 68.53  E-value: 1.91e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSI--DFQITFQSGIARLMIREAFAEDSGRFTCSAVNE 977
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569   978 AGTVSTSCYLAV 989
Cdd:cd20974      81 SGQATSTAELLV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3461-3550 1.92e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 68.60  E-value: 1.92e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSAD---YKFVFDGNNHSLIILFTRFQDEGEYTCMASN 3537
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569  3538 EYGRAVCSAHLKV 3550
Cdd:cd20951      81 IHGEASSSASVVV 93
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
32306-32396 1.92e-12

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 68.26  E-value: 1.92e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGP-HIEIVHEGLDYYALHIRDTLPEDTGYYRVTATNT 32384
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTdRISLYQDNCGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569 32385 AGSTSCQAHLQV 32396
Cdd:cd05892      81 AGVVSCNARLDV 92
I-set pfam07679
Immunoglobulin I-set domain;
5604-5693 1.93e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.44  E-value: 1.93e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5604 PYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSV-WKDDTSTiLELFSAKAADSGTYICQLSNDV 5682
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVtYEGGTYT-LTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|.
gi 1958765569  5683 GTTSSKATIFV 5693
Cdd:pfam07679    80 GEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33423-33505 1.95e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 68.30  E-value: 1.95e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33423 RDTTVSSDSVAKFVIKVTGEPQPTVTWTKDG-KAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSC 33501
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  33502 KLTI 33505
Cdd:smart00410    82 TLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8910-8977 2.03e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 67.74  E-value: 2.03e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8910 VVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPIGSASSS 8977
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7107-7183 2.07e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.98  E-value: 2.07e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATN 7183
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4393-4476 2.08e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.08e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4393 PKSLTTFVGKAAKFLCTVSGTPVIETIWQKDG-TALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKFGADICQ 4471
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   4472 AELTI 4476
Cdd:smart00410    81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
29855-29941 2.13e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.21  E-value: 2.13e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29855 GPPSAPRVVDTTKSSISLAWTKPMYDGGtDIIGYVLEMQEKDT---DQWCRVHTNTTirnnEFTVPDLKMGQKYSFRVAA 29931
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSgepWNEITVPGTTT----SVTLTGLKPGTEYEVRVQA 75
                            90
                    ....*....|
gi 1958765569 29932 VNAKGMSDYS 29941
Cdd:pfam00041    76 VNGGGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5891-5973 2.23e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.23e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5891 ENVTTVLKSSATFQSTVAGSPPISITWLKDD-QILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGVERCYA 5969
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   5970 FLLV 5973
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
24433-24517 2.31e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 2.31e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24433 GPPTNVHIVDTTKNSITLAWgKPIYDGGSDILGYVVEICKADEEE---WQIVTPQTglrvTRFEISKLIEHQEYKIRVCA 24509
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEpwnEITVPGTT----TSVTLTGLKPGTEYEVRVQA 75

                    ....*...
gi 1958765569 24510 LNKVGLGE 24517
Cdd:pfam00041    76 VNGGGEGP 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5525-5600 2.34e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.34e-12
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   5525 GSFIDLECIVAGSHPISIQWFKDDQE-ISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTV 5600
Cdd:smart00410     9 GESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7394-7477 2.37e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.37e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7394 SDVSTLIGDPVELQAVVEGFQPISVVWLKDKGEVIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKNDAGMRECSA 7473
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   7474 LLTV 7477
Cdd:smart00410    82 TLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4386-4463 2.37e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.59  E-value: 2.37e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4386 PPTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASN 4463
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
28480-28560 2.40e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 2.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDGVEI--ERRMNMEITDvlGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEIT 28557
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrsSDRFKVTYEG--GTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 28558 VKV 28560
Cdd:pfam07679    88 LTV 90
I-set pfam07679
Immunoglobulin I-set domain;
27382-27474 2.47e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 2.47e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27382 PVIDLPLEYTEVvkyRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRN 27461
Cdd:pfam07679     1 PKFTQKPKDVEV---QEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 27462 AMGSASATIRVQI 27474
Cdd:pfam07679    78 SAGEAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
33082-33162 2.47e-12

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 67.61  E-value: 2.47e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33082 ITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQFTLT 33161
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569 33162 V 33162
Cdd:cd05748      82 V 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8892-8969 2.49e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.59  E-value: 2.49e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8892 PPSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTN 8969
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
3461-3550 2.49e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 67.91  E-value: 2.49e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTP-SADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEY 3539
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  3540 GRAVCSAHLKV 3550
Cdd:cd05744      81 GENSFNAELVV 91
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16483-16967 2.52e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.19  E-value: 2.52e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16483 VVPDLISEQQYFFRVRAENRFGIGPPAETIQRTTARDPiypPDLPIKLKIGLITKNTVHLSWKPPKNDGgspVTHYIVEC 16562
Cdd:COG3401     195 GGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP---PSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYR 268
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16563 LAWDPTGKKKEAwrqcnrrDVEELEFTVEDLVEGGEYEFRVKAVNEAGV-SKPSATvgpVTVKdqtcppsielkefmeve 16641
Cdd:COG3401     269 SNSGDGPFTKVA-------TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNV---VSVT----------------- 321
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16642 egtdvnivakikgvpfptltwfkappkkpdskepvvydthvnkqvvddtcTLVIPqsrrsdtglysitavnnlgtaskem 16721
Cdd:COG3401     322 --------------------------------------------------TDLTP------------------------- 326
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16722 rlnvlgrPGPPVGpIKFESISADQMTLSWLPPKDDGgskITNYVIEKREANRKTWVRVSSEPKECMYTIPKLLEGHEYVF 16801
Cdd:COG3401     327 -------PAAPSG-LTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYY 395
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16802 RIMAQNKYGIgEPLDSEPETARNLFSVPGAPDKPTVSSVTRNSmTVNWEEPEYDGGSPVTGYWLEMKDTTSKRWKRVNRD 16881
Cdd:COG3401     396 KVTAVDAAGN-ESAPSEEVSATTASAASGESLTASVDAVPLTD-VAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTT 473
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16882 PIKAM--TLGVSYKVTGLIEGSDYQFRVYAINAAGVGPASLPSDPVTARDPVAPPGPPFPKVTDWTKSSVDLEWSPPLKD 16959
Cdd:COG3401     474 SSTVTatTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSL 553

                    ....*...
gi 1958765569 16960 GGSKITGY 16967
Cdd:COG3401     554 TTSASSSV 561
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
31803-32017 2.58e-12

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 73.51  E-value: 2.58e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31803 LVKKEISILNIARHRNIL-YLHESFESMEELVMIFEFI--SGLDIF-ERINT-------SAFELNEREVVSYVRQVCEAL 31871
Cdd:cd14011      48 LLKRGVKQLTRLRHPRILtVQHPLEESRESLAFATEPVfaSLANVLgERDNMpspppelQDYKLYDVEIKYGLLQISEAL 127
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31872 EFLH-SQNIGHFDIRPENIIyqTRKNSIIKIIEFGQA-------------RQLKPGDNFrLLFTAPEYYAPEVHQHDVVS 31937
Cdd:cd14011     128 SFLHnDVKLVHGNICPESVV--INSNGEWKLAGFDFCisseqatdqfpyfREYDPNLPP-LAQPNLNYLAPEYILSKTCD 204
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31938 SATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14011     205 PASDMFSLGVLIYAIYNkGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPF 284

                    .
gi 1958765569 32017 L 32017
Cdd:cd14011     285 F 285
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7300-7382 2.61e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 2.61e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7300 PPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQ-VRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCA 7378
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....
gi 1958765569   7379 CTVK 7382
Cdd:smart00410    81 TTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7293-7370 2.61e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.59  E-value: 2.61e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATN 7370
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
7765-7852 2.67e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 2.67e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7765 FVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEAGQD 7844
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*...
gi 1958765569  7845 ICEALVSV 7852
Cdd:pfam07679    83 EASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
26496-26581 2.67e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 2.67e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26496 SPPTSLEITSVTKDSMTLCWSRPEtDGGSDISGYIIERREKNSLRWMRVNKKPVYDLRVKSTGLREGCEYEYRVFAENAA 26575
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 26576 GLSLPS 26581
Cdd:pfam00041    80 GEGPPS 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
900-989 2.68e-12

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 67.80  E-value: 2.68e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSG-LKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSiDFQITFQSGiaRLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd20978       1 PKFIQKpEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGP-MERATVEDG--TLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd20978      78 GDIYTETLLHV 88
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
28318-28713 2.79e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.19  E-value: 2.79e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28318 VNTSPISGREYRATGLIEGLDYQFRVYAENSAGLSSPSDPSKFTLAVSPVDPPGTPDYIDVTRETITLKWNPPLRDGgsk 28397
Cdd:COG3401     184 SLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--- 260
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28398 IVAYSIEKRQGSD-RWVRCNFTDVSEcqYTVSGLSPGDRYEFRIIARNAVGTISPPSqssglimtrdenvpptvefgpey 28476
Cdd:COG3401     261 ATGYRVYRSNSGDgPFTKVATVTTTS--YTDTGLTNGTTYYYRVTAVDAAGNESAPS----------------------- 315
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28477 fdglviksgdslrikalvqgrpvprvtwfkdgveierrmnmeitdvlgstslfvrdatrdhrgvytveaknvsgstkAEI 28556
Cdd:COG3401     316 -----------------------------------------------------------------------------NVV 318
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28557 TVKVQDTPGKVVGPIRFTNITGEKMTLWWEAPLNdgcAPVTHYIIEKRETSRLAWALIEDHCEAQSYTAIKLITGNEYQF 28636
Cdd:COG3401     319 SVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD---ADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYY 395
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 28637 RVSAVNKFGvgrpLESDP--VVAQIQYTIPDAPGIPEPSNVTGNSITLTWTRPESDGGNEIQHYILERREKKSTRWVKV 28713
Cdd:COG3401     396 KVTAVDAAG----NESAPseEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPF 470
fn3 pfam00041
Fibronectin type III domain;
16731-16814 2.80e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 2.80e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16731 PPVGPIKFESISADQMTLSWLPPkDDGGSKITNYVIEKREANR-KTWVRVSSEPKECMYTIPKLLEGHEYVFRIMAQNKY 16809
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 16810 GIGEP 16814
Cdd:pfam00041    80 GEGPP 84
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
908-989 2.83e-12

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 67.92  E-value: 2.83e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   908 NVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGiARLMIREAFAEDSGRFTCSAVNEA-GTVSTSCY 986
Cdd:cd20970      11 TVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENG-TTLTIRNIRRSDMGIYLCIASNGVpGSVEKRIT 89

                    ...
gi 1958765569   987 LAV 989
Cdd:cd20970      90 LQV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7023-7099 2.93e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.53  E-value: 2.93e-12
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   7023 TVGLPVTLTCRLNGSAPIHVCWYRDG-VLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSTARLT 7099
Cdd:smart00410     7 KEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7107-7196 2.97e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 67.91  E-value: 2.97e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPH-LRILKVGKGDSGQYTCQATNDV 7185
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  7186 GKDMCSAQLSV 7196
Cdd:cd05744      81 GENSFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
4199-4286 3.03e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.67  E-value: 3.03e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4199 PTILKPLVDTISEKGDTVHLTSSISNAK--EVNWYFKGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNG 4276
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569  4277 KAMTSAKLTV 4286
Cdd:pfam07679    81 EAEASAELTV 90
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
31762-32017 3.10e-12

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 74.40  E-value: 3.10e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARH------RNILYLHESFESMEELVMI 31835
Cdd:cd14224      66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKqdkdntMNVIHMLESFTFRNHICMT 145
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISgLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQlkpgD 31914
Cdd:cd14224     146 FELLS-MNLYELIKKNKFQgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFGSSCY----E 220
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRlLFTAPE---YYAPEVHQHDVVSSATDMWSLGTLVYVLLSG---------------INPFLAETNQQMIENIMNAEY 31976
Cdd:cd14224     221 HQR-IYTYIQsrfYRAPEVILGARYGMPIDMWSFGCILAELLTGyplfpgedegdqlacMIELLGMPPQKLLETSKRAKN 299
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31977 TFDEEAFQEI----------------------------------SLEAM------DFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd14224     300 FISSKGYPRYctvttlpdgsvvlnggrsrrgkmrgppgskdwvtALKGCddplflDFLKRCLEWDPAARMTPSQALRHPW 379

                    .
gi 1958765569 32017 L 32017
Cdd:cd14224     380 L 380
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
28571-28656 3.24e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 3.24e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28571 IRFTNITGEKMTLWWEAPLNDGcAPVTHYIIEKRETSRLAWALIE-DHCEAQSYTAIKLITGNEYQFRVSAVNKFGVGRP 28649
Cdd:cd00063       7 LRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85

                    ....*..
gi 1958765569 28650 LESDPVV 28656
Cdd:cd00063      86 SESVTVT 92
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
31761-32026 3.27e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 73.49  E-value: 3.27e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV--LVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd07872       6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEY 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGlDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQAR-QLKPGDNFR 31917
Cdd:cd07872      86 LDK-DLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGE--LKLADFGLARaKSVPTKTYS 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 LLFTAPEYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEIS--------- 31987
Cdd:cd07872     163 NEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISsndefknyn 242
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31988 -----------------LEAMDFIDRLLVKERKSRMTASEALKHPWLKQRMDRVST 32026
Cdd:cd07872     243 fpkykpqplinhaprldTEGIELLTKFLQYESKKRISAEEAMKHAYFRSLGTRIHS 298
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
21587-21854 3.43e-12

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 76.14  E-value: 3.43e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRV-NVENTATST----ILNINEcvrSDSGAYPLTAKNTVGEVGD 21661
Cdd:COG4733     441 LRVRLPDGTSVARTVQSVAGRTLTVSTAYSETPEAGAVwAFGPDELETqlfrVVSIEE---NEDGTYTITAVQHAPEKYA 517
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21662 VITIQVHDIPGP--PTGPIKFDEVSSDF--------VTFSWEPPENDggvpiSNYVVEMRQtDSTTWVELATTvIRTTYK 21731
Cdd:COG4733     518 AIDAGAFDDVPPqwPPVNVTTSESLSVVaqgtavttLTVSWDAPAGA-----VAYEVEWRR-DDGNWVSVPRT-SGTSFE 590
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21732 ATRLTTGvEYQFRVKAQNRYGV-GPGITSASVVANypFKVPGPPGTPQVTAVTKD-SMTISWHEPLsdgGSPILGYHIER 21809
Cdd:COG4733     591 VPGIYAG-DYEVRVRAINALGVsSAWAASSETTVT--GKTAPPPAPTGLTATGGLgGITLSWSFPV---DADTLRTEIRY 664
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 21810 KERNGILWQTVSKALVPGNIFKSTGLTDGIAYEFRVIAENMAGKS 21854
Cdd:COG4733     665 STTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNV 709
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
31762-32018 3.46e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 76.31  E-value: 3.46e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKG-----TDQVLVkkEISILNIARHRNILYLHESF--ESMEELVM 31834
Cdd:PTZ00266     14 EYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGlkereKSQLVI--EVNVMRELKHKNIVRYIDRFlnKANQKLYI 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINT--SAF-ELNEREVVSYVRQVCEALEFLHSQNIG-------HFDIRPENIIYQT----------R 31894
Cdd:PTZ00266     92 LMEFCDAGDLSRNIQKcyKMFgKIEEHAIVDITRQLLHALAYCHNLKDGpngervlHRDLKPQNIFLSTgirhigkitaQ 171
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31895 KNS-----IIKIIEFGQARQLKPGDNFRLLFTAPEYYAPEVHQHDVVS--SATDMWSLGTLVYVLLSGINPFLAETN-QQ 31966
Cdd:PTZ00266    172 ANNlngrpIAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHETKSydDKSDMWALGCIIYELCSGKTPFHKANNfSQ 251
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31967 MIENIMNAEytfdEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:PTZ00266    252 LISELKRGP----DLPIKGKSKELNILIKNLLNLSAKERPSALQCLGYQIIK 299
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8518-8607 3.46e-12

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 67.42  E-value: 3.46e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRK-LKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAIsSGRKYQTTLTDNTcaLTVNMLEDADAGDYTCIATNVA 8596
Cdd:cd20978       1 PKFIQKpEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDGT--LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  8597 GSDECSAPLTV 8607
Cdd:cd20978      78 GDIYTETLLHV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5510-5587 3.47e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.21  E-value: 3.47e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5510 PPSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATN 5587
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
1516-1607 3.61e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.67  E-value: 3.61e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKN-SDIIVPHKYpRIRIEGtkGEAALKIDSTISQDSAWYTATAIN 1594
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDgQPLRSSDRF-KVTYEG--GTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569  1595 KAGRDTTRCKVNI 1607
Cdd:pfam07679    78 SAGEAEASAELTV 90
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
24824-24914 3.63e-12

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 67.76  E-value: 3.63e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTT--RVNVEETATSTILHIKESSKDDFGKYSVTATNN 24901
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 24902 AGTATENLSVIVL 24914
Cdd:cd20974      81 SGQATSTAELLVL 93
I-set pfam07679
Immunoglobulin I-set domain;
32886-32975 3.64e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.67  E-value: 3.64e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32886 PRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNYKG 32965
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 32966 EASDYATLDV 32975
Cdd:pfam07679    81 EAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
31235-31319 3.68e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 3.68e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31235 PDKPTGpIVIEALLKNSVVISWKAPADDGGSW-ITNYVVEKCEakEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQ 31313
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYRE--EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  31314 NTFGIS 31319
Cdd:smart00060    78 NGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
24307-24742 3.73e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.81  E-value: 3.73e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24307 AVNKYGVGEPLESAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWNRPDSDGGSEIIGYIVEKRDRSGIRWIkcNKRRIT 24386
Cdd:COG3401     113 SSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTS--LTVTST 190
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24387 DLRLRVTGLTEDHEYEFRVSAENAAGVGEPSPATVYYKACDPvfkPGPPTNVHIVDTTKNSITLAWGKPiydGGSDILGY 24466
Cdd:COG3401     191 TLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP---PSAPTGLTATADTPGSVTLSWDPV---TESDATGY 264
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24467 VVEICKADEEEWQIVTpqtGLRVTRFEISKLIEHQEYKIRVCALNKVGLGEAASVPGTVKPEdkleapeldldselrkgi 24546
Cdd:COG3401     265 RVYRSNSGDGPFTKVA---TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTD------------------ 323
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24547 vvraggsarihipfkgrPTPeitwskeegeftdkvqiekginftqlsidncdrndagkyilklenssgsksafvtvkvld 24626
Cdd:COG3401     324 -----------------LTP------------------------------------------------------------ 326
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24627 tPGPPQNLAVKEVRKDSVLLVWEPPiidGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENE 24706
Cdd:COG3401     327 -PAAPSGLTATAVGSSSITLSWTAS---SDADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDA 402
                           410       420       430
                    ....*....|....*....|....*....|....*..
gi 1958765569 24707 FGV-GVPAETSDAVKASEPPSPPGKVTLTDVSQTSAS 24742
Cdd:COG3401     403 AGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVA 439
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6735-6818 3.74e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.53  E-value: 3.74e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6735 PEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVK-GDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNNAGQASCT 6813
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   6814 TRLFV 6818
Cdd:smart00410    81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
11628-11719 3.83e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 3.83e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11628 KFVKEIKDIVLTEaesvGSSAIFECLVSPSTAIT-TWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRL 11706
Cdd:pfam07679     2 KFTQKPKDVEVQE----GESARFTCTVTGTPDPEvSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1958765569 11707 GNKEKTSTAKLIV 11719
Cdd:pfam07679    78 SAGEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
13065-13148 3.83e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 3.83e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13065 EFISKPQNLEILEGEKAEFVCTIS-KESFEVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVV----MVGA 13139
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSAGE 81

                    ....*....
gi 1958765569 13140 ARAAAHLTV 13148
Cdd:pfam07679    82 AEASAELTV 90
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
31761-32016 3.95e-12

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 72.95  E-value: 3.95e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL---VKKEISILNIARHRNILYLHESFESMEE-----L 31832
Cdd:cd07837       1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVpstALREVSLLQMLSQSIYIVRLLDVEHVEEngkplL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31833 VMIFEFISG-----LDIFERinTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsIIKIIEFGQA 31907
Cdd:cd07837      81 YLVFEYLDTdlkkfIDSYGR--GPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKG-LLKIADLGLG 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLK-PGDNFRLLFTAPEYYAPEV---HQHdvVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEE-- 31981
Cdd:cd07837     158 RAFTiPIKSYTHEIVTLWYRAPEVllgSTH--YSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEEvw 235
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31982 ----------------------AFQEISLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07837     236 pgvsklrdwheypqwkpqdlsrAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
I-set pfam07679
Immunoglobulin I-set domain;
17742-17818 4.02e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 4.02e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 17742 IKVGDTLRLSAIIKGVPFPKVTWKKEDREAPT--KAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSsdRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5603-5693 4.05e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 67.61  E-value: 4.05e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5603 PPYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSNDV 5682
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  5683 GTTSSKATIFV 5693
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8988-9065 4.05e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.21  E-value: 4.05e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8988 PPFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAIN 9065
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
20513-20584 4.06e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 4.06e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 20513 RLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKV 20584
Cdd:pfam07679    19 RFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
5514-5600 4.08e-12

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 67.21  E-value: 4.08e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5514 TKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSF-HDNTAFLEISQLEGTDSGTYTCSATNKAGHS 5592
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  5593 QCSGHLTV 5600
Cdd:cd20973      81 TCSAELTV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3206-3288 4.08e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.15  E-value: 4.08e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3206 QPVTVQSGKPARF-CAViAGRPQPKISWYKE-EQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTS 3283
Cdd:smart00410     2 PSVTVKEGESVTLsCEA-SGSPPPEVTWYKQgGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   3284 ASLSV 3288
Cdd:smart00410    81 TTLTV 85
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
31763-32017 4.21e-12

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 72.73  E-value: 4.21e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILN-IARHRNILYLHESFESM------EELVMI 31835
Cdd:cd06636      18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKkYSHHRNIATYYGAFIKKsppghdDQLWLV 97
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERI-NTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd06636      98 MEFCGAGSVTDLVkNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDRTV 175
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31915 NFRLLFTAPEYY-APEVHQHDVVSSAT-----DMWSLGTLVYVLLSGINPfLAETNQqmieniMNAEYTFDEEAFQEI-- 31986
Cdd:cd06636     176 GRRNTFIGTPYWmAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPP-LCDMHP------MRALFLIPRNPPPKLks 248
                           250       260       270
                    ....*....|....*....|....*....|....
gi 1958765569 31987 ---SLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06636     249 kkwSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5530-5595 4.39e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 66.58  E-value: 4.39e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5530 LECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHSQCS 5595
Cdd:cd00096       3 LTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
fn3 pfam00041
Fibronectin type III domain;
20689-20774 4.43e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.05  E-value: 4.43e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20689 DAPPPPNIVDVRHDSVSLTWTdPKKTGGSPITGYHIEFKERNS---LLWKRANKTPIRmkdFKVTGLTEGLEYEFRVMAI 20765
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSgepWNEITVPGTTTS---VTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 20766 NLAGVGKPS 20774
Cdd:pfam00041    77 NGGGEGPPS 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4948-5038 4.73e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 67.22  E-value: 4.73e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4948 APLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSV 5027
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  5028 GSKDSRGALIV 5038
Cdd:cd20972      81 GSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8617-8700 4.91e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.15  E-value: 4.91e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8617 PDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELV-PGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAGRASCT 8695
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   8696 TQLFV 8700
Cdd:smart00410    81 TTLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1258-1337 4.93e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 67.14  E-value: 4.93e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1258 ILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYV 1337
Cdd:cd05744      12 VQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
6915-7001 5.05e-12

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 67.03  E-value: 5.05e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEP-LEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEyRTYFTNNvaTLVFNKVGINDSGEYTCVAENSI 6993
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPME-RATVEDG--TLTIINVQPEDTGYYGCVATNEI 77

                    ....*...
gi 1958765569  6994 GTAASKTV 7001
Cdd:cd20978      78 GDIYTETL 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4967-5038 5.16e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.15  E-value: 5.16e-12
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569   4967 RLDCKIAGSLPMRVSWFKDG-KEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSRGALIV 5038
Cdd:smart00410    13 TLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
16011-16096 5.18e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.05  E-value: 5.18e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16011 SPPRNLAVTDIKAESCYLTWDAPLDnGGSEITHYIIDKRDAsRKKSEWEEVTNTAVERRYGIWKLIPNGQYEFRVRAVNK 16090
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPK-NSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 16091 YGTSDE 16096
Cdd:pfam00041    79 GGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
12087-12170 5.38e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 5.38e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12087 KFISPLEDQTVKEGQTATFVCELS-HEKMHVVWFKNDVKLHTTRTVLMSSEGKTYKLEIRETTLDDISQIKAQVKN---- 12161
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsage 81

                    ....*....
gi 1958765569 12162 LSSTANLKV 12170
Cdd:pfam07679    82 AEASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4949-5025 5.48e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 66.82  E-value: 5.48e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATN 5025
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4572-4663 5.64e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 67.22  E-value: 5.64e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4572 PPSFVKKVDpSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATND 4651
Cdd:cd20972       1 PPQFIQKLR-SQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  4652 AGSDSCSTEVVI 4663
Cdd:cd20972      80 VGSDTTSAEIFV 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6352-6429 5.64e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 66.43  E-value: 5.64e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6352 PPVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQN 6429
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
5423-5504 5.65e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 5.65e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5423 SIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKASI 5502
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569  5503 NV 5504
Cdd:pfam07679    89 TV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7028-7095 5.65e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 66.20  E-value: 5.65e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7028 VTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASST 7095
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
I-set pfam07679
Immunoglobulin I-set domain;
18430-18510 6.05e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 6.05e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18430 ITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVN 18509
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 18510 V 18510
Cdd:pfam07679    90 V 90
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
31769-31997 6.06e-12

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 73.53  E-value: 6.06e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK---VKGTDQV-LVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05628       9 IGRGAFGEVRLVQKKDTGHVYAMKILRkadMLEKEQVgHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDM 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK------------- 31911
Cdd:cd05628      89 MTLLMKKD-TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGH--VKLSDFGLCTGLKkahrtefyrnlnh 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 --PGD-----------------NFR-LLFTA---PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMI 31968
Cdd:cd05628     166 slPSDftfqnmnskrkaetwkrNRRqLAFSTvgtPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETY 245
                           250       260
                    ....*....|....*....|....*....
gi 1958765569 31969 ENIMNAEYTFDEEAFQEISLEAMDFIDRL 31997
Cdd:cd05628     246 KKVMNWKETLIFPPEVPISEKAKDLILRF 274
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
33416-33506 6.11e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 67.06  E-value: 6.11e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAI---AQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVAN 33492
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569 33493 SAGSVSSSCKLTIK 33506
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8234-8317 6.15e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 66.84  E-value: 6.15e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8234 PPVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDV 8313
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....
gi 1958765569  8314 GSDT 8317
Cdd:cd20972      81 GSDT 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
32201-32293 6.17e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 67.14  E-value: 6.17e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDDKKYTFESdkGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVREN--GRHSLIIEPVTKRDAGIYTCIARN 78
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:cd05744      79 RAGENSFNAELVV 91
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12985-13052 6.18e-12

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 66.50  E-value: 6.18e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 12985 EVSEGDTIKLVCEVSKPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCRLPSSR 13052
Cdd:cd20967       8 QVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEK 75
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
31767-32016 6.20e-12

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 72.15  E-value: 6.20e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKV----KGTDQVLVKkEISILNIARHRNILYLHESFESMEELVMIFEFIS-G 31841
Cdd:cd07860       6 EKIGEGTYGVVYKARNKLTGEVVALKKIRLdtetEGVPSTAIR-EISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHqD 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERInTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLK-PGDNFRLLF 31920
Cdd:cd07860      85 LKKFMDA-SALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINT--EGAIKLADFGLARAFGvPVRTYTHEV 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31921 TAPEYYAPEV-HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDE------------------- 31980
Cdd:cd07860     162 VTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEvvwpgvtsmpdykpsfpkw 241
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 31981 --EAFQEI----SLEAMDFIDRLLVKERKSRMTASEALKHPW 32016
Cdd:cd07860     242 arQDFSKVvpplDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
I-set pfam07679
Immunoglobulin I-set domain;
21983-22063 6.29e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 6.29e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21983 ITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNVK 22062
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 22063 V 22063
Cdd:pfam07679    90 V 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
19817-19897 6.46e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 66.76  E-value: 6.46e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDS-TPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  19896 KV 19897
Cdd:smart00410    84 TV 85
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
31804-32018 6.58e-12

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 73.53  E-value: 6.58e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31804 VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFD 31883
Cdd:cd05600      58 VLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGGDFRTLLNNSGI-LSEEHARFYIAEMFAAISSLHQLGYIHRD 136
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31884 IRPENIIYQtrKNSIIKIIEFGQAR-----------QLKPGDNFRLLFT---------------------------APEY 31925
Cdd:cd05600     137 LKPENFLID--SSGHIKLTDFGLASgtlspkkiesmKIRLEEVKNTAFLeltakerrniyramrkedqnyansvvgSPDY 214
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31926 YAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQ------EISLEAMDFIDRLLV 31999
Cdd:cd05600     215 MAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGSTPNETWANLYHWKKTLQRPVYTdpdlefNLSDEAWDLITKLIT 294
                           250       260
                    ....*....|....*....|
gi 1958765569 32000 kERKSRMTASEALK-HPWLK 32018
Cdd:cd05600     295 -DPQDRLQSPEQIKnHPFFK 313
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7594-7661 6.67e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 66.20  E-value: 6.67e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7594 VVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQDESS 7661
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
fn3 pfam00041
Fibronectin type III domain;
22465-22548 6.68e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.67  E-value: 6.68e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22465 GPPQNLKIKEVTKTSVTLTWEPPlLDGGSKIKNYIVEKRESTRKAYSTVATNC-HKTSWKIDQLQEGCSYYFRVLAENEY 22543
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPgTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 22544 GIGLP 22548
Cdd:pfam00041    80 GEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18522-18943 6.79e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 74.65  E-value: 6.79e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18522 VSNVTKENCTISWENPLDNGGSEITNFIVEYRKPNQKGWSIVASDVTKRLIkanllANNEYYFRVCAENKVGVGPTIETK 18601
Cdd:COG3401     150 VDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIE-----PGTTYYYRVAATDTGGESAPSNEV 224
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18602 TPILAINPidrPGEPENLHIADKGKTFVYLKWRRPDYDGGSpnlSYHVERRLKGSADWERVhkGSIKETHYMVDKCVENQ 18681
Cdd:COG3401     225 SVTTPTTP---PSAPTGLTATADTPGSVTLSWDPVTESDAT---GYRVYRSNSGDGPFTKV--ATVTTTSYTDTGLTNGT 296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18682 IYEFRVQTKNEGG-ESDWvrTEEVVVKEDLQKP--VLDLKlsgvLTVKAGDTIRLEagvrgkpfpevaWTK--DKDAT-- 18754
Cdd:COG3401     297 TYYYRVTAVDAAGnESAP--SNVVSVTTDLTPPaaPSGLT----ATAVGSSSITLS------------WTAssDADVTgy 358
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18755 DLTRSPR-----VKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAG-----SFVAYATV------NVLDKPGPVRNLKIA 18818
Cdd:COG3401     359 NVYRSTSgggtyTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesapSEEVSATTasaasgESLTASVDAVPLTDV 438
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18819 DVSSDRCTIRWDPpeddGGCEIQNYILEKCESkrmvWSTYSANVLTPGATVTRLIEGNEYIFRVRAENKIGTGPPTESKP 18898
Cdd:COG3401     439 AGATAAASAASNP----GVSAAVLADGGDTGN----AVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                           410       420       430       440
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 18899 VIAKTKYDRPGRPDPPEVTKVSKEemTVVWNAPEYDGGKSITGYY 18943
Cdd:COG3401     511 VIGASAAAAVGGAPDGTPNVTGAS--PVTVGASTGDVLITDLVSL 553
fn3 pfam00041
Fibronectin type III domain;
26888-26970 6.94e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.67  E-value: 6.94e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26888 SPPEKLGVTSVSKDSVSLSWLKPEhDGGSRILHYVVEALEKG-QKNWVKCAVVKTTHHV-VSGLREGHEYFFRVFAENQA 26965
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNsGEPWNEITVPGTTTSVtLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 26966 GLSDP 26970
Cdd:pfam00041    80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
17923-18005 7.22e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.67  E-value: 7.22e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17923 GPPKDLHHVDVDKTEVSLVWNKPDrDGGSPITGYLVEYQEEGAKDWIKFKTVKN--LECVVTGLQQGKTYRFRVKAENII 18000
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGttTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 18001 GLGLP 18005
Cdd:pfam00041    80 GEGPP 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
3461-3537 7.27e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 66.43  E-value: 7.27e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASN 3537
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5137-5219 7.94e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 66.75  E-value: 7.94e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5137 FTEKLEPSQLLKkGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAV-LRLTDVAIEDSGEYMCEAQNEAG 5215
Cdd:cd05744       3 FLQAPGDLEVQE-GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRAG 81

                    ....
gi 1958765569  5216 SDHC 5219
Cdd:cd05744      82 ENSF 85
fn3 pfam00041
Fibronectin type III domain;
25712-25795 8.11e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 8.11e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25712 SAPVNLTVREVKKDSVTLSWEPPLiDGGAKVTNYIVEKRETTRKAYA-TITNNCTKTTFKIENLQEGCSYYFRVLASNEY 25790
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 25791 GIGLP 25795
Cdd:pfam00041    80 GEGPP 84
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5510-5600 8.41e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 66.45  E-value: 8.41e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5510 PPSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKA 5589
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  5590 GHSQCSGHLTV 5600
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
33415-33492 8.42e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 66.05  E-value: 8.42e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 33415 KPVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVAN 33492
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7855-7946 8.68e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 66.68  E-value: 8.68e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7855 PPYFIEPLEH-VEAaiGEPTTLQCKVDGTPEIRISWYKEHTKLRSA---PAYKMQFKNNVASLVINKVDHSDVGEYTCKA 7930
Cdd:cd20951       1 PEFIIRLQSHtVWE--KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSsipGKYKIESEYGVHVLHIRRVTVEDSAVYSAVA 78
                            90
                    ....*....|....*.
gi 1958765569  7931 ENSVGAVASSAVLVIK 7946
Cdd:cd20951      79 KNIHGEASSSASVVVE 94
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
17839-18352 8.93e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 74.27  E-value: 8.93e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17839 YLTWKEPLDDGGSVVTNYVVERKDVATAQWSPLSTTSKKKSHMAKHLNEGNQYLFRVAAENQYGRGPFVETpkpIKALDP 17918
Cdd:COG3401     153 ANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNE---VSVTTP 229
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17919 LHPPGPPKDLHHVDVDKTEVSLVWNKPDRDGgspITGYLVEYQEEGAKDWIKFKTVKNLECVVTGLQQGKTYRFRVKAEN 17998
Cdd:COG3401     230 TTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVD 306
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17999 iiglglpdttipiecqekleppsveldvklieglvvkagttvrfpaiirgvpvptakwaTDGTEITtddhytvetdsFSS 18078
Cdd:COG3401     307 -----------------------------------------------------------AAGNESA-----------PSN 316
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18079 VLTIKnclrkdtgeyqltvsnaagtktvavhlTVLDVPGPPTGpINILDVTPEYMTISWQPPKDdggSPVINYIVEKQDT 18158
Cdd:COG3401     317 VVSVT---------------------------TDLTPPAAPSG-LTATAVGSSSITLSWTASSD---ADVTGYNVYRSTS 365
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18159 RKGTWGVVSAGSSKLKLKVPHLQKGCEYVFRVKAENKMGVGPPLDsiPTVAKHKFSPPSPPGKPVVTDITENAATVSWTL 18238
Cdd:COG3401     366 GGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPS--EEVSATTASAASGESLTASVDAVPLTDVAGATA 443
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18239 PKSDGGSPITGYYVERREITGKWV----RVNKTPIADLKFRVTGLYEGNTYEFRVFAENLAGLSNPSPSSDPIKACRPIK 18314
Cdd:COG3401     444 AASAASNPGVSAAVLADGGDTGNAvpftTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGA 523
                           490       500       510
                    ....*....|....*....|....*....|....*...
gi 1958765569 18315 PPGPPINPKLKDKTKESADLVWTKPLSDGGSPILGYVV 18352
Cdd:COG3401     524 PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSV 561
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
104-193 9.02e-12

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 66.37  E-value: 9.02e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQ-SSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSV 182
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRpDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569   183 GRATSTADLLV 193
Cdd:cd05744      81 GENSFNAELVV 91
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4386-4476 9.45e-12

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 66.45  E-value: 9.45e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4386 PPTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKF 4465
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  4466 GADICQAELTI 4476
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4479-4556 1.00e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 66.05  E-value: 1.00e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4479 KPHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASN 4556
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4497-4559 1.02e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.81  E-value: 1.02e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  4497 IHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAG 4559
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7200-7290 1.02e-11

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 66.26  E-value: 1.02e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDTSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESwKYNMSFVNSValLTINEASVEDTGDYICEAHNGV 7279
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGP-MERATVEDGT--LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  7280 GHASCSTALKV 7290
Cdd:cd20978      78 GDIYTETLLHV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8905-8981 1.03e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.03e-11
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   8905 TVGLPVVFECAVSGSEPISVSWYKDG-KPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPIGSASSSAKLI 8981
Cdd:smart00410     7 KEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4952-5038 1.06e-11

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 66.06  E-value: 1.06e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4952 TKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVE-GTASLEISRVDMNDAGNFTCRATNSVGSK 5030
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEdGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  5031 DSRGALIV 5038
Cdd:cd20973      81 TCSAELTV 88
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
31767-31975 1.07e-11

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 71.59  E-value: 1.07e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIV---HRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIAR----HRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05091      12 EELGEDRFGKVykgHLFGTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRsrlqHPNIVCLLGVVTKEQPMSMIFSYC 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERI---------------NTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEF 31904
Cdd:cd05091      92 SHGDLHEFLvmrsphsdvgstdddKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLN--VKISDL 169
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31905 GQARQLKPGDNFRLLFTAP---EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIMNAE 31975
Cdd:cd05091     170 GLFREVYAADYYKLMGNSLlpiRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMIRNRQ 244
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
32319-32396 1.08e-11

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 66.29  E-value: 1.08e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32319 EGQSVCFEIRVSGIPAPTLKWEKDGQPL--SLGPHIEIVHEGLDYYALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:cd20951      14 EKSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVV 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1801-1889 1.11e-11

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 66.37  E-value: 1.11e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFR--VRYDGIHYLDIVDCKSYDTGEVKVTAENPE 1878
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmlVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  1879 GVTEHKVKLEI 1889
Cdd:cd05744      81 GENSFNAELVV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32319-32396 1.16e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.16e-11
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  32319 EGQSVCFEIRVSGIPAPTLKWEKDG-QPLSLGPHIEIVHEGLDYYaLHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:smart00410     8 EGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTST-LTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9006-9074 1.19e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.43  E-value: 1.19e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9006 ADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEV-GKDSCTA 9074
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
31053-31121 1.22e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 65.66  E-value: 1.22e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31053 DVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATN 31121
Cdd:pfam13927    10 SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8428-8511 1.25e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.25e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8428 PESIKVTTGDTCTLECMVSGTPELSTKWFKDG-KELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCT 8506
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   8507 VSIQV 8511
Cdd:smart00410    81 TTLTV 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
23063-23145 1.30e-11

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 66.02  E-value: 1.30e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23063 DTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSST-ARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTV 23141
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATeGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 23142 NVKV 23145
Cdd:cd05894      83 FVKV 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1807-1889 1.32e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.32e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNG-QLIRKSKRFRVRYDG-IHYLDIVDCKSYDTGEVKVTAENPEGVTEHK 1884
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGsTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   1885 VKLEI 1889
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8054-8135 1.32e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.99  E-value: 1.32e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8054 PVSVDLALGESGSFKCHVTGTAPIKITWAKDNRE-IRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDSCS 8132
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ...
gi 1958765569   8133 AQL 8135
Cdd:smart00410    81 TTL 83
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
31763-32014 1.32e-11

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 70.83  E-value: 1.32e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK-GTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd06646      11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEpGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGG 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIfERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd06646      91 GSL-QDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLT--DNGDVKLADFGVAAKITATIAKRKSFI 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYY-APE---VHQHDVVSSATDMWSLGtlvyvlLSGINpfLAETNQQMIE-NIMNAEYTFDEEAFQEISLEAM----- 31991
Cdd:cd06646     168 GTPYWmAPEvaaVEKNGGYNQLCDIWAVG------ITAIE--LAELQPPMFDlHPMRALFLMSKSNFQPPKLKDKtkwss 239
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 31992 ---DFIDRLLVKERKSRMTASEALKH 32014
Cdd:cd06646     240 tfhNFVKISLTKNPKKRPTAERLLTH 265
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6072-6162 1.36e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 66.07  E-value: 1.36e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6072 PPSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVA 6151
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  6152 GDNACSGILTV 6162
Cdd:cd20972      81 GSDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
22563-22644 1.41e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.51  E-value: 1.41e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22563 PPGKITLMDVTRNSVSLSWEKPEhDGGSRILGYIVEMQSKGS-DKWATCATVKVT-EATITGLIQGEEYSFRVSAQNEKG 22640
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 22641 ISDP 22644
Cdd:pfam00041    81 EGPP 84
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5697-5788 1.45e-11

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 65.90  E-value: 1.45e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVLRnGQSTTFECQVTGTPEIRVSWYLDGNEIT---DLRRYGISFVDGLATFQISNARVENSGTYVCEAR 5773
Cdd:cd20951       1 PEFIIRLQSHTVWE-KSDAKLRVEVQGKPDPEVKWYKNGVPIDpssIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAK 79
                            90
                    ....*....|....*
gi 1958765569  5774 NDAGTASCSIELKVK 5788
Cdd:cd20951      80 NIHGEASSSASVVVE 94
fn3 pfam00041
Fibronectin type III domain;
24919-25002 1.51e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.51  E-value: 1.51e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24919 PPVGPVKFDEVSADFVVISWEPPAYTGGcQISNYIVEKRDTTTTN-WQMVSATVARTTIKVSKLKTGTEYQFRIFAENRY 24997
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 24998 GKSTP 25002
Cdd:pfam00041    80 GEGPP 84
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
31769-32017 1.52e-11

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 70.15  E-value: 1.52e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVkkeiSILNIARHRNILYLHESFESMEELVMIFEFISG-LDIFER 31847
Cdd:cd13976       1 LEPAEGSSLYRCVDIHTGEELVCKVVPVPECHAVLR----AYFRLPSHPNISGVHEVIAGETKAYVFFERDHGdLHSYVR 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31848 intSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKpGDNFRLL--FTAPEY 31925
Cdd:cd13976      77 ---SRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILE-GEDDSLSdkHGCPAY 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31926 YAPEV--HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRLLVKERK 32003
Cdd:cd13976     153 VSPEIlnSGATYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPE----TLSPRARCLIRSLLRREPS 228
                           250
                    ....*....|....
gi 1958765569 32004 SRMTASEALKHPWL 32017
Cdd:cd13976     229 ERLTAEDILLHPWL 242
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21185-21269 1.53e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.71  E-value: 1.53e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21185 PGPPSNAHVTDTTKKSASLAWGKPHYDGGL-EITGYVVEHQKVGDDaWIKDTTGTalRITQFVVPDLQTKEKYNFRISAV 21263
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSE-WKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  21264 NDAGVG 21269
Cdd:smart00060    78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5143-5225 1.60e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.60  E-value: 1.60e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5143 PSQLLKKGDATQLVCKVTGTPPIKITWFANDRE-LRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTS 5221
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   5222 IVIV 5225
Cdd:smart00410    82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
15920-16006 1.65e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 65.74  E-value: 1.65e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15920 IKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIeKPTDALNITKEEVSrseakTELSIPKAVREDKGTYTITASNRLGSVF 15999
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPL-RSSDRFKVTYEGGT-----YTLTISNVQPDDSGKYTCVATNSAGEAE 83

                    ....*..
gi 1958765569 16000 RNVHVEV 16006
Cdd:pfam07679    84 ASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
15097-15178 1.67e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.51  E-value: 1.67e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15097 DVEVHNPTAKAMTITWKPPLyDGGSKIMGYIIEKLAKG-EDRWKRCNEHLVPVlTYTAKGLEEGKEYQFRVRAENAAGIG 15175
Cdd:pfam00041     5 NLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNsGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    ...
gi 1958765569 15176 EPS 15178
Cdd:pfam00041    83 PPS 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4309-4377 1.67e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.04  E-value: 1.67e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4309 AKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEY-GSVSCTA 4377
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3478-3545 1.70e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.04  E-value: 1.70e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  3478 AKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYGRAVCS 3545
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
31769-32019 1.71e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 71.72  E-value: 1.71e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVK-------VKGTDQVL--------VKKEISILNIARHRNILYLHESFESMEELV 31833
Cdd:PTZ00024     17 LGEGTYGKVEKAYDTLTGKIVAIKKVKiieisndVTKDRQLVgmcgihftTLRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGlDIfERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQ---- 31909
Cdd:PTZ00024     97 LVMDIMAS-DL-KKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIF--INSKGICKIADFGLARRygyp 172
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LKPGDNFRLLFTAPE-----------YYAPE-VHQHDVVSSATDMWSLGTLVYVLLSGiNPFLAETNQ--QM--IENIMN 31973
Cdd:PTZ00024    173 PYSDTLSKDETMQRReemtskvvtlwYRAPElLMGAEKYHFAVDMWSVGCIFAELLTG-KPLFPGENEidQLgrIFELLG 251
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31974 A----------------EYTFD-----EEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:PTZ00024    252 TpnednwpqakklplytEFTPRkpkdlKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKS 318
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19604-19687 1.72e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.33  E-value: 1.72e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19604 PSEPKNARVTKVNKDCIFVAWDRPDSDGG-SPITGYLIERKERNSlLWVKANdTIVRSTEYPCAGLVEGLEYSFRIYALN 19682
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  19683 KAGSS 19687
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
25116-25202 1.81e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.51  E-value: 1.81e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25116 DPPGRPEAIIITRNSVTLKWKKPTyDGGSKITGYIVEKKDLPDGRWMKASFTNVVETEFTVTGLVEDQRYEFRVIARNAA 25195
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*..
gi 1958765569 25196 dNFSEPS 25202
Cdd:pfam00041    80 -GEGPPS 85
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
31758-32022 1.82e-11

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 71.91  E-value: 1.82e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31758 ELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK---EISILNIARHRNILYLHESF---ESMEE 31831
Cdd:cd07880      12 EVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRayrELRLLKHMKHENVIGLLDVFtpdLSLDR 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 -----LVMIFefiSGLDIFERINTSafELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIiyQTRKNSIIKIIEFGQ 31906
Cdd:cd07880      92 fhdfyLVMPF---MGTDLGKLMKHE--KLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNL--AVNEDCELKILDFGL 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARQlkpGDNFRLLFTAPEYY-APEVHQHDVVSSAT-DMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQ 31984
Cdd:cd07880     165 ARQ---TDSEMTGYVVTRWYrAPEVILNWMHYTQTvDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQ 241
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31985 EISLE---------------------------AMDFIDRLLVKERKSRMTASEALKHPWLKQRMD 32022
Cdd:cd07880     242 KLQSEdaknyvkklprfrkkdfrsllpnanplAVNVLEKMLVLDAESRITAAEALAHPYFEEFHD 306
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6370-6432 1.82e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.04  E-value: 1.82e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  6370 VSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVG 6432
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6635-6712 1.86e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 65.28  E-value: 1.86e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6635 PPSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAAN 6712
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5041-5118 1.89e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 65.28  E-value: 1.89e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5041 PPSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSN 5118
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4573-4663 1.99e-11

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 65.59  E-value: 1.99e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4573 PSFVKKVDpSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAI-LDITDVKVDDSGTYSCEATND 4651
Cdd:cd05744       1 PHFLQAPG-DLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569  4652 AGSDSCSTEVVI 4663
Cdd:cd05744      80 AGENSFNAELVV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
30147-30230 1.99e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.33  E-value: 1.99e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30147 PLVPTKLEVVDVTKSTVTLAWEKPLYDGG-SRLTGYVLEACKAGtERWmKVVTLKPTVLDHTVISLNEGEQYLFRVRAQN 30225
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEW-KEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  30226 EKGVS 30230
Cdd:smart00060    79 GAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5143-5212 2.09e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 64.89  E-value: 2.09e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5143 PSQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQN 5212
Cdd:pfam13927     9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
14597-14681 2.09e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.09e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14597 SPPRWLEVINITKNTADLKWTVPEkDGGSPITNYIVEKRDVRRKGWQTVDTTVKDTK-CTVTPLTEGSLYVFRVAAENAI 14675
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 14676 GQSDYT 14681
Cdd:pfam00041    80 GEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
2843-2926 2.13e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 65.36  E-value: 2.13e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2843 HITKTMRNIEVPETKAASFECEVSHFNVPS-MWLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVC----GN 2917
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEvSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2918 DQVSATLTV 2926
Cdd:pfam07679    82 AEASAELTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
32312-32396 2.20e-11

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 65.29  E-value: 2.20e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32312 LANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDYYALHIRDTLPEDTGYYRVTATNTAGSTSCQ 32391
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                    ....*
gi 1958765569 32392 AHLQV 32396
Cdd:cd20973      84 AELTV 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5697-5787 2.22e-11

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 65.11  E-value: 2.22e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDlRRYGISFVDGlaTFQISNARVENSGTYVCEARNDA 5776
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG-PMERATVEDG--TLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  5777 GTASCSIELKV 5787
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3203-3288 2.25e-11

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 65.29  E-value: 2.25e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3203 QELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLI-EAFPEDAAVYTCEAKNDYGVAT 3281
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIIsDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569  3282 TSASLSV 3288
Cdd:cd20973      82 CSAELTV 88
fn3 pfam00041
Fibronectin type III domain;
21381-21465 2.26e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.26e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21381 GPVLNLRPTDITKDSVTLHWDLPLiDGGSRITNYIVEKREATRKSYS-TVTTKCHKCTYKVTGLTEGCEYFFRVMAENEY 21459
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 21460 GIGEPT 21465
Cdd:pfam00041    80 GEGPPS 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6259-6350 2.30e-11

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 65.52  E-value: 2.30e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASD---KYQMTFIDSVAVMQMNSLGTEDSGDFICEAQ 6335
Cdd:cd20951       1 PEFIIRLQ-SHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAK 79
                            90
                    ....*....|....*
gi 1958765569  6336 NPAGSTSCSTKVIVK 6350
Cdd:cd20951      80 NIHGEASSSASVVVE 94
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5696-5787 2.30e-11

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 65.35  E-value: 2.30e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5696 PPQFIKKPsPVLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEIT-DLRRYGISfvDGLATFQISNARVENSGTYVCEARN 5774
Cdd:cd20976       1 APSFSSVP-KDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQyAADRSTCE--AGVGELHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|...
gi 1958765569  5775 DAGTASCSIELKV 5787
Cdd:cd20976      78 AAGQVSCSAWVTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8235-8325 2.32e-11

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 65.52  E-value: 2.32e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRS---GKKYKIMSENLLTSIHILNVDTADIGEYQCKATN 8311
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  8312 DVGSDTCVGSVTLK 8325
Cdd:cd20951      81 IHGEASSSASVVVE 94
fn3 pfam00041
Fibronectin type III domain;
24332-24417 2.35e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.35e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24332 GPPKSLEVTNIAKDSMTVCWNRPDsDGGSEIIGYIVEKRD-RSGIRWIKCNKRRITDlRLRVTGLTEDHEYEFRVSAENA 24410
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPkNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 24411 AGVGEPS 24417
Cdd:pfam00041    79 GGEGPPS 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2044-2128 2.38e-11

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 65.29  E-value: 2.38e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2044 IQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIAGETSSH 2123
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                    ....*
gi 1958765569  2124 AFLLV 2128
Cdd:cd20973      84 AELTV 88
fn3 pfam00041
Fibronectin type III domain;
28270-28355 2.47e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.47e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28270 GPPGKPVIYNVTSDGMSLTWDAPVyDGGSEVTGFHVEKKERNSI-LWQRVNTSPISgREYRATGLIEGLDYQFRVYAENS 28348
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGePWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 28349 AGLSSPS 28355
Cdd:pfam00041    79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27878-27960 2.51e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.94  E-value: 2.51e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27878 PAACQKLQVKHVSLGTVTLLWDPPLIDGG-SPIINYVIEKRDaTKRTWSIVSHKCSGTSFKVMDLSEKTPFFFRVLAENE 27956
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1958765569  27957 IGIG 27960
Cdd:smart00060    80 AGEG 83
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6914-6998 2.58e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 65.30  E-value: 2.58e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6914 PPYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSI 6993
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....*
gi 1958765569  6994 GTAAS 6998
Cdd:cd20972      81 GSDTT 85
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
31805-32017 2.58e-11

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 69.69  E-value: 2.58e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31805 KKEISILNIARHRNILYLHESFESMEELVMIFEFISGlDIFERINtSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDI 31884
Cdd:cd14023      33 DKIRPYIQLPSHRNITGIVEVILGDTKAYVFFEKDFG-DMHSYVR-SCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDL 110
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31885 RPENIIYQTRKNSIIKIIEFGQARQLKPGDN-FRLLFTAPEYYAPEVHQHDVVSS--ATDMWSLGTLVYVLLSGINPFLA 31961
Cdd:cd14023     111 KLRKFVFSDEERTQLRLESLEDTHIMKGEDDaLSDKHGCPAYVSPEILNTTGTYSgkSADVWSLGVMLYTLLVGRYPFHD 190
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31962 ETNQQMIENIMNAEYTFDEEafqeISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14023     191 SDPSALFSKIRRGQFCIPDH----VSPKARCLIRSLLRREPSERLTAPEILLHPWF 242
fn3 pfam00041
Fibronectin type III domain;
23836-23918 2.61e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 2.61e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23836 DPPKGpVKFDEVSAESITLSWNPPLYTGGcQITNYIVQKRDT-TTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENR 23914
Cdd:pfam00041     1 SAPSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....
gi 1958765569 23915 YGQS 23918
Cdd:pfam00041    79 GGEG 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1800-1876 2.66e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 64.51  E-value: 2.66e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1800 KPDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSK-RFRVRYDGIHYLDIVDCKSYDTGEVKVTAEN 1876
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGStRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27182-27265 2.67e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.94  E-value: 2.67e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27182 PGPPSTPWVSNVTRESITVGWHEPVS-NGGSAVIGYHLEMKDRNSiLWQKANKmIIRTTHFKVTTISAGLIYEFRVYAEN 27260
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDdGITGYIVGYRVEYREEGS-EWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  27261 AAGIG 27265
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
21479-21560 2.67e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.74  E-value: 2.67e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21479 PPDSLNIMDITKNTVSLAWPKPRhDGGSKITGYVIEAQRKGS-DQWTHISTVKGL-ECVVRNLTEGEEYTFQVMAVNSAG 21556
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 21557 RSAP 21560
Cdd:pfam00041    81 EGPP 84
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
15-97 2.80e-11

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 64.53  E-value: 2.80e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    15 VVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLpgVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATSTAE 94
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGR--VQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    ...
gi 1958765569    95 LLV 97
Cdd:cd05748      80 VKV 82
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
31769-32018 2.98e-11

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 71.62  E-value: 2.98e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGT---DQVL-VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05625       9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVllrNQVAhVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FER-INTSAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENII--------------------------YQT---- 31893
Cdd:cd05625      89 MSLlIRMGVFP--EDLARFYIAELTCAVESVHKMGFIHRDIKPDNILidrdghikltdfglctgfrwthdskyYQSgdhl 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31894 RKNSIIKIIEFGQARQLKPGDNFR----------------LLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGIN 31957
Cdd:cd05625     167 RQDSMDFSNEWGDPENCRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQP 246
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31958 PFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFIDRLL--VKERKSRMTASEALKHPWLK 32018
Cdd:cd05625     247 PFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCrgPEDRLGKNGADEIKAHPFFK 309
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
24832-24913 2.98e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 64.83  E-value: 2.98e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24832 TYSVQAGEDLKIEIPVIGRPRPKISWVKDG-EPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLS 24910
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  24911 VIV 24913
Cdd:smart00410    83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
21772-21857 3.03e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.74  E-value: 3.03e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21772 GPPGTPQVTAVTKDSMTISWHEPlSDGGSPILGYHIERKERNGI-LWQTVSkalVPGNI--FKSTGLTDGIAYEFRVIAE 21848
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGePWNEIT---VPGTTtsVTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 21849 NMAGKSKPS 21857
Cdd:pfam00041    77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
2407-2490 3.08e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.97  E-value: 3.08e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2407 VITPLKDVNVIEGTKAVLECKVS---VPDVTsvkWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYKL----MV 2479
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTgtpDPEVS---WFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSA 79
                            90
                    ....*....|.
gi 1958765569  2480 GRVETSCNLSV 2490
Cdd:pfam07679    80 GEAEASAELTV 90
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7856-7945 3.10e-11

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 64.72  E-value: 3.10e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAI-GEPTTLQCKVDGTPEIRISWYKEHTKLrSAPAYKMQFKNNvaSLVINKVDHSDVGEYTCKAENSV 7934
Cdd:cd20978       1 PKFIQKPEKNVVVKgGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDG--TLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  7935 GAVASSAVLVI 7945
Cdd:cd20978      78 GDIYTETLLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8252-8314 3.18e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 64.27  E-value: 3.18e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8252 VHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVG 8314
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32209-32293 3.20e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 64.83  E-value: 3.20e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  32209 NKTAYVGENVRFGVTITVHPEPRVTWYKsgQKIKPGDDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARNKHGEDSCK 32288
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYK--QGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  32289 AKLTV 32293
Cdd:smart00410    81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
30445-30530 3.37e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.74  E-value: 3.37e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30445 GPPETLQIFDISRDGMTLTWYPPEDdGGSQVTGYIIERKEVRA-DRWVRVNKVPVTmTRYRSTGLIEGLEYEHRVTAINA 30523
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSgEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 30524 RGTGKPS 30530
Cdd:pfam00041    79 GGEGPPS 85
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1038-1128 3.60e-11

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 64.73  E-value: 3.60e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|.
gi 1958765569  1118 HGETSASASLL 1128
Cdd:cd05893      81 QGRISCTGRLM 91
I-set pfam07679
Immunoglobulin I-set domain;
21587-21667 3.60e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.59  E-value: 3.60e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITIQ 21666
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 21667 V 21667
Cdd:pfam07679    90 V 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27478-27561 3.61e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.56  E-value: 3.61e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27478 PGPPGGpIEFKTVTAEKITLLWRPPADDGGAK-ITHYIVEKRETSRVvWSMVAENLEECIITTTKIIKGNEYIFRVRAVN 27556
Cdd:smart00060     1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  27557 KYGIG 27561
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
19010-19100 3.64e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 3.64e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19010 GPPTNFKVVDTTKNSITLAWgKPVYDGGAPIIGYVVEMRPKiadaSPDEGWKRCNAAAQlvRMEFTVTSLDENQEYEFRV 19089
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPK----NSGEPWNEITVPGT--TTSVTLTGLKPGTEYEVRV 73
                            90
                    ....*....|.
gi 1958765569 19090 CAQNQVGIGRP 19100
Cdd:pfam00041    74 QAVNGGGEGPP 84
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
31768-32019 3.68e-11

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 70.16  E-value: 3.68e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31768 DLGRGEFGIVHRcVETSSKKTFMAK---FVKVKGTDQVLVKKEISILNIARHRNILYLHESF-ESMEELVMIFEFiSGLD 31843
Cdd:cd06620      12 DLGAGNGGSVSK-VLHIPTGTIMAKkviHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFlNENNNIIICMEY-MDCG 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAFELNErEVVSYVR-QVCEALEFLHSQ-NIGHFDIRPENIIYQTRKNsiIKIIEFGQARQL--KPGDNFRLL 31919
Cdd:cd06620      90 SLDKILKKKGPFPE-EVLGKIAvAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQ--IKLCDFGVSGELinSIADTFVGT 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTapeYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFlAETNQ------------QMIENIMN-------AEYTFDE 31980
Cdd:cd06620     167 ST---YMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF-AGSNDdddgyngpmgilDLLQRIVNeppprlpKDRIFPK 242
                           250       260       270
                    ....*....|....*....|....*....|....*....
gi 1958765569 31981 eafqeislEAMDFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd06620     243 --------DLRDFVDRCLLKDPRERPSPQLLLDHDPFIQ 273
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
26441-26778 3.70e-11

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 73.06  E-value: 3.70e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26441 AWTICEAELRTTSCKVTKLLKGNEYIFRVTGV----NKYgvgEPLESVAVKALDPFTTPSPPTSLEITSVTKD-----SM 26511
Cdd:COG4733     478 VWAFGPDELETQLFRVVSIEENEDGTYTITAVqhapEKY---AAIDAGAFDDVPPQWPPVNVTTSESLSVVAQgtavtTL 554
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26512 TLCWSRPETDggsdiSGYIIERReKNSLRWmrVNKKPVYDLRVKSTGLREGcEYEYRVFAENAAGLSLPSDTSPLVRAed 26591
Cdd:COG4733     555 TVSWDAPAGA-----VAYEVEWR-RDDGNW--VSVPRTSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETTV-- 623
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26592 pVFLPSPPSKPK--IVDSGKTTITIGWVkplFDGGAPITGYTVEYkkSEETDW---KVAIQSFRGTEYTMSGLTTGAEYV 26666
Cdd:COG4733     624 -TGKTAPPPAPTglTATGGLGGITLSWS---FPVDADTLRTEIRY--STTGDWasaTVAQALYPGNTYTLAGLKAGQTYY 697
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26667 FRVRSLNKVGasDPSDITDPQVAKEREEEPAFDVDSEMRKTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYID 26746
Cdd:COG4733     698 YRARAVDRSG--NVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGV 775
                           330       340       350
                    ....*....|....*....|....*....|..
gi 1958765569 26747 STDSRTSLTIENANRNDSGKYTLTIQNVLSAA 26778
Cdd:COG4733     776 ATAAAIGAEARVAATVAESATAAAATGTAADA 807
I-set pfam07679
Immunoglobulin I-set domain;
28085-28154 3.82e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.59  E-value: 3.82e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28085 ISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDNAV 28154
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7969-8036 3.83e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.89  E-value: 3.83e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7969 VAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLGTASSS 8036
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
31767-32036 3.85e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 69.91  E-value: 3.85e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIFEFISG--L 31842
Cdd:cd06619       7 EILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQkqIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGgsL 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFElneREVVSYVRqvceALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFTA 31922
Cdd:cd06619      87 DVYRKIPEHVLG---RIAVAVVK----GLTYLWSLKILHRDVKPSNMLVNTRGQ--VKLCDFGVSTQLVNSIAKTYVGTN 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PeYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLA-ETNQQMIENIMNAEYTFDEEA----FQEISLEAMDFIDRL 31997
Cdd:cd06619     158 A-YMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQiQKNQGSLMPLQLLQCIVDEDPpvlpVGQFSEKFVHFITQC 236
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|...
gi 1958765569 31998 LVKERKSRMTASEALKHPWLKQ----RMDRVSTKVIRTLRHRR 32036
Cdd:cd06619     237 MRKQPKERPAPENLMDHPFIVQyndgNAEVVSMWVCRALEERR 279
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
33075-33163 3.89e-11

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 64.75  E-value: 3.89e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33075 ILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVV---STSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTD 33151
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|..
gi 1958765569 33152 GKQEAQFTLTVQ 33163
Cdd:cd20951      83 GEASSSASVVVE 94
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9003-9078 3.93e-11

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 64.82  E-value: 3.93e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  9003 GESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAH-LTIVKVDKGDSGQYTCYAINEVGKDSCTAQLNI 9078
Cdd:cd05744      15 GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9292-9380 4.05e-11

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 64.75  E-value: 4.05e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKG--KWRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKH 9369
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNgvPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|.
gi 1958765569  9370 GEIESNVNLQV 9380
Cdd:cd20951      83 GEASSSASVVV 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9199-9266 4.22e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.89  E-value: 4.22e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9199 LQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSDTSK 9266
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31239-31663 4.31e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 72.34  E-value: 4.31e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31239 TGPIVIEALLKNSVVISWKAPADDGGSWITNYVVEKCEAKEGAEWQLVSSAISVTTCRIV---------NLTENAGYYFR 31309
Cdd:COG3401     129 TAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTsttlvdgggDIEPGTTYYYR 208
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31310 VSAQNTFGISEPLEVASVVIIKSPfekPSVPGKPTITAVTKDSCVVAWKPPASDGgakIRNYYLEKREKKQNKWIAVTTe 31389
Cdd:COG3401     209 VAATDTGGESAPSNEVSVTTPTTP---PSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT- 281
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31390 eIRETVFSVQNLIEGLEYEFRVKCENLGG-ESEWSETSEpVTPKSDVPiQAPhfkeelRNLNVRYQSNATLVckvtghpk 31468
Cdd:COG3401     282 -VTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVS-VTTDLTPP-AAP------SGLTATAVGSSSIT-------- 344
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31469 piVKWyrqGKEIIADGLKYRVQ--EFKGGYHQLIIASV-----TDDDAT-----VYQVRATNQGGSVSGTAS----LEVE 31532
Cdd:COG3401     345 --LSW---TASSDADVTGYNVYrsTSGGGTYTKIAETVtttsyTDTGLTpgttyYYKVTAVDAAGNESAPSEevsaTTAS 419
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31533 VPAKIHLPKTLEGMGAVHALRGEVVSIKIpfSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNGVERKDAGFYV 31612
Cdd:COG3401     420 AASGESLTASVDAVPLTDVAGATAAASAA--SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31613 vcakNRFGIDQKTVELDVADVPDPPRGVKVSDVSRDSVNLTWTEPASDGGS 31663
Cdd:COG3401     498 ----GGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
31053-31132 4.37e-11

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 64.45  E-value: 4.37e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31053 DVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQ-SRKYKMSSDGRthTLTVMTEEQEDEGVYTCVATNEV-GEVETSS 31130
Cdd:cd20970      11 TVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEfNTRYIVRENGT--TLTIRNIRRSDMGIYLCIASNGVpGSVEKRI 88

                    ..
gi 1958765569 31131 KL 31132
Cdd:cd20970      89 TL 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7293-7376 4.45e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 64.53  E-value: 4.45e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....
gi 1958765569  7373 GSDT 7376
Cdd:cd20972      81 GSDT 84
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
19817-19897 4.45e-11

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 64.48  E-value: 4.45e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEG-VKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGrVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 19896 KV 19897
Cdd:cd05894      85 KV 86
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
31767-31961 4.47e-11

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 69.54  E-value: 4.47e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVH-RCVETSSKKTfmAKFVKVK----GTDQVLV---KKEISILNIARHRNILYLHESFESMEE--LVMIF 31836
Cdd:cd05080      10 RDLGEGHFGKVSlYCYDPTNDGT--GEMVAVKalkaDCGPQHRsgwKQEIDILKTLYHENIVKYKGCCSEQGGksLQLIM 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFI---SGLDIFERINtsafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPG 31913
Cdd:cd05080      88 EYVplgSLRDYLPKHS-----IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLD--NDRLVKIGDFGLAKAVPEG 160
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31914 DNFRLLFTAPE----YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLA 31961
Cdd:cd05080     161 HEYYRVREDGDspvfWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQS 212
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5041-5131 4.54e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 64.53  E-value: 4.54e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5041 PPSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVA 5120
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  5121 GSVECSANLFV 5131
Cdd:cd20972      81 GSDTTSAEIFV 91
I-set pfam07679
Immunoglobulin I-set domain;
26706-26786 4.55e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.59  E-value: 4.55e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26706 KTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAY--IDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTFV 26783
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRfkVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 26784 VKV 26786
Cdd:pfam07679    88 LTV 90
fn3 pfam00041
Fibronectin type III domain;
17426-17509 4.56e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 4.56e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17426 PPVGPVVFDEVTKEYMVISWKPPlDDGGSEITNYIIEKKELGK-DIWMPVTSASAKTTCKVPKLLEGKDYIFRIHAENLY 17504
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 17505 GISDP 17509
Cdd:pfam00041    80 GEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1264-1327 4.57e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.89  E-value: 4.57e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  1264 VTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFlQDGRASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRS-ELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
33697-33786 4.57e-11

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 64.68  E-value: 4.57e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33697 APSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFR 33776
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82
                            90
                    ....*....|
gi 1958765569 33777 GQCSATASLT 33786
Cdd:cd05747      83 GKQEAQFTLT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8335-8418 4.63e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 64.06  E-value: 4.63e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8335 SDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIVRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKNDAGVQECYA 8414
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   8415 TLSV 8418
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
31635-31718 4.69e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 4.69e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31635 DPPRGVKVSDVSRDSVNLTWTEPaSDGGSKVTNYIVEKCAT---TAERWLRVGqARETRYTVVNLFGKTSYQFRVIAENK 31711
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnsgEPWNEITVP-GTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 31712 FGLSKPS 31718
Cdd:pfam00041    79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
17128-17211 4.83e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.17  E-value: 4.83e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17128 PGPVGIPFLSDNlTNDSCKLTWFSPEDDGG-SPITNYVIQKREADRRaWTPVTYTVTRQNATVQGLIQGKSYFFRIAAEN 17206
Cdd:smart00060     1 PSPPSNLRVTDV-TSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  17207 SIGMG 17211
Cdd:smart00060    79 GAGEG 83
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4572-4654 5.13e-11

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 64.50  E-value: 5.13e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4572 PPSFVKKVdPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMS-FANSEAI----LDITDVKVDDSGTYSC 4646
Cdd:cd20956       1 APVLLETF-SEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGdYVTSDGDvvsyVNISSVRVEDGGEYTC 79

                    ....*...
gi 1958765569  4647 EATNDAGS 4654
Cdd:cd20956      80 TATNDVGS 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8162-8218 5.13e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.50  E-value: 5.13e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8162 ECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:cd00096       4 TCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60
fn3 pfam00041
Fibronectin type III domain;
22168-22253 5.17e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 5.17e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22168 DPPKNPEVTTITKDSMVVCWGHPDsDGGSEIINYIVERRDK-AGQRWVKCNKKAlTDLRFKVSGLTEGHEYEFRIMAENA 22246
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnSGEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 22247 AGVSAPS 22253
Cdd:pfam00041    79 GGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
30150-30232 5.23e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 5.23e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30150 PTKLEVVDVTKSTVTLAWEKPLyDGGSRLTGYVLEACKAGTERWMKVVTLKPTVLDHTVISLNEGEQYLFRVRAQNEKGV 30229
Cdd:pfam00041     3 PSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                    ...
gi 1958765569 30230 SEP 30232
Cdd:pfam00041    82 GPP 84
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
31769-32018 5.27e-11

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 69.39  E-value: 5.27e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKF-----VKVKGTDQVLVKKEISILNIARHRN---ILYLHESFESMEELVMIFEFIS 31840
Cdd:cd05606       2 IGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGETLALNERIMLSLVSTGGDcpfIVCMTYAFQTPDKLCFILDLMN 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQA---RQLKPGDNFr 31917
Cdd:cd05606      82 GGDLHYHLSQHGV-FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLD--EHGHVRISDLGLAcdfSKKKPHASV- 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31918 llfTAPEYYAPEVHQHDVV-SSATDMWSLGTLVYVLLSGINPFLAETNQQMIEnIMNAEYTFDEEAFQEISLEAMDFIDR 31996
Cdd:cd05606     158 ---GTHGYMAPEVLQKGVAyDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHE-IDRMTLTMNVELPDSFSPELKSLLEG 233
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31997 LLVKERKSRM-----TASEALKHPWLK 32018
Cdd:cd05606     234 LLQRDVSKRLgclgrGATEVKEHPFFK 260
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
31769-31960 5.40e-11

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 69.18  E-value: 5.40e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRC--------VETSSKKTFMAK--------FVKVKGTDQV----LVKKEISILNIARHRNILYLHESFES 31828
Cdd:cd14000       2 LGDGGFGSVYRAsykgepvaVKIFNKHTSSNFanvpadtmLRHLRATDAMknfrLLRQELTVLSHLHHPSIVYLLGIGIH 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31829 MEELVMIFEFISGLDIFERINTSAF-ELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQT--RKNSI-IKIIEF 31904
Cdd:cd14000      82 PLMLVLELAPLGSLDHLLQQDSRSFaSLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlyPNSAIiIKIADY 161
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31905 GQARQLKPgDNFRLLFTAPEYYAPEVHQHDVV-SSATDMWSLGTLVYVLLSGINPFL 31960
Cdd:cd14000     162 GISRQCCR-MGAKGSEGTPGFRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGAPMV 217
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5901-5966 5.44e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.50  E-value: 5.44e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5901 ATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGVER 5966
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8066-8133 5.55e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.50  E-value: 5.55e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8066 SFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASN-VAGKDSCSA 8133
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
33697-33787 5.57e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 64.14  E-value: 5.57e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33697 APSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFR 33776
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569 33777 GQCSATASLTV 33787
Cdd:cd20972      81 GSDTTSAEIFV 91
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
31753-31965 5.58e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 70.50  E-value: 5.58e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31753 HSKTKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNI-----ARHRNILYLHESFE 31827
Cdd:cd14228       7 HEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRlssenADEYNFVRSYECFQ 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31828 SMEELVMIFEFISGlDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIEF 31904
Cdd:cd14228      87 HKNHTCLVFEMLEQ-NLYDFLKQNKFSpLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdPVRQPYRVKVIDF 165
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31905 GQARQLKPGDNFRLLfTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSG--INPFLAETNQ 31965
Cdd:cd14228     166 GSASHVSKAVCSTYL-QSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGwpLYPGASEYDQ 227
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
31769-31959 5.61e-11

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 70.45  E-value: 5.61e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVK----GTDQVLVKKEISILNIA-RHRNILYLHESFESMEELVMIFEFISGLD 31843
Cdd:cd05618      28 IGRGSYAKVLLVRLKKTERIYAMKVVKKElvndDEDIDWVQTEKHVFEQAsNHPFLVGLHSCFQTESRLFFVIEYVNGGD 107
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ-LKPGDNFRLLFTA 31922
Cdd:cd05618     108 LMFHMQRQR-KLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH--IKLTDYGMCKEgLRPGDTTSTFCGT 184
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958765569 31923 PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd05618     185 PNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
21870-21950 5.65e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.79  E-value: 5.65e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21870 DPPGKPVPLNITRHTVALKWAKPEYTGGFK-ITSYVVEKRDlPNGRWLKANFSNIlENEFTVSGLTEDAAYEFRVIAKNA 21948
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYRE-EGSEWKEVNVTPS-STSYTLTGLKPGTEYEFRVRAVNG 79

                     ..
gi 1958765569  21949 AG 21950
Cdd:smart00060    80 AG 81
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7010-7098 5.68e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 64.14  E-value: 5.68e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7010 PPSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPL 7089
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....*....
gi 1958765569  7090 GTASSTARL 7098
Cdd:cd20972      81 GSDTTSAEI 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6072-6149 5.70e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 63.74  E-value: 5.70e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6072 PPSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSN 6149
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
18723-18805 6.20e-11

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 64.09  E-value: 6.20e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18723 LTVKAGDTIRLEAGVRGKPFPEVAWTKDkDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAGSFVAYAT 18802
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRG-DKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                    ...
gi 1958765569 18803 VNV 18805
Cdd:cd05894      84 VKV 86
fn3 pfam00041
Fibronectin type III domain;
27579-27664 6.29e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 6.29e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27579 GPPSIPEVTKITKNSMTVVWNRPTvDGGSEINGYFLEKRDKKSLAWLKVLKETIRDTRQKVTGLTENSDYQYRVCAVNAA 27658
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 27659 GMGPFS 27664
Cdd:pfam00041    80 GEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
15521-15599 6.35e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 6.35e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15521 RVADTSSTTIELEWEPPaFNGGGEIMGYFVDKQLVGTNEWSRctEKMVK--VRQFTVKEIREGADYKLRVSAVNAAGEGP 15598
Cdd:pfam00041     7 TVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWN--EITVPgtTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83

                    .
gi 1958765569 15599 P 15599
Cdd:pfam00041    84 P 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
19417-19500 6.45e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.68  E-value: 6.45e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19417 PEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVT-SSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQK 19495
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  19496 IKVTV 19500
Cdd:smart00410    81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
22952-23038 6.48e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 6.48e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22952 DPPGRPEAIIVTRNSVTLQWKKPTyDGGSKITGYVVEKKELPDGRWMKASFTNIIDTQFEVTGLIEDHRYEFRVIARNAA 23031
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*..
gi 1958765569 23032 GvFSEPS 23038
Cdd:pfam00041    80 G-EGPPS 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7124-7186 6.55e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.50  E-value: 6.55e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  7124 ADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVG 7186
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
31769-31959 6.56e-11

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 69.76  E-value: 6.56e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVK----GTDQVLVKKEISILNIA-RHRNILYLHESFESMEELVMIFEFISGLD 31843
Cdd:cd05588       3 IGRGSYAKVLMVELKKTKRIYAMKVIKKElvndDEDIDWVQTEKHVFETAsNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ-LKPGDNFRLLFTA 31922
Cdd:cd05588      83 LMFHMQRQR-RLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGH--IKLTDYGMCKEgLRPGDTTSTFCGT 159
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958765569 31923 PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd05588     160 PNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7311-7373 6.62e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.50  E-value: 6.62e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  7311 VILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVG 7373
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
13648-13903 6.62e-11

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 71.90  E-value: 6.62e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13648 WVLVTDRADSCEFTVTGLQKGGvEYLFRVSARNRVGtgepvETDSPVEARSKYDVPGPPLNVTIT-----DVNRFG---- 13718
Cdd:COG4733     479 WAFGPDELETQLFRVVSIEENE-DGTYTITAVQHAP-----EKYAAIDAGAFDDVPPQWPPVNVTtseslSVVAQGtavt 552
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13719 -VSLTWEPPEYDggaeiTNYVIELRdKTSIRWDTAMtvRAEDLSATVTDVVEGQeYSFRVRAQNRIGVGKPSAATPFVKV 13797
Cdd:COG4733     553 tLTVSWDAPAGA-----VAYEVEWR-RDDGNWVSVP--RTSGTSFEVPGIYAGD-YEVRVRAINALGVSSAWAASSETTV 623
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13798 ADPIERPSPPVNLSASeQTQSSVQLTWEPPLkdgGSPILGYIIERQEEGKDNWIRCNMKPVPELTYKVTGLQKGNKYLYR 13877
Cdd:COG4733     624 TGKTAPPPAPTGLTAT-GGLGGITLSWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYR 699
                           250       260
                    ....*....|....*....|....*.
gi 1958765569 13878 VSAENAAGVSDPSEILGPLTADDASV 13903
Cdd:COG4733     700 ARAVDRSGNVSAWWVSGQASADAAGI 725
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
31448-31531 6.72e-11

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 64.07  E-value: 6.72e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31448 NLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEFKggyHQLIIASVTDDDATVYQVRATNQ-GGSVSGT 31526
Cdd:cd20970      11 TVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENG---TTLTIRNIRRSDMGIYLCIASNGvPGSVEKR 87

                    ....*
gi 1958765569 31527 ASLEV 31531
Cdd:cd20970      88 ITLQV 92
fn3 pfam00041
Fibronectin type III domain;
18117-18201 6.73e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 6.73e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18117 GPPTGPiNILDVTPEYMTISWQPPkDDGGSPVINYIVEKQDTRKGTWGV-VSAGSSKLKLKVPHLQKGCEYVFRVKAENK 18195
Cdd:pfam00041     1 SAPSNL-TVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 18196 MGVGPP 18201
Cdd:pfam00041    79 GGEGPP 84
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
24831-24913 6.77e-11

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 63.71  E-value: 6.77e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24831 NTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTT-RVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENL 24909
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 24910 SVIV 24913
Cdd:cd05894      83 FVKV 86
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
31760-32017 6.82e-11

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 69.34  E-value: 6.82e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYmiaEDLGRGEFGIVHRCVETSSKKTFMAKFVKVK---GTDQVLVKkEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd07869       7 YEKL---EKLGEGSYATVYKGKSKVNGKLVALKVIRLQeeeGTPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTLVF 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISgLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQAR-QLKPGDN 31915
Cdd:cd07869      83 EYVH-TDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGE--LKLADFGLARaKSVPSHT 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31916 FRLLFTAPEYYAPEVHQHDV-VSSATDMWSLGTLVYVLLSGINPFLAETN-QQMIENIMNAEYTFDE------------- 31980
Cdd:cd07869     160 YSNEVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGVAAFPGMKDiQDQLERIFLVLGTPNEdtwpgvhslphfk 239
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31981 -------------EAFQEISL--EAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07869     240 perftlyspknlrQAWNKLSYvnHAEDLASKLLQCFPKNRLSAQAALSHEYF 291
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
31757-31954 6.93e-11

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 69.15  E-value: 6.93e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31757 KELYEKYMiaEDLGRGEFGIVHRC----VETSSKKTFMAKFVKVKGTDQVL-VKKEISILN------IARHRNILYlhes 31825
Cdd:cd05081       2 EERHLKYI--SQLGKGNFGSVELCrydpLGDNTGALVAVKQLQHSGPDQQRdFQREIQILKalhsdfIVKYRGVSY---- 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31826 FESMEELVMIFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFG 31905
Cdd:cd05081      76 GPGRRSLRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAH--VKIADFG 153
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31906 QARQLkPGDNFRLLFTAPE-----YYAPEVHQHDVVSSATDMWSLGTLVYVLLS 31954
Cdd:cd05081     154 LAKLL-PLDKDYYVVREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
fn3 pfam00041
Fibronectin type III domain;
16535-16615 6.93e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 6.93e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16535 ITKNTVHLSWKPPKnDGGSPVTHYIVEClaWDPTGKKKEAWRqcnRRDVEELEFTVEDLVEGGEYEFRVKAVNEAGVSKP 16614
Cdd:pfam00041    11 VTSTSLTVSWTPPP-DGNGPITGYEVEY--RPKNSGEPWNEI---TVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84

                    .
gi 1958765569 16615 S 16615
Cdd:pfam00041    85 S 85
I-set pfam07679
Immunoglobulin I-set domain;
12711-12782 7.05e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 7.05e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12711 LRPLKDVTVTAGETATFDCELS-YEDIPVEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAK 12782
Cdd:pfam07679     4 TQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT 76
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
33423-33505 7.06e-11

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 63.79  E-value: 7.06e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33423 RDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKA---IAQSSKYKLSNDKEEFIleILKTETSDGGLYSCTVANSAGSVSS 33499
Cdd:cd05763       7 HDITIRAGSTARLECAATGHPTPQIAWQKDGGTdfpAARERRMHVMPEDDVFF--IVDVKIEDTGVYSCTAQNSAGSISA 84

                    ....*.
gi 1958765569 33500 SCKLTI 33505
Cdd:cd05763      85 NATLTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7951-8041 7.18e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 63.76  E-value: 7.18e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7951 PPSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPL 8030
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8031 GTASSSAKLIL 8041
Cdd:cd20972      81 GSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6085-6162 7.39e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.68  E-value: 7.39e-11
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569   6085 VLGSSIHMECKVSGSLPINAQWFKDG-KEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAGDNACSGILTV 6162
Cdd:smart00410     7 KEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
31440-31531 7.40e-11

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 64.05  E-value: 7.40e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEfKGGYHQLIIASVTDDDATVYQVRATNQ 31519
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVR-ENGRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569 31520 GGSVSGTASLEV 31531
Cdd:cd05744      80 AGENSFNAELVV 91
fn3 pfam00041
Fibronectin type III domain;
20986-21069 7.42e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 7.42e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20986 GPPGPIEISNVSAEKATLTWTPPlEDGGSPIKAYVLEKRETSRL-LWTVVSEDIQACRHVVTKLIQGNEYLFRVSAVNHY 21064
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 21065 GKGEP 21069
Cdd:pfam00041    80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
26198-26284 7.50e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 7.50e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26198 DPPGQPEVTNITRKSVSLKWSKPRyDGGAKITGYIVERRELPDGRWLKcNFTNV-QETYFEVTELTEDQRYEFRVFARNA 26276
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWN-EITVPgTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*...
gi 1958765569 26277 AdSVSEPS 26284
Cdd:pfam00041    79 G-GEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
21186-21271 7.50e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 7.50e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21186 GPPSNAHVTDTTKKSASLAWGKPHYDGGlEITGYVVEHQKVGD-DAWI-KDTTGTAlriTQFVVPDLQTKEKYNFRISAV 21263
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSgEPWNeITVPGTT---TSVTLTGLKPGTEYEVRVQAV 76

                    ....*...
gi 1958765569 21264 NDAGVGEP 21271
Cdd:pfam00041    77 NGGGEGPP 84
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
18723-18806 7.79e-11

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 63.79  E-value: 7.79e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18723 LTVKAGDTIRLEAGVRGKPFPEVAWTKDkDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAGSFVAYAT 18802
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKD-GGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANAT 87

                    ....
gi 1958765569 18803 VNVL 18806
Cdd:cd05763      88 LTVL 91
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
31768-32030 7.94e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 69.30  E-value: 7.94e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31768 DLGRGEFGIVHRCVETSS-------KKTFMAKFVKVKGTDqvlVKKEISILNIARHRNILYLHESF--ESMEELVMIFEF 31838
Cdd:cd06633      28 EIGHGSFGAVYFATNSHTnevvaikKMSYSGKQTNEKWQD---IIKEVKFLQQLKHPNTIEYKGCYlkDHTAWLVMEYCL 104
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFErinTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFrl 31918
Cdd:cd06633     105 GSASDLLE---VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT--EPGQVKLADFGSASIASPANSF-- 177
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 lFTAPEYYAPEV------HQHDvvsSATDMWSLGtlvyvlLSGINpfLAETNQQMIE-NIMNAEYTF---DEEAFQ--EI 31986
Cdd:cd06633     178 -VGTPYWMAPEVilamdeGQYD---GKVDIWSLG------ITCIE--LAERKPPLFNmNAMSALYHIaqnDSPTLQsnEW 245
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 31987 SLEAMDFIDRLLVKERKSRMTASEALKHPWL-KQRMDRVSTKVIR 32030
Cdd:cd06633     246 TDSFRGFVDYCLQKIPQERPSSAELLRHDFVrRERPPRVLIDLIQ 290
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5603-5680 8.02e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 63.35  E-value: 8.02e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5603 PPYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSN 5680
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
30346-30427 8.11e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 8.11e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30346 PPIGPIKIDEVDATSVTISWEPPElDGGAPLSGYVVEQRDAHRPG-WLPVSESVTRPTFKFTRLTEGNEYVFRVAATNRF 30424
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ...
gi 1958765569 30425 GIG 30427
Cdd:pfam00041    80 GEG 82
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
31763-32015 8.19e-11

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 68.10  E-value: 8.19e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVH--RCVETSSK---KTFMAKFvkvkgTDQVLVKKEI----SILNIARHRNILYLHESFESMEELV 31833
Cdd:cd14050       3 FTILSKLGEGSFGEVFkvRSREDGKLyavKRSRSRF-----RGEKDRKRKLeeveRHEKLGEHPNCVRFIKAWEEKGILY 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEF--ISGLDIFERINtsafELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLK 31911
Cdd:cd14050      78 IQTELcdTSLQQYCEETH----SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS--KDGVCKLGDFGLVVELD 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 PGDNFRLLFTAPEYYAPEVHQhDVVSSATDMWSLGtlVYVLLSGIN---PFLAETNQQMIENIMNAEYTfdeeafQEISL 31988
Cdd:cd14050     152 KEDIHDAQEGDPRYMAPELLQ-GSFTKAADIFSLG--ITILELACNlelPSGGDGWHQLRQGYLPEEFT------AGLSP 222
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31989 EAMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd14050     223 ELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
31762-32017 8.26e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 69.53  E-value: 8.26e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARH--------RNILYLHESFESMEE-- 31831
Cdd:cd14136      11 RYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREadpkdpgrEHVVQLLDDFKHTGPng 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 --LVMIFEFI--SGLDIFERINTSAFELNEreVVSYVRQVCEALEFLHSQ-NIGHFDIRPENIIYqTRKNSIIKIIEFGQ 31906
Cdd:cd14136      91 thVCMVFEVLgpNLLKLIKRYNYRGIPLPL--VKKIARQVLQGLDYLHTKcGIIHTDIKPENVLL-CISKIEVKIADLGN 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 A----RQlkpgdnfrllFTAP----EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGinPFLAETNQ------------Q 31966
Cdd:cd14136     168 AcwtdKH----------FTEDiqtrQYRSPEVILGAGYGTPADIWSTACMAFELATG--DYLFDPHSgedysrdedhlaL 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31967 MIE--------------------------------------NIMNAEYTFDEEAFQEISleamDFIDRLLVKERKSRMTA 32008
Cdd:cd14136     236 IIEllgriprsiilsgkysreffnrkgelrhisklkpwpleDVLVEKYKWSKEEAKEFA----SFLLPMLEYDPEKRATA 311

                    ....*....
gi 1958765569 32009 SEALKHPWL 32017
Cdd:cd14136     312 AQCLQHPWL 320
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
3198-3275 8.26e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 63.35  E-value: 8.26e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  3198 PPQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKN 3275
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
31761-31978 8.33e-11

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 68.85  E-value: 8.33e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYmIAEdlgrGEFGIVH--RCVETSSKktFMAKFVKVKGTDQ-VLVKKEISIL-NIARHRNIL-YLHESFESME----E 31831
Cdd:cd14037       8 EKY-LAE----GGFAHVYlvKTSNGGNR--AALKRVYVNDEHDlNVCKREIEIMkRLSGHKNIVgYIDSSANRSGngvyE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMIFEFISG---LDIF-ERINTSafeLNEREVVSYVRQVCEALEFLHSQN--IGHFDIRPENIIYQTRKNsiIKIIEFG 31905
Cdd:cd14037      81 VLLLMEYCKGggvIDLMnQRLQTG---LTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGN--YKLCDFG 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31906 QA----RQLKPGDNFRLL------FTAPEYYAPE---VHQHDVVSSATDMWSLGTLVYVLLSGINPFlaETNQQMieNIM 31972
Cdd:cd14037     156 SAttkiLPPQTKQGVTYVeedikkYTTLQYRAPEmidLYRGKPITEKSDIWALGCLLYKLCFYTTPF--EESGQL--AIL 231

                    ....*.
gi 1958765569 31973 NAEYTF 31978
Cdd:cd14037     232 NGNFTF 237
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8531-8607 8.38e-11

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 63.75  E-value: 8.38e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8531 SGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLT-DNTCALTVNMLEDADAGDYTCIATNVAGSDECSAPLTV 8607
Cdd:cd20973      11 EGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDeDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8517-8607 8.47e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 63.76  E-value: 8.47e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8517 PPSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVA 8596
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8597 GSDECSAPLTV 8607
Cdd:cd20972      81 GSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
14212-14292 9.16e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.29  E-value: 9.16e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14212 LTVKAGTKIELPATVTGKPEPKITWTK-ADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEV 14290
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  14291 NV 14292
Cdd:smart00410    84 TV 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
27589-27928 9.28e-11

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 71.51  E-value: 9.28e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27589 ITKNSMTVVWNRPTVDggseiNGYFLEKRDKKSlAWLKVLKETirDTRQKVTGLTeNSDYQYRVCAVNAAGM-GPFSEPS 27667
Cdd:COG4733     549 TAVTTLTVSWDAPAGA-----VAYEVEWRRDDG-NWVSVPRTS--GTSFEVPGIY-AGDYEVRVRAINALGVsSAWAASS 619
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27668 DFYKAADpIDPPGPPAKIRiADSTKSSITLGWSKPVydgGSDVTGYvvEMRQGEEEEWTI-VSTKGEARTTEYVVSNLKP 27746
Cdd:COG4733     620 ETTVTGK-TAPPPAPTGLT-ATGGLGGITLSWSFPV---DADTLRT--EIRYSTTGDWASaTVAQALYPGNTYTLAGLKA 692
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27747 GVNYYFQVSAVNCAGQ--GEPITMTEPVQAKDILEepeiDLDVALRTSVIAKAGEDVQllipfkgrppPTVTWRKDEKNL 27824
Cdd:COG4733     693 GQTYYYRARAVDRSGNvsAWWVSGQASADAAGILD----AITGQILETELGQELDAII----------QNATVAEVVAAT 758
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27825 GSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSSTVSVKVLDTPAAcqklqVKHVSLGTVTL--LWDPPL 27902
Cdd:COG4733     759 VTDVTAQIDTAVLFAGVATAAAIGAEARVAATVAESATAAAATGTAADAAGDASGG-----VTAGTSGTTGAgdTAASTT 833
                           330       340
                    ....*....|....*....|....*.
gi 1958765569 27903 IDGGSPIINYVIEKRDATKRTWSIVS 27928
Cdd:COG4733     834 RVAAAVVLAGVVVYGDAIIESGNTGD 859
fn3 pfam00041
Fibronectin type III domain;
15315-15400 9.38e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 9.38e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15315 GPPINFVFEDIRKDSVLCKWEPPlDDGGSEIINYTLEKKDKTKPDSE-WIVITSTLRNckYSVTKLIEGKEYLFRVRAEN 15393
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTS--VTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 15394 RFGPGPP 15400
Cdd:pfam00041    78 GGGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6654-6725 9.62e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.29  E-value: 9.62e-11
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569   6654 VLECKVAGSSPISIAWFHEK-TKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTV 6725
Cdd:smart00410    13 TLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
31045-31132 9.72e-11

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 63.67  E-value: 9.72e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31045 PGVRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSD--GRtHTLTVMTEEQEDEGVYTCVATNE 31122
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRenGR-HSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|
gi 1958765569 31123 VGEVETSSKL 31132
Cdd:cd05744      80 AGENSFNAEL 89
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
29567-29649 9.81e-11

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 63.32  E-value: 9.81e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29567 DLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCE-KVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSV 29645
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 29646 MVKV 29649
Cdd:cd05894      83 FVKV 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
14907-14988 9.81e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.29  E-value: 9.81e-11
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  14907 DIVVIEGEKLSIPVPFRAVPVPTVSWHKDG-KEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASIN 14985
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  14986 VKV 14988
Cdd:smart00410    83 LTV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
31047-31132 1.03e-10

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 63.18  E-value: 1.03e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31047 VRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRkykmssdGRT----HTLTVMTEEQEDEGVYTCVATNE 31122
Cdd:cd20978       4 IQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPM-------ERAtvedGTLTIINVQPEDTGYYGCVATNE 76
                            90
                    ....*....|
gi 1958765569 31123 VGEVETSSKL 31132
Cdd:cd20978      77 IGDIYTETLL 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5790-5867 1.04e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.97  E-value: 1.04e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5790 PPIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIAN 5867
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
23250-23335 1.07e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 1.07e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23250 DAPKAPEVTAVTKDSMIVVWERPaSDGGSEILGYVLEKRDKEGIRWTRcHKRLIG-ELRLRVTGLLENHNYEFRVSAENA 23328
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWN-EITVPGtTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 23329 AGLSEPS 23335
Cdd:pfam00041    79 GGEGPPS 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6543-6629 1.08e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 63.28  E-value: 1.08e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6543 VEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKIS-SLKILSVEKEDAGTYTFQVQNNVGKS 6621
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRhSLIIEPVTKRDAGIYTCIARNRAGEN 83

                    ....*...
gi 1958765569  6622 SCTAVVDV 6629
Cdd:cd05744      84 SFNAELVV 91
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
31767-31971 1.10e-10

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 67.85  E-value: 1.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK--KEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd05041       1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKflQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPG-----DNFRLL 31919
Cdd:cd05041      81 LTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCL--VGENNVLKISDFGMSREEEDGeytvsDGLKQI 158
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31920 ftaP-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05041     159 ---PiKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTREQI 209
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5696-5787 1.12e-10

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 63.35  E-value: 1.12e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5696 PPQFIKKPSPvLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGIS-FVDGLAT----FQISNARVENSGTYVC 5770
Cdd:cd20956       1 APVLLETFSE-QTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGdYVTSDGDvvsyVNISSVRVEDGGEYTC 79
                            90
                    ....*....|....*..
gi 1958765569  5771 EARNDAGTASCSIELKV 5787
Cdd:cd20956      80 TATNDVGSVSHSARINV 96
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
18613-18696 1.13e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.02  E-value: 1.13e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18613 PGEPENLHIADKGKTFVYLKWRRPDYDGG-SPNLSYHVERRLKGSaDWERVHKgSIKETHYMVDKCVENQIYEFRVQTKN 18691
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  18692 EGGES 18696
Cdd:smart00060    79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
21672-21755 1.16e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 1.16e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21672 GPPTGPiKFDEVSSDFVTFSWEPPEnDGGVPISNYVVEMRQTDSTT-WVELATTVIRTTYKATRLTTGVEYQFRVKAQNR 21750
Cdd:pfam00041     1 SAPSNL-TVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*
gi 1958765569 21751 YGVGP 21755
Cdd:pfam00041    79 GGEGP 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1254-1324 1.19e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.97  E-value: 1.19e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  1254 KNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIrRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASN 1324
Cdd:pfam13927     9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPI-SSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
28881-28957 1.19e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.19e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 28881 VRAGASIRLFIAYQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFTVKV 28957
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLrsSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
14618-15072 1.21e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.80  E-value: 1.21e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14618 VPEKDGGSPITNYIVEKRDVRRKGWQTVDTTVKDTKCTVTPLTEGSLYVFRVAAENAIGqsDYTEIGDSVLAKDTFTTPG 14697
Cdd:COG3401      65 GGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVG--TATTATAVAGGAATAGTYA 142
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14698 PPYALTVVDVTKRHVDLKWEPPKNDGGRPIQRYIIEKKEKLGTRWVKAGKTSGPDcnfrvtDVIEGTEVQFQVRAENEAG 14777
Cdd:COG3401     143 LGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGG------DIEPGTTYYYRVAATDTGG 216
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14778 VGHPSEPteiLSIEDPVGPPSPPLDLHVTDAGRKHIAIAWKPPEKNGgspIIGYHVEMCPVGTEKWMRVNSrpIKDLKFk 14857
Cdd:COG3401     217 ESAPSNE---VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSY- 287
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14858 VEEGVVPDKEYVLRVRAVNAVGV-SDPSEISenvvakdpdckptidlethdivviegeklsipvpfravpvptvswhkdg 14936
Cdd:COG3401     288 TDTGLTNGTTYYYRVTAVDAAGNeSAPSNVV------------------------------------------------- 318
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14937 kevkasdrltmkndhisahlevpksvhadagvytitlenklgSATASINvkvigLPGPCKDIKASDITKSSCKLTWEPPE 15016
Cdd:COG3401     319 ------------------------------------------SVTTDLT-----PPAAPSGLTATAVGSSSITLSWTASS 351
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 15017 fdgGSPILHYVLERREAGRRTYIPVMSGENKLSWTVKDLIPNGEYFFRVKAVNKIG 15072
Cdd:COG3401     352 ---DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12798-12881 1.24e-10

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 63.21  E-value: 1.24e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12798 EFTKPLEDQTVEEEATAVLECEVSRE-NAKVKWFKNGTEI---LKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAKD- 12872
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNi 81
                            90
                    ....*....|..
gi 1958765569 12873 ---FKTSCNLNV 12881
Cdd:cd20951      82 hgeASSSASVVV 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3468-3550 1.25e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.91  E-value: 1.25e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3468 SDVEISIEDVAKLSVTVVGCPKPKIQWFFNGM-LLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYGRAVCSA 3546
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569   3547 HLKV 3550
Cdd:smart00410    82 TLTV 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
29967-30046 1.31e-10

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 62.94  E-value: 1.31e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29967 TVIIRAGASLRLMVSVSGRPSPVITWSK--KGI-DLANRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVL 30043
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRgdKAFtATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                    ...
gi 1958765569 30044 VKV 30046
Cdd:cd05894      84 VKV 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
29752-29836 1.32e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.02  E-value: 1.32e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29752 PSQPGIPEGVGAGKEHIIIQWTKPESDGGNE-ISNYLVDKREKKSlRWTRVNKDyvVYDTRLKVTSLMEGCDYQFRVTAV 29830
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGS-EWKEVNVT--PSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  29831 NSAGNS 29836
Cdd:smart00060    78 NGAGEG 83
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
31770-31959 1.35e-10

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 67.29  E-value: 1.35e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31770 GRGEFGIVHRCVETSSKKTfmakfVKVKGTDQVlvKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERIN 31849
Cdd:cd14060       2 GGGSFGSVYRAIWVSQDKE-----VAVKKLLKI--EKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLN 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31850 TS-AFELNEREVVSYVRQVCEALEFLHSQ---NIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNFRLLFTAPeY 31925
Cdd:cd14060      75 SNeSEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAA--DGVLKICDFGASRFHSHTTHMSLVGTFP-W 151
                           170       180       190
                    ....*....|....*....|....*....|....
gi 1958765569 31926 YAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd14060     152 MAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8423-8498 1.36e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.58  E-value: 1.36e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8423 TIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQN 8498
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5048-5131 1.38e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.91  E-value: 1.38e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5048 PESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGS-CYITKEASESSLELYAVKTTDSGTYTCKVSNVAGSVECS 5126
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   5127 ANLFV 5131
Cdd:smart00410    81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
29060-29141 1.40e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 1.40e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29060 PPRRLDVVDTSKSSAVLAWLKPEhDGGSRITSYLLEMRQKGS-DFWVE---AGHTKqlTFTVERLVENTEYEFRVKAKND 29135
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEitvPGTTT--SVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 29136 AGYSEP 29141
Cdd:pfam00041    79 GGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
33230-33319 1.41e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.41e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33230 PKITQSLK-AEASR-DIAKLTCAVESSALcaKEVAWYKDGKKLKENGHFQFHYSaDGTYELKIHNLSESDCGEYVCEVSG 33307
Cdd:pfam07679     1 PKFTQKPKdVEVQEgESARFTCTVTGTPD--PEVSWFKDGQPLRSSDRFKVTYE-GGTYTLTISNVQPDDSGKYTCVATN 77
                            90
                    ....*....|..
gi 1958765569 33308 EGGTSKTSFQFT 33319
Cdd:pfam07679    78 SAGEAEASAELT 89
I-set pfam07679
Immunoglobulin I-set domain;
12354-12428 1.44e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.44e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12354 FITPLSDVKVFEKDEAKFECEVSREPK-TFRWLKGTQEIAGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAEDK 12428
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
33891-33966 1.44e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.58  E-value: 1.44e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33891 PPKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENTddlTTLIIMDVQKQDGGLYT 33966
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSN---STLTISNVTRSDAGTYT 73
I-set pfam07679
Immunoglobulin I-set domain;
26311-26391 1.47e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.47e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26311 IVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNCK 26390
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 26391 V 26391
Cdd:pfam07679    90 V 90
I-set pfam07679
Immunoglobulin I-set domain;
25229-25310 1.51e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 1.51e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25229 IIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETaARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPITV 25308
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS-DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569 25309 KV 25310
Cdd:pfam07679    89 TV 90
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
33079-33163 1.52e-10

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 62.94  E-value: 1.52e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33079 PRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVV-STSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGkqEAQ 33157
Cdd:cd05894       2 ENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFtATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVG--EDH 79

                    ....*.
gi 1958765569 33158 FTLTVQ 33163
Cdd:cd05894      80 ASLFVK 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
26395-26478 1.54e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.63  E-value: 1.54e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26395 PGPPaGPLEINGLTAEKCSLSWGRPQEDGG-ADIDYYIVEKRETSRlAWTICEAELRTTSCKVTKLLKGNEYIFRVTGVN 26473
Cdd:smart00060     1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1958765569  26474 KYGVG 26478
Cdd:smart00060    79 GAGEG 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33715-33783 1.56e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 62.35  E-value: 1.56e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33715 VLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKN-FRGQCSATA 33783
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
31048-31134 1.56e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 62.98  E-value: 1.56e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31048 RKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTH-TLTVMTEEQEDEGVYTCVATNEVGEV 31126
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLcSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569 31127 ETSSKLLL 31134
Cdd:cd20973      81 TCSAELTV 88
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
29562-29649 1.60e-10

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 62.99  E-value: 1.60e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29562 ARLQG---DLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQY-TGKRATAVIKYCDRSDSGKYTLTVKNA 29637
Cdd:cd05737       1 ARVLGglpDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVeAGRTVYFTINGVSSEDSGKYGLVVKNK 80
                            90
                    ....*....|..
gi 1958765569 29638 SGTKSVSVMVKV 29649
Cdd:cd05737      81 YGSETSDVTVSV 92
fn3 pfam00041
Fibronectin type III domain;
28368-28453 1.60e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 1.60e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28368 DPPGTPDYIDVTRETITLKWNPPlRDGGSKIVAYSIEKRQ--GSDRWVRCNfTDVSECQYTVSGLSPGDRYEFRIIARNA 28445
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPknSGEPWNEIT-VPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*...
gi 1958765569 28446 VGtISPPS 28453
Cdd:pfam00041    79 GG-EGPPS 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4573-4664 1.65e-10

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 62.82  E-value: 1.65e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4573 PSFVKKVDPsYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRM----SFANsEAILDITDVKVDDSGTYSCEA 4648
Cdd:cd20951       1 PEFIIRLQS-HTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKykieSEYG-VHVLHIRRVTVEDSAVYSAVA 78
                            90
                    ....*....|....*.
gi 1958765569  4649 TNDAGSDSCSTEVVIK 4664
Cdd:cd20951      79 KNIHGEASSSASVVVE 94
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11121-11427 1.65e-10

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 70.18  E-value: 1.65e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11121 PEVPKEvvPEKKVAVPKKPEVPPAKVPEVPKKPVVEEKPVIEEKPaipvaeKVESPPTEVYEEPE----EVAAQEEEPAP 11196
Cdd:NF033839    281 QDTPKE--PGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKP------QLEKPKPEVKPQPEkpkpEVKPQLETPKP 352
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11197 VVEEEeyeappppapeipvpqvPEEPKKVV---PEKKypvikkpeppppkvpEVSKKPAPMKKVPVVKKPEPPEAEVPEV 11273
Cdd:NF033839    353 EVKPQ-----------------PEKPKPEVkpqPEKP---------------KPEVKPQPETPKPEVKPQPEKPKPEVKP 400
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11274 PKKLAPVKKEPVPVTKKPEVLPEkvPEAPKkitPEKRESapvpeepeappapveeiPEETIYEEKATITIGRKETPPvee 11353
Cdd:NF033839    401 QPEKPKPEVKPQPEKPKPEVKPQ--PEKPK---PEVKPQ-----------------PEKPKPEVKPQPEKPKPEVKP--- 455
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 11354 reierfiQPEEPGMEPQPE-ETPVQEPEPEKKVIEKPKLKPRPPIRAPSPPKEDVKEKIFQLKAVSKKKVPEKPE 11427
Cdd:NF033839    456 -------QPETPKPEVKPQpEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNKPK 523
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
31440-31518 1.67e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.58  E-value: 1.67e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIadGLKYRVQEFKGGYHQLIIASVTDDDATVYQVRATN 31518
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPIS--SGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4404-4466 1.69e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 62.35  E-value: 1.69e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  4404 AKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
16940-17016 1.72e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.63  E-value: 1.72e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  16940 KVTDWTKSSVDLEWSPPLKDGG-SKITGYIVEYKEEGKEEWEKGKDkeVRGTKLVVTGLKEGAFYKFRVRAVNIAGVG 17016
Cdd:smart00060     8 RVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVT--PSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
23645-23726 1.75e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 1.75e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23645 PPGKITVDDVTRNSVSLSWTKPEhDGGSKIIQYIVEMQAKNT-DKWSECARVKSL-EAVITSLTQGEEYLFRVIAVNEKG 23722
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 23723 RSDP 23726
Cdd:pfam00041    81 EGPP 84
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
31763-31955 1.76e-10

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 68.52  E-value: 1.76e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK------VKGTDQVLVKKEISILNIARHrNILYLHESFESMEELVMIF 31836
Cdd:cd14229       2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKnhpsyaRQGQIEVGILARLSNENADEF-NFVRAYECFQHRNHTCLVF 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGlDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIEFGQARQLKpg 31913
Cdd:cd14229      81 EMLEQ-NLYDFLKQNKFSpLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdPVRQPYRVKVIDFGSASHVS-- 157
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 1958765569 31914 DNFRLLFTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSG 31955
Cdd:cd14229     158 KTVCSTYLQSRYYrAPEIILGLPFCEAIDMWSLGCVIAELFLG 200
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
33075-33162 1.81e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 62.76  E-value: 1.81e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33075 ILTKP-RSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSA--RHQVTTAKYKSTFEISSVQASDEGNYSVVVENTD 33151
Cdd:cd20974       2 VFTQPlQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|.
gi 1958765569 33152 GKQEAQFTLTV 33162
Cdd:cd20974      82 GQATSTAELLV 92
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8514-8607 1.81e-10

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 62.90  E-value: 1.81e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8514 RIIPPSFTRKLKETnglsGSSVVMECKVF-GSPPISVLWLHDGNAISSGRKYQTTLTDN-TCALTVNMLEDADAGDYTCI 8591
Cdd:cd20959       3 RIIPFAFGEGAAQV----GMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRrSSILSIDSLEASHAGNYTCH 78
                            90
                    ....*....|....*.
gi 1958765569  8592 ATNVAGSDECSAPLTV 8607
Cdd:cd20959      79 ARNSAGSASYTAPLTV 94
I-set pfam07679
Immunoglobulin I-set domain;
25918-25996 1.85e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 62.66  E-value: 1.85e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 25918 VKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIV 25996
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
28610-28982 1.85e-10

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 70.74  E-value: 1.85e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28610 AWALIEDHCEAQSYTAIKLITGNEYQFRVSAV----NKF-------GVGRPLESDP--VVAQIQYTIpdapgipEPSNVT 28676
Cdd:COG4733     478 VWAFGPDELETQLFRVVSIEENEDGTYTITAVqhapEKYaaidagaFDDVPPQWPPvnVTTSESLSV-------VAQGTA 550
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28677 GNSITLTWTRPESDGGNEIQHyileRREkkSTRWVKVISkrpISETRFKVTGLVEGNeYEFHVMAENAAGV--GPASGIS 28754
Cdd:COG4733     551 VTTLTVSWDAPAGAVAYEVEW----RRD--DGNWVSVPR---TSGTSFEVPGIYAGD-YEVRVRAINALGVssAWAASSE 620
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28755 RLIKCREPvnPPSAPAVVKVTDTSkTTVSLEWARPVfdgGMEIIGYIIEMckADLGDWH--KVNTEPCVKTRYTVTDLQA 28832
Cdd:COG4733     621 TTVTGKTA--PPPAPTGLTATGGL-GGITLSWSFPV---DADTLRTEIRY--STTGDWAsaTVAQALYPGNTYTLAGLKA 692
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28833 GEEYKFRVSAINGAGKGDSCEVTGTikAVDRLSAPELDIDANFKQTHIVRAGASI--RLFIAYQGRPTPTAVWSKPDSNL 28910
Cdd:COG4733     693 GQTYYYRARAVDRSGNVSAWWVSGQ--ASADAAGILDAITGQILETELGQELDAIiqNATVAEVVAATVTDVTAQIDTAV 770
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 28911 SIRADI------HTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFTVKVLDSPGPPGPITFKDVTRGSATLMWD 28982
Cdd:COG4733     771 LFAGVAtaaaigAEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVYG 848
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
15919-16006 1.90e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.52  E-value: 1.90e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15919 TIKVKAGEPVNIPADVTGLPMPKIEWSKN--EKVIEKPtdalnitKEEVSRSEAKTELSIPKAVREDKGTYTITASNRLG 15996
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQggKLLAESG-------RFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG 75
                             90
                     ....*....|
gi 1958765569  15997 SVFRNVHVEV 16006
Cdd:smart00410    76 SASSGTTLTV 85
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
22659-22756 1.91e-10

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 63.05  E-value: 1.91e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22659 PPAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSA 22738
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*...
gi 1958765569 22739 GEATETLNVIVLDKPGPP 22756
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPP 98
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33090-33156 1.96e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 61.96  E-value: 1.96e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33090 ARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEA 33156
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8421-8511 1.96e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 62.60  E-value: 1.96e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8421 PATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8501 GKDSCTVSIQV 8511
Cdd:cd20972      81 GSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
18030-18112 1.96e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.52  E-value: 1.96e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18030 EGLVVKAGTTVRFPAIIRGVPVPTAKWATDGTE-ITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAV 18108
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  18109 HLTV 18112
Cdd:smart00410    82 TLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29023-29480 1.99e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.03  E-value: 1.99e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29023 DLTEGVPYYFRVSAENEYGVGEPYEMPEPIVATEQPAPPRRLDVVDTSKSSAVLAWLKPEhdgGSRITSYLLEMRQKGSD 29102
Cdd:COG3401     198 DIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDG 274
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29103 FWVEAGHTKQLTFTVERLVENTEYEFRVKAKNDAG-YSEPreafssviikepqieptadltgitnqlitckagstftidv 29181
Cdd:COG3401     275 PFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP---------------------------------------- 314
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29182 pisgrpapkvtwkleemrlketdrmsitttkdrttltvkdsmrgdsgryfltlENTAGVKTFTITvvvigrPGPVTGpIE 29261
Cdd:COG3401     315 -----------------------------------------------------SNVVSVTTDLTP------PAAPSG-LT 334
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29262 VSSVSAESCVLSWSEPKDDGgteITNYIVEKRESGTTAWQLINSSVKRTQIKVTHLTKYKEYCFRVSSENRFGvskpLES 29341
Cdd:COG3401     335 ATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG----NES 407
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29342 VP--IVAEHPFVPPSAPTRPEVYYVSANAMSIRWEEPYHDGGSKIVGYWVEKKERNTILWVKENKVPClecnYKVTGLVE 29419
Cdd:COG3401     408 APseEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSS----TVTATTTD 483
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 29420 GLEYQFRTYALNAAGVSKASEASRPIMAQNPVDPPGRPEVTDVTRSTVSLVWSAPMYDGGS 29480
Cdd:COG3401     484 TTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3464-3550 2.16e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 62.59  E-value: 2.16e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3464 IKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGN-NHSLIILFTRFQDEGEYTCMASNEYGRA 3542
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  3543 VCSAHLKV 3550
Cdd:cd20973      81 TCSAELTV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7482-7557 2.17e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.20  E-value: 2.17e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7482 RIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVEN 7557
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4292-4368 2.17e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.20  E-value: 2.17e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASN 4368
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31512-31733 2.20e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.03  E-value: 2.20e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31512 YQVRATNQGGSvsGTASLEVEVPAKIHLPKTLEGMGAVHALRGEVVsikipfsgkpdpvITWQKGQDL----------ID 31581
Cdd:COG3401     207 YRVAATDTGGE--SAPSNEVSVTTPTTPPSAPTGLTATADTPGSVT-------------LSWDPVTESdatgyrvyrsNS 271
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31582 NNGHYQVIVTRSFTSLVFPNgverKDAG---FYVVCAKNRFGI-----DQKTVELDVAdVPDPPRGVKVSDVSRDSVNLT 31653
Cdd:COG3401     272 GDGPFTKVATVTTTSYTDTG----LTNGttyYYRVTAVDAAGNesapsNVVSVTTDLT-PPAAPSGLTATAVGSSSITLS 346
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31654 WTEPASDGgskVTNYIVEKCATTAERWLRVGQ-ARETRYTVVNLFGKTSYQFRVIAENKFGLSkpSEPSEPTVTKEDKTR 31732
Cdd:COG3401     347 WTASSDAD---VTGYNVYRSTSGGGTYTKIAEtVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAA 421

                    .
gi 1958765569 31733 A 31733
Cdd:COG3401     422 S 422
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
14209-14293 2.22e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 62.76  E-value: 2.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14209 LAGLTVKAGTKIELPATVTGKPEPKITWTK----ADTLLRPdqRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRA 14284
Cdd:cd20974       7 LQSVVVLEGSTATFEAHVSGKPVPEVSWFRdgqvISTSTLP--GVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQA 84

                    ....*....
gi 1958765569 14285 TAVVEVNVL 14293
Cdd:cd20974      85 TSTAELLVL 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
33891-33984 2.22e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 62.60  E-value: 2.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQqgrFHIENTDDLTTLIIMDVQKQDGGLYTLSLG 33970
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPD---IQIHQEGDLHSLIIAEAFEEDTGRYSCLAT 77
                            90
                    ....*....|....
gi 1958765569 33971 NEFGSDSATVNINI 33984
Cdd:cd20972      78 NSVGSDTTSAEIFV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6259-6349 2.23e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 62.51  E-value: 2.23e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDS-VAVMQMNSLGTEDSGDFICEAQNP 6337
Cdd:cd05744       1 PHFLQAPG-DLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569  6338 AGSTSCSTKVIV 6349
Cdd:cd05744      80 AGENSFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
13336-13419 2.23e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 2.23e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13336 EFVEHLEDQTVTEFDDAVFSCQLS-REKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVEDR--- 13411
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*....
gi 1958765569 13412 -KSRARLFV 13419
Cdd:pfam07679    82 aEASAELTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
30352-30645 2.27e-10

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 70.36  E-value: 2.27e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30352 KIDEVDATSVTISWEPPEldggAPlsgyvveqrdahRPGWLPVSESVTRPT--FKFTRLTEGNEYVFRVAAT----NRFG 30425
Cdd:COG4733     454 TVQSVAGRTLTVSTAYSE----TP------------EAGAVWAFGPDELETqlFRVVSIEENEDGTYTITAVqhapEKYA 517
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30426 IGsylQSEVIECRSSISIPGPPETLQIFDISRDG-----MTLTWYPPEDDGGSQVtgyiierkEVRAD--RWVRVNKVpv 30498
Cdd:COG4733     518 AI---DAGAFDDVPPQWPPVNVTTSESLSVVAQGtavttLTVSWDAPAGAVAYEV--------EWRRDdgNWVSVPRT-- 584
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30499 TMTRYRSTGLIEGlEYEHRVTAINARGT-GKPSRPSKPTVAMDpIAPPGKPQNPRVTDTTRtSVSLAWSVPEDEGgskVT 30577
Cdd:COG4733     585 SGTSFEVPGIYAG-DYEVRVRAINALGVsSAWAASSETTVTGK-TAPPPAPTGLTATGGLG-GITLSWSFPVDAD---TL 658
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30578 GYLIEMQKVDQREWTKCNTTPTKIREYTLTHLPQGAEYRFRVLACNAGGPGEPAEVPG--TVKVTEMLEY 30645
Cdd:COG4733     659 RTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGqaSADAAGILDA 728
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15709-15790 2.28e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.25  E-value: 2.28e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15709 PGPVLDLKPVVTNRKMCLLNWSDPADDGG-SEITGFIIERKDAKMHTWRQPIETERSKCDITGLIEGQEYKFRVIAKNKF 15787
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  15788 GCG 15790
Cdd:smart00060    81 GEG 83
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
31768-31954 2.31e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 67.65  E-value: 2.31e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31768 DLGRGEFGIVHRC-VETSSKKTfmAKFVKVK-------GTDQVLVKKEISILNIARHRNIL----YLHESFESMEELVMi 31835
Cdd:cd05079      11 DLGEGHFGKVELCrYDPEGDNT--GEQVAVKslkpesgGNHIADLKKEIEILRNLYHENIVkykgICTEDGGNGIKLIM- 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 fEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRknSIIKIIEFGQARQLKPGDN 31915
Cdd:cd05079      88 -EFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE--HQVKIGDFGLTKAIETDKE 164
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 1958765569 31916 FRLL---FTAPEY-YAPEVHQHDVVSSATDMWSLGTLVYVLLS 31954
Cdd:cd05079     165 YYTVkddLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLT 207
fn3 pfam00041
Fibronectin type III domain;
19605-19690 2.35e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.35e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19605 SEPKNARVTKVNKDCIFVAWDRPDsDGGSPITGYLIERKERNSLlWVKANDTIVRST-EYPCAGLVEGLEYSFRIYALNK 19683
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSG-EPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 19684 AGSSPPS 19690
Cdd:pfam00041    79 GGEGPPS 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8713-8786 2.35e-10

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 62.22  E-value: 2.35e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  8713 YSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKDS 8786
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
fn3 pfam00041
Fibronectin type III domain;
29354-29439 2.37e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.37e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29354 SAPTRPEVYYVSANAMSIRWEEPyHDGGSKIVGYWVEKKERNTILWVKENKVPCLECNYKVTGLVEGLEYQFRTYALNAA 29433
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 29434 GVSKAS 29439
Cdd:pfam00041    80 GEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33898-33984 2.38e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 2.38e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGrrIQSQEQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                     ....*..
gi 1958765569  33978 ATVNINI 33984
Cdd:smart00410    79 SGTTLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8518-8607 2.38e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 62.51  E-value: 2.38e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQtTLTDNTCALTVnMLEDA---DAGDYTCIATN 8594
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHK-MLVRENGRHSL-IIEPVtkrDAGIYTCIARN 78
                            90
                    ....*....|...
gi 1958765569  8595 VAGSDECSAPLTV 8607
Cdd:cd05744      79 RAGENSFNAELVV 91
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
31766-32025 2.39e-10

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 66.90  E-value: 2.39e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31766 AEDLGRGEFGIVHRCVETSSKKTFMaKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd05112       9 VQEIGSGQFGLVHLGYWLNKDKVAI-KTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLS 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQL-------KPGDNFRL 31918
Cdd:cd05112      88 DYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCL--VGENQVVKVSDFGMTRFVlddqytsSTGTKFPV 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 lftapEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENImNAEYtfdeeafqeisleamdfidRL 31997
Cdd:cd05112     166 -----KWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDI-NAGF-------------------RL 220
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31998 LvKERKSRMTASEALKHPWLKQRMDRVS 32025
Cdd:cd05112     221 Y-KPRLASTHVYEIMNHCWKERPEDRPS 247
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8243-8325 2.41e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 2.41e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8243 PVETLKGADVHLECELQGTPPFQVSWYKDKRE-LRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDTcvGS 8321
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS--SG 80

                     ....
gi 1958765569   8322 VTLK 8325
Cdd:smart00410    81 TTLT 84
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
26707-26786 2.43e-10

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 62.16  E-value: 2.43e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26707 TLTVKAGSSFTMTVPFRGRPIPNVSWSKPD---TDLRTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTFV 26783
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRGDkafTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                    ...
gi 1958765569 26784 VKV 26786
Cdd:cd05894      84 VKV 86
fn3 pfam00041
Fibronectin type III domain;
19902-19985 2.44e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.44e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19902 GPPASVKINKMYADRAMLSWEPPlEDGGSEITNYIVDKRETSRPN-WAQVSATVPITSCTVEKLIEGHEYQFRICAENKY 19980
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 19981 GVGDP 19985
Cdd:pfam00041    80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
30944-31028 2.46e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.46e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30944 SQPGELEILSISKDSVILQWEKPEcDGGKEILGYWVEYRQSGD-SAWKKSNKERIKdRQFTIGGLLEATEYEFRVFAENE 31022
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 31023 TGLSRP 31028
Cdd:pfam00041    79 GGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8532-8607 2.48e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 2.48e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   8532 GSSVVMECKVFGSPPISVLWLHDG-NAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAGSDECSAPLTV 8607
Cdd:smart00410     9 GESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5978-6066 2.50e-10

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 62.44  E-value: 2.50e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5978 QIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRY-FSMSFEN--NVASFRIQSVMKQDSGQYTFKVEND 6054
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpGKYKIESeyGVHVLHIRRVTVEDSAVYSAVAKNI 81
                            90
                    ....*....|..
gi 1958765569  6055 FGSSSCDAYLRV 6066
Cdd:cd20951      82 HGEASSSASVVV 93
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
32206-32293 2.52e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 62.21  E-value: 2.52e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32206 PLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKpgdDDKKYTFESDK-GLYQLTINSVTTDDDAEYAVVARNKHGE 32284
Cdd:cd20973       3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIV---ESRRFQIDQDEdGLCSLIISDVCGDDSGKYTCKAVNSLGE 79

                    ....*....
gi 1958765569 32285 DSCKAKLTV 32293
Cdd:cd20973      80 ATCSAELTV 88
I-set pfam07679
Immunoglobulin I-set domain;
12442-12525 2.53e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 2.53e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12442 KFLTPLKDVTAKERENAVFTVELSHDNIP-VSWFKNDQRLHTSKRVSMHDEGKTHSITFKDLSIDDTSQIRVEAMGI--- 12517
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*....
gi 1958765569 12518 -SSEAKLTV 12525
Cdd:pfam07679    82 aEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
14996-15076 2.56e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.56e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14996 KDIKASDITKSSCKLTWEPPEfDGGSPILHYVLERREAGRRTY-IPVMSGENKLSWTVKDLIPNGEYFFRVKAVNKIGGG 15074
Cdd:pfam00041     4 SNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    ..
gi 1958765569 15075 EY 15076
Cdd:pfam00041    83 PP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
22670-22749 2.60e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 2.60e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDD-VPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNVI 22748
Cdd:smart00410     5 TVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84

                     .
gi 1958765569  22749 V 22749
Cdd:smart00410    85 V 85
fn3 pfam00041
Fibronectin type III domain;
16112-16202 2.66e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.66e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16112 GPPGKPKVLERTKGSMLVSWTPPLDnGGSPITGY---WLEKREEGGAYWSRVSRAPITkvglkgveFSVPRLIEGVKYQF 16188
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYeveYRPKNSGEPWNEITVPGTTTS--------VTLTGLKPGTEYEV 71
                            90
                    ....*....|....
gi 1958765569 16189 RAMAINAAGIGPPS 16202
Cdd:pfam00041    72 RVQAVNGGGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31610-31731 2.77e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.65  E-value: 2.77e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31610 FYVVCAKNRFGIDQKTVELDV---ADVPDPPRGVKVSDVSRDSVNLTWTEPASDGgskVTNYIVEKCATTAERWLRVGQA 31686
Cdd:COG3401     206 YYRVAATDTGGESAPSNEVSVttpTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 31687 RETRYTVVNLFGKTSYQFRVIAENKFGlsKPSEPSEPTVTKEDKT 31731
Cdd:COG3401     283 TTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLT 325
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
13336-13420 2.93e-10

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 62.44  E-value: 2.93e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13336 EFVEHLEDQTVTEFDDAVFSCQLSRE-KANVKWYRNGREI---KEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVEDR 13411
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNI 81
                            90
                    ....*....|...
gi 1958765569 13412 ----KSRARLFVE 13420
Cdd:cd20951      82 hgeaSSSASVVVE 94
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5697-5788 3.06e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 62.37  E-value: 3.06e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVLRnGQSTTFECQVTGTPEIRVSWYLDGNEI--TDLRRYGISFVDGLATFQISNARVENSGTYVCEARN 5774
Cdd:cd20974       1 PVFTQPLQSVVVLE-GSTATFEAHVSGKPVPEVSWFRDGQVIstSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569  5775 DAGTASCSIELKVK 5788
Cdd:cd20974      80 GSGQATSTAELLVL 93
I-set pfam07679
Immunoglobulin I-set domain;
16638-16725 3.23e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 3.23e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16638 MEVEEGTDVNIVAKIKGVPFPTLTWFKAppkkpdsKEPVVYDTHVNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTA 16717
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKD-------GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                    ....*...
gi 1958765569 16718 SKEMRLNV 16725
Cdd:pfam07679    83 EASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7959-8040 3.32e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.75  E-value: 3.32e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7959 KDVHETLGFPVAFECRINGSEPLQVSWYKDG-QLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLGTASSSA 8037
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569   8038 KLI 8040
Cdd:smart00410    82 TLT 84
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4390-4476 3.39e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 61.64  E-value: 3.39e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4390 LSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALspsPDCRITDADNkHSLELSNLTVQDRGVYSCKASNKFGADI 4469
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL---PKGRYEILDD-HSLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  4470 CQAELTI 4476
Cdd:cd05725      77 ASATLTV 83
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
27382-27475 3.40e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 61.99  E-value: 3.40e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27382 PVIDLPLEYTEVvkyRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNAL--VCVENSTDLASILIKDANRLNSGSYELKL 27459
Cdd:cd20974       1 PVFTQPLQSVVV---LEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLpgVQISFSDGRAKLSIPAVTKANSGRYSLTA 77
                            90
                    ....*....|....*.
gi 1958765569 27460 RNAMGSASATIRVQIL 27475
Cdd:cd20974      78 TNGSGQATSTAELLVL 93
fn3 pfam00041
Fibronectin type III domain;
23351-23435 3.43e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 3.43e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23351 GPPNNPKVMDVTRSSVFLSWTKPIYDGGcEIQGYIVEKCDV-SVGEWTMCTPPTgiNKTNLEVEKLLEKHEYNFRICAIN 23429
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKnSGEPWNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*.
gi 1958765569 23430 KAGVGE 23435
Cdd:pfam00041    78 GGGEGP 83
fn3 pfam00041
Fibronectin type III domain;
26791-26874 3.47e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 3.47e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26791 GPPANITVREVTKETAVLSWDVPEnDGGAPVKNYHIEKREASK-KAWVSVTNNCSRLSYKVTNLQEGAVYYFRVSGENEF 26869
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 26870 GVGVP 26874
Cdd:pfam00041    80 GEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
17340-17420 3.49e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 3.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17340 LTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFCQVN 17419
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 17420 V 17420
Cdd:pfam07679    90 V 90
I-set pfam07679
Immunoglobulin I-set domain;
2136-2222 3.49e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 3.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2136 FTQELQDVVAKEKDTmATFECETS-EPFVKVKWYKDGIEVHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSCVlVEDE-- 2212
Cdd:pfam07679     3 FTQKPKDVEVQEGES-ARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV-ATNSag 80
                            90
                    ....*....|
gi 1958765569  2213 NIKTTAKLIV 2222
Cdd:pfam07679    81 EAEASAELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8440-8507 3.52e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 61.19  E-value: 3.52e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8440 TLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPV-GKDSCTV 8507
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7107-7196 3.58e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.83  E-value: 3.58e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVG 7186
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81
                            90
                    ....*....|
gi 1958765569  7187 KDMCSAQLSV 7196
Cdd:cd20972      82 SDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
18429-18510 3.63e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.75  E-value: 3.63e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18429 VITVRVGQTIRILARVKGRPEPDITWSKEGKVLVK-DKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  18508 VNV 18510
Cdd:smart00410    83 LTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7200-7290 3.77e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 61.74  E-value: 3.77e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDTSKVaKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNS-VALLTINEASVEDTGDYICEAHNG 7278
Cdd:cd05744       1 PHFLQAPGDLEV-QEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569  7279 VGHASCSTALKV 7290
Cdd:cd05744      80 AGENSFNAELVV 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
14214-14300 4.08e-10

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 61.89  E-value: 4.08e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14214 VKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVNVL 14293
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*..
gi 1958765569 14294 DKPGPPA 14300
Cdd:cd05762      93 DKPDPPA 99
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5976-6066 4.11e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.83  E-value: 4.11e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5976 PAQIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDF 6055
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  6056 GSSSCDAYLRV 6066
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5229-5305 4.14e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 61.43  E-value: 4.14e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTN 5305
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7200-7291 4.20e-10

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 61.67  E-value: 4.20e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDTSKVAkQGESIQLECKISGSPEIKVVWFRND---SELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAH 7276
Cdd:cd20951       1 PEFIIRLQSHTVW-EKSDAKLRVEVQGKPDPEVKWYKNGvpiDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAK 79
                            90
                    ....*....|....*
gi 1958765569  7277 NGVGHASCSTALKVK 7291
Cdd:cd20951      80 NIHGEASSSASVVVE 94
I-set pfam07679
Immunoglobulin I-set domain;
2931-3013 4.24e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.50  E-value: 4.24e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2931 ITSMLKDINAEEKDTITFEVTVnyEG---ISYKWLKNGVEIKSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVA----G 3003
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTV--TGtpdPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaG 80
                            90
                    ....*....|
gi 1958765569  3004 KATSTATLYV 3013
Cdd:pfam07679    81 EAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1254-1337 4.28e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.37  E-value: 4.28e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   1254 KNYRILEGMGVTFHCKMSGYPLPKIAWYKDG-KRIRRGERYQMDFlQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICS 1332
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSR-SGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   1333 GKLYV 1337
Cdd:smart00410    81 TTLTV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7855-7945 4.29e-10

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 61.88  E-value: 4.29e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7855 PPYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAyKMQFKNNVASLVINKVDHSDVGEYTCKAENSV 7934
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  7935 GAVASSAVLVI 7945
Cdd:cd20976      80 GQVSCSAWVTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6090-6159 4.49e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 60.81  E-value: 4.49e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6090 IHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAGDNACSGI 6159
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
19703-19787 4.56e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 61.48  E-value: 4.56e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19703 DPPGKPEVVDVTKNSASLIWARPKHDGG-SKIIGYFVEACKlPGDKWVRCNTTPHQiplEEYTATGLEENAQYQFRAIAK 19781
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKEVNVTPSS---TSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1958765569  19782 TAVNIS 19787
Cdd:smart00060    78 NGAGEG 83
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
1417-1507 4.65e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 61.60  E-value: 4.65e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIK-EDGTQSLIIVPALPSDSGEWTVVAQNR 1495
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISfSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  1496 AGKSTISVTLTV 1507
Cdd:cd20974      81 SGQATSTAELLV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8535-8603 4.67e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 60.81  E-value: 4.67e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8535 VVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATN-VAGSDECSA 8603
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
3461-3550 4.76e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.44  E-value: 4.76e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYG 3540
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81
                            90
                    ....*....|
gi 1958765569  3541 RAVCSAHLKV 3550
Cdd:cd20972      82 SDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
18909-18994 4.78e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 4.78e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18909 GRPDPPEVTKVSKEEMTVVWNAPEYDGGKsITGYYLEKKEK-HAVRWVPVNKSAiPERRLKVQNLLPGHEYQFRVKAENE 18987
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKnSGEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 18988 VGIGEPS 18994
Cdd:pfam00041    79 GGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4499-4569 4.81e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.37  E-value: 4.81e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569   4499 LECQVDEDRKVSITWSKDGQKLPAGKD-YKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAGSSSSSATVAV 4569
Cdd:smart00410    14 LSCEASGSPPPEVTWYKQGGKLLAESGrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
12530-12614 4.99e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.44  E-value: 4.99e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12530 PYFTGKLQDYTGVEKDEVVLQCEISKADAP-VKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC----DCG 12604
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPvVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSClatnSVG 81
                            90
                    ....*....|
gi 1958765569 12605 TDQTSGKLDI 12614
Cdd:cd20972      82 SDTTSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5808-5870 5.05e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 60.81  E-value: 5.05e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5808 VELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANEGG 5870
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
103-180 5.23e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 61.04  E-value: 5.23e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   103 PPNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATN 180
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
32317-32389 5.24e-10

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 61.07  E-value: 5.24e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 32317 CHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIeIVHEGLDYYALHIRDTLPEDTGYYRVTATNTAGSTS 32389
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRV-QIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
I-set pfam07679
Immunoglobulin I-set domain;
12798-12881 5.25e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.50  E-value: 5.25e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12798 EFTKPLEDQTVEEEATAVLECEVS-RENAKVKWFKNGTEILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAKD---- 12872
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsage 81

                    ....*....
gi 1958765569 12873 FKTSCNLNV 12881
Cdd:pfam07679    82 AEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
14798-14884 5.27e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 5.27e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14798 SPPLDLHVTDAGRKHIAIAWKPPEkNGGSPIIGYHVEMCPVGTEKWMRVNSRP-------IKDLKfkveegvvPDKEYVL 14870
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPgtttsvtLTGLK--------PGTEYEV 71
                            90
                    ....*....|....
gi 1958765569 14871 RVRAVNAVGVSDPS 14884
Cdd:pfam00041    72 RVQAVNGGGEGPPS 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1516-1607 5.29e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.44  E-value: 5.29e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIvpHKYPRIRIEGTKGEAALKIDSTISQDSAWYTATAINK 1595
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKEL--QNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  1596 AGRDTTRCKVNI 1607
Cdd:cd20972      80 VGSDTTSAEIFV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8989-9079 5.33e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 61.60  E-value: 5.33e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREI---RSGGnYQISYLENSAHLTIVKVDKGDSGQYTCYAIN 9065
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIstsTLPG-VQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569  9066 EVGKDSCTAQLNIK 9079
Cdd:cd20974      80 GSGQATSTAELLVL 93
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
13351-13419 5.61e-10

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 61.10  E-value: 5.61e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 13351 DAVFSCQLSREKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVEDRKSRARLFV 13419
Cdd:cd20967      14 KIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18678-18960 5.63e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.49  E-value: 5.63e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18678 VENQIYEFRVQTKNEGGESDWVRTEEVVVKEDLQKPVLDLKLSGVLTvkagDTIRLeagvrgkpfpevAWT--KDKDAT- 18754
Cdd:COG3401     200 EPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTP----GSVTL------------SWDpvTESDATg 263
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18755 -DLTRS-----PRVKIDTSAESskfSLTKAKRSDGGKY--VVTATNPAG-----SFVAYATVNVLdKPGPVRNLKIADVS 18821
Cdd:COG3401     264 yRVYRSnsgdgPFTKVATVTTT---SYTDTGLTNGTTYyyRVTAVDAAGnesapSNVVSVTTDLT-PPAAPSGLTATAVG 339
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18822 SDRCTIRWDPPEDDGgceIQNYILEKCESKRMVWSTYSANVLTPGATVTRLIEGNEYIFRVRAENKIGTGPPTeSKPVIA 18901
Cdd:COG3401     340 SSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAP-SEEVSA 415
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 18902 KTKYDRPG------RPDPPEVTKVSKEEMTVVWNAPEYDGGKSITGYYLEKKEKHAVRWVPVNKS 18960
Cdd:COG3401     416 TTASAASGesltasVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
1038-1127 5.81e-10

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 61.32  E-value: 5.81e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|
gi 1958765569  1118 HGETSASASL 1127
Cdd:cd05892      81 AGVVSCNARL 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4386-4475 5.93e-10

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 61.22  E-value: 5.93e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4386 PPTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKF 4465
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82
                            90
                    ....*....|
gi 1958765569  4466 GADICQAELT 4475
Cdd:cd05747      83 GKQEAQFTLT 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4588-4663 5.95e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 61.05  E-value: 5.95e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNtvRMSFANSE---AILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVI 4663
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESR--RFQIDQDEdglCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
9181-9271 6.07e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.44  E-value: 6.07e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9181 PPVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVA 9260
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  9261 GSDTSKCKVTI 9271
Cdd:cd20972      81 GSDTTSAEIFV 91
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
19181-19401 6.08e-10

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 68.82  E-value: 6.08e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19181 TRDDSGKYSLTLVNPAGEK------AVFVNVKVLDTPGPVS-----DLKVSDVTKTSCHVSWAPPENdggspVTHYIVEK 19249
Cdd:COG4733     497 EENEDGTYTITAVQHAPEKyaaidaGAFDDVPPQWPPVNVTtseslSVVAQGTAVTTLTVSWDAPAG-----AVAYEVEW 571
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19250 ReAERKTWSTVtPEVKKTSFNVTNLVPGNeYFFRVTAVNEYG-PGVPTDVPKPVLASDPLSEPDPPRkVEVTEMTkNSAT 19328
Cdd:COG4733     572 R-RDDGNWVSV-PRTSGTSFEVPGIYAGD-YEVRVRAINALGvSSAWAASSETTVTGKTAPPPAPTG-LTATGGL-GGIT 646
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 19329 LAWLPPLrdgGAKIDGYIISYREEDQPADRWTEYSVVKDLSLIITGLKEGKKYKFRVAARNAVGVSMPREAEG 19401
Cdd:COG4733     647 LSWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSG 716
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8893-8983 6.11e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 61.21  E-value: 6.11e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGK--PLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNP 8970
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  8971 IGSASSSAKLILT 8983
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
25229-25311 6.11e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 61.21  E-value: 6.11e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25229 IIVRAGETFVLEADIRGKPIPDIVWSKDGNELE-ETAARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPIT 25307
Cdd:cd20974      10 VVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIStSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAE 89

                    ....
gi 1958765569 25308 VKVL 25311
Cdd:cd20974      90 LLVL 93
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33701-33787 6.33e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 60.87  E-value: 6.33e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33701 ISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKN--NLPISISSNISVSrsrnmyTLEIRNASVSDSGKYTVKAKNFRGQ 33778
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEdgELPKGRYEILDDH------SLKIRKVTAGDMGSYTCVAENMVGK 74

                    ....*....
gi 1958765569 33779 CSATASLTV 33787
Cdd:cd05725      75 IEASATLTV 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8163-8231 6.38e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.98  E-value: 6.38e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8163 CKIGGSPEIKVLWYKDEVE-IQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARNAAGSASSSTSLKV 8231
Cdd:smart00410    16 CEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
24544-24624 6.39e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.12  E-value: 6.39e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24544 KGIVVRAGGSARIHIPFKGRPTPEITWSKEEGEFT--DKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVT 24621
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 24622 VKV 24624
Cdd:pfam07679    88 LTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6258-6349 6.43e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.06  E-value: 6.43e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6258 PPKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNP 6337
Cdd:cd20972       1 PPQFIQKLR-SQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  6338 AGSTSCSTKVIV 6349
Cdd:cd20972      80 VGSDTTSAEIFV 91
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
16068-16389 6.51e-10

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 68.82  E-value: 6.51e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16068 RRYGIWKLIPNGQYEFRVRAV----NKYGTSDECKSDKVVIQDPyrlpgPPGKPKVLERTK-------GSMLVSWTPPLD 16136
Cdd:COG4733     489 QLFRVVSIEENEDGTYTITAVqhapEKYAAIDAGAFDDVPPQWP-----PVNVTTSESLSVvaqgtavTTLTVSWDAPAG 563
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16137 NggspiTGYWLEKREEGGAyWSRVSRAPITkvglkgvEFSVPRLIEGVkYQFRAMAINAAGI-GPPSEPSDPAVAGDPIY 16215
Cdd:COG4733     564 A-----VAYEVEWRRDDGN-WVSVPRTSGT-------SFEVPGIYAGD-YEVRVRAINALGVsSAWAASSETTVTGKTAP 629
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16216 PPGPPSCpevkdKTKS---SISLAWKPPAkdgGSPIKGYivEMQEEGTTDWKKVNEPDKLLTACECVVPNLKELRKYRFR 16292
Cdd:COG4733     630 PPAPTGL-----TATGglgGITLSWSFPV---DADTLRT--EIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYR 699
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16293 VKAVNEAGESEPSDTTGEipATDIQEVPEVFIDIGAQDCLICKAGSQIRIPAVIKGRPtpkSSWEFDGKAKKAMKDGIHD 16372
Cdd:COG4733     700 ARAVDRSGNVSAWWVSGQ--ASADAAGILDAITGQILETELGQELDAIIQNATVAEVV---AATVTDVTAQIDTAVLFAG 774
                           330
                    ....*....|....*..
gi 1958765569 16373 IPEDAQLETAENSSVIV 16389
Cdd:COG4733     775 VATAAAIGAEARVAATV 791
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
33898-33984 6.57e-10

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 61.01  E-value: 6.57e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEqqGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:cd05894       2 ENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATE--GRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDH 79

                    ....*..
gi 1958765569 33978 ATVNINI 33984
Cdd:cd05894      80 ASLFVKV 86
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
27801-27870 6.64e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 60.42  E-value: 6.64e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27801 VQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSSTV 27870
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
24544-24624 7.04e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.98  E-value: 7.04e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24544 KGIVVRAGGSARIHIPFKGRPTPEITWSKEEGE---FTDKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFV 24620
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  24621 TVKV 24624
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
22754-22836 7.14e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 7.14e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22754 GPPTGpVKMDEVTADSVTLSWEPPKyDGGSSINNYIVEKRDTSTT---AWQIVSATVARTTIKasRLKTGCEYQFRIAAE 22830
Cdd:pfam00041     1 SAPSN-LTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGepwNEITVPGTTTSVTLT--GLKPGTEYEVRVQAV 76

                    ....*.
gi 1958765569 22831 NRYGKS 22836
Cdd:pfam00041    77 NGGGEG 82
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5705-5787 7.52e-10

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 61.01  E-value: 7.52e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5705 PVLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDglaTFQISNARVENSGTYVCEARNDAGTASCSIE 5784
Cdd:cd20957       9 PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQATAE 85

                    ...
gi 1958765569  5785 LKV 5787
Cdd:cd20957      86 LKL 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8611-8700 7.53e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 60.97  E-value: 7.53e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDS-VAELELFDVDTSQSGDYTCIVSNEA 8689
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  8690 GRASCTTQLFV 8700
Cdd:cd05744      81 GENSFNAELVV 91
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
31761-31972 7.57e-10

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 65.53  E-value: 7.57e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFmakfVKVKGTDQVLV----KKEISILNIARHRNILYLHESFESMEELVMIF 31836
Cdd:cd05148       6 EEFTLERKLGSGYFGEVWEGLWKNRVRVA----IKILKSDDLLKqqdfQKEVQALKRLRHKHLISLFAVCSVGEPVYIIT 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFISGLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKpgDN 31915
Cdd:cd05148      82 ELMEKGSLLAFLRSPEGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNIL--VGEDLVCKVADFGLARLIK--ED 157
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31916 FRLLFTAP---EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIM 31972
Cdd:cd05148     158 VYLSSDKKipyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQIT 218
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7480-7570 7.67e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 61.06  E-value: 7.67e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7480 PARIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSV 7559
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  7560 GKSSCTVSVHV 7570
Cdd:cd20972      81 GSDTTSAEIFV 91
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
31763-32017 7.78e-10

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 66.14  E-value: 7.78e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQV--LVKKEISILNIARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd07870       2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVpfTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 gLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK-PGDNFRLL 31919
Cdd:cd07870      82 -TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE--LKLADFGLARAKSiPSQTYSSE 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FTAPEYYAPEVHQHDV-VSSATDMWSLGTLVYVLLSGiNPFLAETNQ--QMIENIMNAEYTFDEEAFQEIS--------- 31987
Cdd:cd07870     159 VVTLWYRPPDVLLGATdYSSALDIWGAGCIFIEMLQG-QPAFPGVSDvfEQLEKIWTVLGVPTEDTWPGVSklpnykpew 237
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*....
gi 1958765569 31988 -------------------LEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07870     238 flpckpqqlrvvwkrlsrpPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
26706-26786 7.91e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 7.91e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26706 KTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDL---RTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTF 26782
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  26783 VVKV 26786
Cdd:smart00410    82 TLTV 85
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
8247-8325 8.00e-10

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 60.50  E-value: 8.00e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8247 LKGADVHLECELQGTPPFQVSWYKDKRELRSGKkykIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDTCVGSVTLK 8325
Cdd:cd05731       8 LRGGVLLLECIAEGLPTPDIRWIKLGGELPKGR---TKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTVE 83
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
31867-32026 8.02e-10

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 65.91  E-value: 8.02e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31867 VCEALEFLHSQ-NIGHFDIRPENIIyqTRKNSIIKIIEFGQARQL------------KPgdnfrllFTAPEYYAPEVHQ- 31932
Cdd:cd06617     112 IVKALEYLHSKlSVIHRDVKPSNVL--INRNGQVKLCDFGISGYLvdsvaktidagcKP-------YMAPERINPELNQk 182
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31933 -HDVVSsatDMWSLG-------TLVYVLLSGINPFlaetnQQMIENIMNAEYTFDEEAFqeiSLEAMDFIDRLLVKERKS 32004
Cdd:cd06617     183 gYDVKS---DVWSLGitmielaTGRFPYDSWKTPF-----QQLKQVVEEPSPQLPAEKF---SPEFQDFVNKCLKKNYKE 251
                           170       180
                    ....*....|....*....|..
gi 1958765569 32005 RMTASEALKHPWLKQRMDRVST 32026
Cdd:cd06617     252 RPNYPELLQHPFFELHLSKNTD 273
fn3 pfam00041
Fibronectin type III domain;
18810-18894 8.10e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 8.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18810 GPVRNLKIADVSSDRCTIRWDPPEDDGGcEIQNYILEKCESKRM-VWSTYSANVLTPGATVTRLIEGNEYIFRVRAENKI 18888
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 18889 GTGPPT 18894
Cdd:pfam00041    80 GEGPPS 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
18024-18113 8.11e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 61.21  E-value: 8.11e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18024 LDVKLiEGLVVKAGTTVRFPAIIRGVPVPTAKWATDG--TEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAA 18101
Cdd:cd20974       3 FTQPL-QSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|..
gi 1958765569 18102 GTKTVAVHLTVL 18113
Cdd:cd20974      82 GQATSTAELLVL 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
24824-24900 8.11e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 60.66  E-value: 8.11e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATN 24900
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
4577-4661 8.28e-10

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 60.72  E-value: 8.28e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4577 KKVDPSYLMLPGESARLHCKLKGsPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCeatnDAGSDS 4656
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC----VAGGEK 75

                    ....*
gi 1958765569  4657 CSTEV 4661
Cdd:cd20967      76 CSFEL 80
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1044-1127 8.39e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 8.39e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   1044 PVVQKLVEGGSVVFECQIGGNPKPHVYWKKSG-VPLTTGYRYKVSYNKQTGEcrLVIS-MTFaDDAGEYTIVIRNKHGET 1121
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTST--LTISnVTP-EDSGTYTCAATNSSGSA 77

                     ....*.
gi 1958765569   1122 SASASL 1127
Cdd:smart00410    78 SSGTTL 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
27781-27860 8.52e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 60.27  E-value: 8.52e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27781 PEIdldVALRTSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIEN 27860
Cdd:pfam13927     2 PVI---TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
14697-14782 8.59e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 8.59e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14697 GPPYALTVVDVTKRHVDLKWEPPKnDGGRPIQRYIIEKKEKLGTRWVKAGKTSGPDCNFRVTDVIEGTEVQFQVRAENEA 14776
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 14777 GVGHPS 14782
Cdd:pfam00041    80 GEGPPS 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
5987-6066 8.70e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 60.67  E-value: 8.70e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5987 DVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSF-ENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLR 6065
Cdd:cd20973       8 EVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87

                    .
gi 1958765569  6066 V 6066
Cdd:cd20973      88 V 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
5707-5787 8.70e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 60.67  E-value: 8.70e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5707 LVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISF-VDGLATFQISNARVENSGTYVCEARNDAGTASCSIEL 5785
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569  5786 KV 5787
Cdd:cd20973      87 TV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33438-33500 8.73e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 60.04  E-value: 8.73e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 33438 KVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSS 33500
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
6-97 8.83e-10

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 60.94  E-value: 8.83e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTlpgVQISF---SDGRARLMIPAVTKANSGRYSLRA 82
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNT---DRISLyqdNCGRICLLIQNANKKDAGWYTVSA 77
                            90
                    ....*....|....*
gi 1958765569    83 TNGSGQATSTAELLV 97
Cdd:cd05892      78 VNEAGVVSCNARLDV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
29966-30046 8.90e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 8.90e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29966 KTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLA---NRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATV 30042
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  30043 LVKV 30046
Cdd:smart00410    82 TLTV 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4301-4381 8.96e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 60.67  E-value: 8.96e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4301 LEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSI-RSSNYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATL 4379
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569  4380 TV 4381
Cdd:cd20973      87 TV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4573-4664 9.02e-10

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.83  E-value: 9.02e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4573 PSFVKKVDpSYLMLPGESARLHCKLKGSPVIQVTWFKNNK--ELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATN 4650
Cdd:cd20974       1 PVFTQPLQ-SVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569  4651 DAGSDSCSTEVVIK 4664
Cdd:cd20974      80 GSGQATSTAELLVL 93
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
32306-32396 9.08e-10

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 60.73  E-value: 9.08e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDyyALHIRDTLPEDTGYYRVTATNTA 32385
Cdd:cd20976       2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVG--ELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569 32386 GSTSCQAHLQV 32396
Cdd:cd20976      80 GQVSCSAWVTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
20635-20968 9.12e-10

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 68.43  E-value: 9.12e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20635 WVTCASAVQKTTFRVTRLHEGIEYTFRVSA----ENKYGVGEglkSEPIVakhpfDVPDAPPPPNIV----------DVR 20700
Cdd:COG4733     479 WAFGPDELETQLFRVVSIEENEDGTYTITAvqhaPEKYAAID---AGAFD-----DVPPQWPPVNVTtseslsvvaqGTA 550
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20701 HDSVSLTWTDPKKTggspiTGYHIEFKeRNSLLWKRANKTPIRmkDFKVTGLTEGlEYEFRVMAINLAGV-GKPSLPSEP 20779
Cdd:COG4733     551 VTTLTVSWDAPAGA-----VAYEVEWR-RDDGNWVSVPRTSGT--SFEVPGIYAG-DYEVRVRAINALGVsSAWAASSET 621
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20780 VVALDpIDPPGKPEVISVTRN--SVTLIWTEPKYDGghkLTGYIVEKRDLPSKSWMKANHVNVPDCAFTVTDLVEGGKYE 20857
Cdd:COG4733     622 TVTGK-TAPPPAPTGLTATGGlgGITLSWSFPVDAD---TLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYY 697
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20858 FRIRAKNTAGAISAPSESTGTiicKDEYEAPTIVLDPTIKDGLTVKAGDSIvLSAISILGKPLPKSSWSKAGKDIRPSDI 20937
Cdd:COG4733     698 YRARAVDRSGNVSAWWVSGQA---SADAAGILDAITGQILETELGQELDAI-IQNATVAEVVAATVTDVTAQIDTAVLFA 773
                           330       340       350
                    ....*....|....*....|....*....|.
gi 1958765569 20938 AQITSTPTSSMLTVKYATRKDAGEYTITATN 20968
Cdd:COG4733     774 GVATAAAIGAEARVAATVAESATAAAATGTA 804
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6359-6436 9.16e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 9.16e-10
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569   6359 PPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQ-LRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVGSDTC 6436
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
1417-1507 9.36e-10

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 60.94  E-value: 9.36e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDyTHKVVIKEDGT--QSLIIVPALPSDSGEWTVVAQN 1494
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYN-TDRISLYQDNCgrICLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569  1495 RAGKSTISVTLTV 1507
Cdd:cd05892      80 EAGVVSCNARLDV 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7112-7196 9.53e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 60.49  E-value: 9.53e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7112 KPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIrPGGNYTITcvgNTPHLRILKVGKGDSGQYTCQATNDVGKDMCS 7191
Cdd:cd05725       3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL-PKGRYEIL---DDHSLKIRKVTAGDMGSYTCVAENMVGKIEAS 78

                    ....*
gi 1958765569  7192 AQLSV 7196
Cdd:cd05725      79 ATLTV 83
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
31753-31965 9.78e-10

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 66.65  E-value: 9.78e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31753 HSKTKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISIL-----NIARHRNILYLHESFE 31827
Cdd:cd14227       7 HEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILarlstESADDYNFVRAYECFQ 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31828 SMEELVMIFEFISGlDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIEF 31904
Cdd:cd14227      87 HKNHTCLVFEMLEQ-NLYDFLKQNKFSpLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdPSRQPYRVKVIDF 165
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31905 GQARQLKPGDNFRLLfTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSG--INPFLAETNQ 31965
Cdd:cd14227     166 GSASHVSKAVCSTYL-QSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGwpLYPGASEYDQ 227
fn3 pfam00041
Fibronectin type III domain;
29452-29536 9.85e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 9.85e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29452 DPPGRPEVTDVTRSTVSLVWSAPmYDGGSKVVGYIIERKPVSEVGDGRWlkcnYTIVSD-NFFTVTALSEGDTYEFRVLA 29530
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNE----ITVPGTtTSVTLTGLKPGTEYEVRVQA 75

                    ....*.
gi 1958765569 29531 KNAAGI 29536
Cdd:pfam00041    76 VNGGGE 81
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
28568-28647 9.86e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 60.32  E-value: 9.86e-10
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28568 VGPIRFTNITGEKMTLWWEAPLNDGC-APVTHYIIEKRETSRlAWALIEDHCEAQSYTAIKLITGNEYQFRVSAVNKFGV 28646
Cdd:smart00060     4 PSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82

                     .
gi 1958765569  28647 G 28647
Cdd:smart00060    83 G 83
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
27045-27364 9.92e-10

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 68.05  E-value: 9.92e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27045 TINLKESVTADAGKYEITAANSSGTTKTfiniivldrpgpptgpVAISDITEESVTLKWE----PPKYDggshvtnyivl 27120
Cdd:COG4733     425 VVTLDRPVTMEAGDRYLRVRLPDGTSVA----------------RTVQSVAGRTLTVSTAysetPEAGA----------- 477
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27121 kretstaVWTEVSATVARTMIKVMKLTTGEEYQFRIKA----ENRFgisDHIDSacvvvklPYTTPGPPSTPWVSNVTRE 27196
Cdd:COG4733     478 -------VWAFGPDELETQLFRVVSIEENEDGTYTITAvqhaPEKY---AAIDA-------GAFDDVPPQWPPVNVTTSE 540
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27197 S------------ITVGWhEPVSNggsaVIGYHLEMKdRNSILWQkaNKMIIRTTHFKVTTISAGlIYEFRVYAENAAGI 27264
Cdd:COG4733     541 SlsvvaqgtavttLTVSW-DAPAG----AVAYEVEWR-RDDGNWV--SVPRTSGTSFEVPGIYAG-DYEVRVRAINALGV 611
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27265 -GKPSHSSEPVLAIDACEPPRNVRITDISKN-SVNLSWQQPAfdgGSKITGYIVERRDlpDGRWTKASFTNVIETQ--FT 27340
Cdd:COG4733     612 sSAWAASSETTVTGKTAPPPAPTGLTATGGLgGITLSWSFPV---DADTLRTEIRYST--TGDWASATVAQALYPGntYT 686
                           330       340
                    ....*....|....*....|....
gi 1958765569 27341 VSGLTQNSQYEFRVFARNAVGSVS 27364
Cdd:COG4733     687 LAGLKAGQTYYYRARAVDRSGNVS 710
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
27792-27874 1.00e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 60.62  E-value: 1.00e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27792 SVIAKAGEDVQLLIPFKGRPPPTVTWRKDEK-NLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSStV 27870
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRGDKaFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS-L 82

                    ....
gi 1958765569 27871 SVKV 27874
Cdd:cd05894      83 FVKV 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5336-5411 1.00e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.60  E-value: 1.00e-09
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   5336 GGTAAFQATLKGSLPITVTWLKDNDE-ITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSV 5411
Cdd:smart00410     9 GESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8610-8700 1.06e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 60.67  E-value: 1.06e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8610 PPSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAEL---ELFDVDTsqsGDYTCIVS 8686
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLiiaEAFEEDT---GRYSCLAT 77
                            90
                    ....*....|....
gi 1958765569  8687 NEAGRASCTTQLFV 8700
Cdd:cd20972      78 NSVGSDTTSAEIFV 91
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
25914-25996 1.07e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 60.24  E-value: 1.07e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25914 NTFNVKANDQLKIDIPFKGRPQATVAWKKDGQVLRETT-RVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPI 25992
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 25993 TVIV 25996
Cdd:cd05894      83 FVKV 86
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
31769-32014 1.08e-09

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 65.47  E-value: 1.08e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNIL-YLHESFESmEELVMIFEFISGLDIF 31845
Cdd:cd14046      14 LGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNsrILREVMLLSRLNHQHVVrYYQAWIER-ANLYIQMEYCEKSTLR 92
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSAFElNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLK-------------- 31911
Cdd:cd14046      93 DLIDSGLFQ-DTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN--VKIGDFGLATSNKlnvelatqdinkst 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31912 -----PGDNFRLLFTAPEYYAPEVHQHDVVS--SATDMWSLGT----LVYVLLSGINPFlaetnqQMIENIMNAEYTFDE 31980
Cdd:cd14046     170 saalgSSGDLTGNVGTALYVAPEVQSGTKSTynEKVDMYSLGIiffeMCYPFSTGMERV------QILTALRSVSIEFPP 243
                           250       260       270
                    ....*....|....*....|....*....|....
gi 1958765569 31981 EAFQEISLEAMDFIDRLLVKERKSRMTASEALKH 32014
Cdd:cd14046     244 DFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7858-7935 1.12e-09

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 60.42  E-value: 1.12e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7858 FIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVG 7935
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
19411-19487 1.13e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.89  E-value: 1.13e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 19411 PPKILM-PEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAEN 19487
Cdd:pfam13927     1 KPVITVsPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7580-7666 1.15e-09

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 60.28  E-value: 1.15e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7580 IRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSF-ADNVCTLTLSSLEPSDTGAYTCVAANVAGQD 7658
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  7659 ESSALLTV 7666
Cdd:cd20973      81 TCSAELTV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4760-4850 1.16e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.44  E-value: 1.16e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4760 PTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDG--KIKMSFSSGVAVLTISDVQIGLGGKYTCLAENE 4837
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  4838 AGSQTSVGELIVK 4850
Cdd:cd20974      81 SGQATSTAELLVL 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
27975-28056 1.17e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 60.32  E-value: 1.17e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27975 PAPIRDLSMKDSTKTSVVLSWTKPDFDGG-SIITDYLVERKGKGEQAWSHAGISKTCEIEIGQLKEQSVLEFRVSARNEK 28053
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                     ...
gi 1958765569  28054 GQS 28056
Cdd:smart00060    81 GEG 83
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12549-12609 1.18e-09

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 60.33  E-value: 1.18e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 12549 LQCEISKADAPVKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTCDCGTDQTS 12609
Cdd:cd20967      17 LTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCS 77
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
32201-32293 1.20e-09

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 60.50  E-value: 1.20e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDdkKYTFESD-KGLYQLTINSVTTDDDAEYAVVAR 32279
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSD--HYTIQRDlDGTCSLHTTASTLDDDGNYTIMAA 78
                            90
                    ....*....|....
gi 1958765569 32280 NKHGEDSCKAKLTV 32293
Cdd:cd05893      79 NPQGRISCTGRLMV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
31457-31527 1.23e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 59.65  E-value: 1.23e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31457 ATLVCKVTGHPKPIVKWYRQGKEIIADglKYRVQEFKGGYHQLIIASVTDDDATVYQVRATNQ-GGSVSGTA 31527
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPS--SRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSaGGSASASV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
18720-18805 1.28e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.21  E-value: 1.28e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  18720 SGVLTVKAGDTIRLEAGVRGKPFPEVAWTKDkDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAGSFVA 18799
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQ-GGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                     ....*.
gi 1958765569  18800 YATVNV 18805
Cdd:smart00410    80 GTTLTV 85
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
31769-31959 1.30e-09

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 65.06  E-value: 1.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCvetsskkTFMAKFVKVKGTDQ----------VLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14146       2 IGVGGFGKVYRA-------TWKGQEVAVKAARQdpdedikataESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEF 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERI---NTSAFELNEREV-----VSYVRQVCEALEFLHSQN---IGHFDIRPENIIYQTRK------NSIIKI 31901
Cdd:cd14146      75 ARGGTLNRALaaaNAAPGPRRARRIpphilVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKIehddicNKTLKI 154
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31902 IEFGQARQLKPGDNFRLLFTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd14146     155 TDFGLAREWHRTTKMSAAGTY-AWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6172-6255 1.30e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.21  E-value: 1.30e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6172 PERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLE-GSTSFLNLYSVDASKTGQYTCQVTNDVGSDSCT 6250
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRsGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   6251 TMLLV 6255
Cdd:smart00410    81 TTLTV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6728-6818 1.30e-09

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 60.34  E-value: 1.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6728 PPSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGAREL-VKGDRCNIyfEDTVAELELFNIDVSQSGEYTCVVSNN 6806
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTC--EAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  6807 AGQASCTTRLFV 6818
Cdd:cd20976      79 AGQVSCSAWVTV 90
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7386-7489 1.31e-09

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 60.74  E-value: 1.31e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7386 PPRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDKGEvIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKND 7465
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQ-IQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENK 79
                            90       100
                    ....*....|....*....|....
gi 1958765569  7466 AGMRECSALLTvleparIVEKPEP 7489
Cdd:cd05762      80 LGSRQAQVNLT------VVDKPDP 97
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
11643-11719 1.35e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.21  E-value: 1.35e-09
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  11643 SVGSSAIFECLVS-PSTAITTWMKDGSN-IRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLIV 11719
Cdd:smart00410     7 KEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
899-984 1.37e-09

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 60.27  E-value: 1.37e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQI-TFQSGIARLM----IREAFAEDSGRFTCS 973
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgDYVTSDGDVVsyvnISSVRVEDGGEYTCT 80
                            90
                    ....*....|.
gi 1958765569   974 AVNEAGTVSTS 984
Cdd:cd20956      81 ATNDVGSVSHS 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7765-7852 1.38e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 60.51  E-value: 1.38e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7765 FVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPL---SQSPNCGITTTERSSILEILESTIEDYAQYACLIENEA 7841
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|.
gi 1958765569  7842 GQDICEALVSV 7852
Cdd:cd20951      83 GEASSSASVVV 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
33698-33787 1.39e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 60.20  E-value: 1.39e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRN-MYTLEIRNASVSDSGKYTVKAKNFR 33776
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569 33777 GQCSATASLTV 33787
Cdd:cd05744      81 GENSFNAELVV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5246-5313 1.42e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 59.65  E-value: 1.42e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5246 VMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEVGSSTCS 5313
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
31769-31959 1.43e-09

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 64.77  E-value: 1.43e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHrcvetssKKTFMAKFVKVK----GTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd14058       1 VGRGSFGVVC-------KARWRNQIVAVKiiesESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTS--AFELNEREVVSYVRQVCEALEFLHS---QNIGHFDIRPENIIYqTRKNSIIKIIEFGQARQLKP--GDNFR 31917
Cdd:cd14058      74 YNVLHGKepKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLL-TNGGTVLKICDFGTACDISThmTNNKG 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 31918 llfTAPeYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd14058     153 ---SAA-WMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
I-set pfam07679
Immunoglobulin I-set domain;
12530-12601 1.46e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.96  E-value: 1.46e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12530 PYFTGKLQDYTGVEKDEVVLQCEISKADAP-VKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC 12601
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6277-6345 1.46e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 59.65  E-value: 1.46e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6277 ARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCST 6345
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
31765-31968 1.48e-09

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 65.08  E-value: 1.48e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILyLHESFESMEELVMIFEFISGLDI 31844
Cdd:cd14151      12 VGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQA---RQLKPGDNFRLLFT 31921
Cdd:cd14151      91 YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH--EDLTVKIGDFGLAtvkSRWSGSHQFEQLSG 168
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPEV---HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMI 31968
Cdd:cd14151     169 SILWMAPEVirmQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 218
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
31857-32017 1.49e-09

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 65.54  E-value: 1.49e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31857 EREVV---SYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiIKIIEFGQARQLKPGDNF---RLLFTaPEYYAPEV 31930
Cdd:cd14013     116 KRENViikSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQ-FKIIDLGAAADLRIGINYipkEFLLD-PRYAPPEQ 193
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31931 HqhdVVSSAT-------------------------DMWSLGTlvyVLL----------SGINPFLAETNQ---------Q 31966
Cdd:cd14013     194 Y---IMSTQTpsappapvaaalspvlwqmnlpdrfDMYSAGV---ILLqmafpnlrsdSNLIAFNRQLKQcdydlnawrM 267
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31967 MIENIMNAEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14013     268 LVEPRASADLREGFEILDLDDGAGWDLVTKLIRYKPRGRLSASAALAHPYF 318
I-set pfam07679
Immunoglobulin I-set domain;
30658-30736 1.49e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.96  E-value: 1.49e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30658 VFVRQGGVIRLTIPIKGKPFPICKWTKEGQDV--SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVK 30735
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrsSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 30736 V 30736
Cdd:pfam07679    90 V 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7577-7667 1.50e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 60.13  E-value: 1.50e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISS---PKCQPSFADNVCTLTLSSLEPSDTGAYTCVAAN 7653
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSsipGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  7654 VAGQDESSALLTVQ 7667
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
6541-6629 1.51e-09

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 60.20  E-value: 1.51e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6541 VIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNkiSSLKILSVEKEDAGTYTFQVQNNVGK 6620
Cdd:cd20952       1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLEN--GSLQIKGAEKSDTGEYTCVALNLSGE 78

                    ....*....
gi 1958765569  6621 SSCTAVVDV 6629
Cdd:cd20952      79 ATWSAVLDV 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4213-4286 1.54e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 1.54e-09
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   4213 GDTVHLTSSISNAK--EVNWYF-KGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNGKAMTSAKLTV 4286
Cdd:smart00410     9 GESVTLSCEASGSPppEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
19819-19898 1.56e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.06  E-value: 1.56e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19819 VKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTE--GVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:cd20974      12 VLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELL 91

                    ..
gi 1958765569 19897 VL 19898
Cdd:cd20974      92 VL 93
fn3 pfam00041
Fibronectin type III domain;
26001-26085 1.56e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 1.56e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26001 GPPGPIRIDEVSCDNVSISWTPPEYDGGcQISNYIVEKRETTSTT-WQVVSQAVARTSIKIVRLTTGSEYQFRVCAENRY 26079
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 26080 GKSSYS 26085
Cdd:pfam00041    80 GEGPPS 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
9182-9272 1.57e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.06  E-value: 1.57e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9182 PVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSD--RCSFSFASGTAVLELKDTAKADSGDYVCKASNV 9259
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  9260 AGSDTSKCKVTIK 9272
Cdd:cd20974      81 SGQATSTAELLVL 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1038-1116 1.58e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.50  E-value: 1.58e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGecRLVISMTFADDAGEYTIVIRN 1116
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNS--TLTISNVTRSDAGTYTCVASN 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
22670-22749 1.59e-09

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 59.90  E-value: 1.59e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTEN-NSLLTIKEACREDVGHYTVKLTNSAGEATETLNVI 22748
Cdd:cd20973       8 EVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87

                    .
gi 1958765569 22749 V 22749
Cdd:cd20973      88 V 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33076-33162 1.63e-09

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 59.72  E-value: 1.63e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33076 LTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSaRHQVTTAKyksTFEISSVQASDEGNYSVVVENTDGKQE 33155
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDH---SLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569 33156 AQFTLTV 33162
Cdd:cd05725      77 ASATLTV 83
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
31769-32015 1.69e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 64.76  E-value: 1.69e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVH--RCVETSskkTFMA----KFVKVKGTDQVLV----KKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd06630       8 LGTGAFSSCYqaRDVKTG---TLMAvkqvSFCRNSSSEQEEVveaiREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEW 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERI-NTSAFElnEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrKNSIIKIIEFGQARQLKP----G 31913
Cdd:cd06630      85 MAGGSVASLLsKYGAFS--ENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDS-TGQRLRIADFGAAARLASkgtgA 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31914 DNFR--LLFTApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQ---QMIENIMNAEYTFDEEafQEISL 31988
Cdd:cd06630     162 GEFQgqLLGTI-AFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISnhlALIFKIASATTPPPIP--EHLSP 238
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31989 EAMDFIDRLLVKERKSRMTASEALKHP 32015
Cdd:cd06630     239 GLRDVTLRCLELQPEDRPPARELLKHP 265
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
5976-6056 1.70e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 60.06  E-value: 1.70e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5976 PAQIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDF 6055
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    .
gi 1958765569  6056 G 6056
Cdd:cd05747      83 G 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6729-6818 1.74e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 59.82  E-value: 1.74e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6729 PSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFEDT-VAELELFNIDVSQSGEYTCVVSNNA 6807
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  6808 GQASCTTRLFV 6818
Cdd:cd05744      81 GENSFNAELVV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28480-28560 1.76e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 1.76e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDGVE-IERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEITV 28558
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  28559 KV 28560
Cdd:smart00410    84 TV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5798-5878 1.78e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 1.78e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5798 EPVEVVKDSDVELECEVMGTTPFEVTWLKNN-KEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANEGGSCACTA 5876
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ..
gi 1958765569   5877 RV 5878
Cdd:smart00410    82 TL 83
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
9293-9380 1.78e-09

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 59.72  E-value: 1.78e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9293 VSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKgkwrqlnQGGRILI---HQKGDESkLEIRDTTKTDSGLYRCVAFNKH 9369
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRK-------EDGELPKgryEILDDHS-LKIRKVTAGDMGSYTCVAENMV 72
                            90
                    ....*....|.
gi 1958765569  9370 GEIESNVNLQV 9380
Cdd:cd05725      73 GKIEASATLTV 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5511-5601 1.79e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 60.13  E-value: 1.79e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASD---KYKFSFHDNTAFLEISQLEGTDSGTYTCSATN 5587
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  5588 KAGHSQCSGHLTVK 5601
Cdd:cd20951      81 IHGEASSSASVVVE 94
PTZ00121 PTZ00121
MAEBL; Provisional
10032-10560 1.83e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 1.83e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10032 RRMEEEKV--QVTKVPEVSKKIVPQKPSRTPVQEEII----EVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKK 10105
Cdd:PTZ00121   1218 RKAEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIrkfeEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10106 TvtEEKIHVAVSKKIEPPPKVPEPPKKPVPEEVVPVPIPKKVEPPAVKVPEAPKKPVPEEKKPVPIPKKEPAA------- 10178
Cdd:PTZ00121   1298 A--EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekkkee 1375
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10179 PPKVPEAPKKPAPEEKTAVPVAKKKEAPPPKVTEVQKKVVTEEKITIIPQREESPPPAvpEIPKKKVPEEKRP--VPRKE 10256
Cdd:PTZ00121   1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKAdeAKKKA 1453
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10257 EVPPPKAPPKKPVPEEVVPVPIPKKAPP--RAEVSKKTVVEEKKFAAEERLSMAVPQRVELMRHEEEEWTYSEEEEqvsv 10334
Cdd:PTZ00121   1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---- 1529
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10335 svyreEERDEEEAEITEYEVLEEPEEYVVEEKLHVISKRVEVEPAKVPEKHEKKIIPRPKVPAKIEEPPPTKVPEPPKKm 10414
Cdd:PTZ00121   1530 -----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE- 1603
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10415 vPEKKVPAPPPKKVPPAKAPEEPKKPVPERRVPAEVVEIEEPPPTKvTEKHMKITQEEKVLVAVTKKEEPPRARVPEEPK 10494
Cdd:PTZ00121   1604 -EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 10495 KVVPEEKFPKLKPRREEEPPAKVTEVRKRAVKEEKVSIEVPKREprPTKEVTVTEEKKwsytREEE 10560
Cdd:PTZ00121   1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE--EENKIKAEEAKK----EAEE 1741
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
1249-1337 1.84e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.06  E-value: 1.84e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRI--RRGERYQMDFlQDGRASLRIPVVLPEDEGIYTAFASNIK 1326
Cdd:cd20974       3 FTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIstSTLPGVQISF-SDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|.
gi 1958765569  1327 GNAICSGKLYV 1337
Cdd:cd20974      82 GQATSTAELLV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7010-7087 1.84e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.50  E-value: 1.84e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7010 PPSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASN 7087
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8808-8886 1.87e-09

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 59.72  E-value: 1.87e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8808 VTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKnnvaTLVFTQVDSNDSGEYICRAENSVGEVSSSTFLTV 8886
Cdd:cd05725       9 VLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILDDH----SLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
902-989 1.91e-09

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 59.82  E-value: 1.91e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   902 LVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIarLMIREAFAEDSGRFTCSAVNEAGTV 981
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENGS--LQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569   982 STSCYLAV 989
Cdd:cd20952      80 TWSAVLDV 87
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5791-5881 1.92e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 60.13  E-value: 1.92e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5791 PIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRS---GKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIAN 5867
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  5868 EGGSCACTARVALK 5881
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
19804-19905 1.92e-09

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 59.97  E-value: 1.92e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19804 PPRI-ELSVEMKslltVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITA 19882
Cdd:cd05762       1 PPQIiQFPEDMK----VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEV 76
                            90       100
                    ....*....|....*....|...
gi 1958765569 19883 ENSSGSKSATIKLKVLDKPGPPA 19905
Cdd:cd05762      77 ENKLGSRQAQVNLTVVDKPDPPA 99
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
23064-23146 1.93e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.06  E-value: 1.93e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23064 TVVVQAGESFKIDADIYGKPIPTTQWVKGDQ--ELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTV 23141
Cdd:cd20974       9 SVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTA 88

                    ....*
gi 1958765569 23142 NVKVL 23146
Cdd:cd20974      89 ELLVL 93
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4949-5038 1.95e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.06  E-value: 1.95e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASD--RYQIAFVEGTASLEISRVDMNDAGNFTCRATNS 5026
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  5027 VGSKDSRGALIV 5038
Cdd:cd20974      81 SGQATSTAELLV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1417-1507 1.99e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 59.90  E-value: 1.99e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKvVIKEDGTQSLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQ-IHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1249-1338 2.01e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 59.74  E-value: 2.01e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRR---GERYQMdFLQDGRASLRIPVVLPEDEGIYTAFASNI 1325
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKI-ESEYGVHVLHIRRVTVEDSAVYSAVAKNI 81
                            90
                    ....*....|...
gi 1958765569  1326 KGNAICSGKLYVE 1338
Cdd:cd20951      82 HGEASSSASVVVE 94
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
8052-8141 2.02e-09

Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 409440  Cd Length: 102  Bit Score: 60.06  E-value: 2.02e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8052 LKPVSVDLALGESGSFKCHVTG--TAPIKITWAKDNREI---RPGGNYKMTLVENT-ATLTVLKVAKGDAGQYTCYASNV 8125
Cdd:cd05854       7 LAPSSADINQGENLTLQCHASHdpTMDLTFTWSLDDFPIdldKPNGHYRRMEVKETiGDLVIVNAQLSHAGTYTCTAQTV 86
                            90
                    ....*....|....*.
gi 1958765569  8126 AGKDSCSAQLGVQEPP 8141
Cdd:cd05854      87 VDSASASATLVVRGPP 102
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8532-8607 2.03e-09

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 59.82  E-value: 2.03e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8532 GSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTcaLTVNMLEDADAGDYTCIATNVAGSDECSAPLTV 8607
Cdd:cd20952      14 GGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENGS--LQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
19412-19501 2.05e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 60.06  E-value: 2.05e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19412 PKILMPEQ-ITIKAGKKLRVEAHVYGKPNPICKWKKGED--DVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENS 19488
Cdd:cd20974       1 PVFTQPLQsVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 19489 SGTDTQKIKVTVM 19501
Cdd:cd20974      81 SGQATSTAELLVL 93
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
14212-14292 2.12e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 59.47  E-value: 2.12e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14212 LTVKAGTKIELPATVTGKPEPKITWTKADTLLR-PDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEV 14290
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTaTEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 14291 NV 14292
Cdd:cd05894      85 KV 86
I-set pfam07679
Immunoglobulin I-set domain;
23462-23540 2.14e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.58  E-value: 2.14e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23462 KVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSS--FTSLVLDNVNRYDSGKYTLTLENSSG--TKSAF 23537
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEggTYTLTISNVQPDDSGKYTCVATNSAGeaEASAE 87

                    ...
gi 1958765569 23538 VTV 23540
Cdd:pfam07679    88 LTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1516-1607 2.16e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 59.82  E-value: 2.16e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKyPRIRIEGTKGEAALKIDSTISQDSAWYTATAINK 1595
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDS-AHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569  1596 AGRDTTRCKVNI 1607
Cdd:cd05744      80 AGENSFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
2582-2664 2.16e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.58  E-value: 2.16e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2582 ISKPLTDQTVAESQEAVFECEV-ANPESEGEWLKDGKHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYTYKVATS---- 2656
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVtGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSagea 82

                    ....*...
gi 1958765569  2657 KTSAKLKV 2664
Cdd:pfam07679    83 EASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
20397-20479 2.17e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.17e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20397 GPVVDLKVLAVTKSSCTIGWKKPRsDGGSRITGYVVDF--LTEENKWQRVMKSLSL-QYSTKDLKEGKEYTFRVSAENEN 20473
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYrpKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 20474 GEGTPS 20479
Cdd:pfam00041    80 GEGPPS 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8235-8318 2.18e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 59.82  E-value: 2.18e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIM-SENLLTSIHILNVDTADIGEYQCKATNDV 8313
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLvRENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                    ....*
gi 1958765569  8314 GSDTC 8318
Cdd:cd05744      81 GENSF 85
fn3 pfam00041
Fibronectin type III domain;
16425-16508 2.21e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.21e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16425 GPPKDLKVSDITRGSCRLSWKMPDDDGGDrIKGYVIEKKTID-GKAWTKVNPNCGSTAFVVPDLISEQQYFFRVRAENRF 16503
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 16504 GIGPP 16508
Cdd:pfam00041    80 GEGPP 84
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12887-12958 2.22e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 59.74  E-value: 2.22e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12887 EFLRPLTDLQVKEKETARFECEIS-KENVKVQWFKDGAEI---KKGKKYDIISKGAVRILVINKCLLNDEAEYSCE 12958
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAV 77
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
33891-33984 2.25e-09

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 59.97  E-value: 2.25e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPSDISIAEGKVLTVACAFTGEPTPEITWScgGRRIQSQEQQGrFHIENTDDLTTLIIMDVQKQDGGLYTLSLG 33970
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWM--KFRKQIQEGEG-IKIENTENSSKLTITEGQQEHCGCYTLEVE 77
                            90
                    ....*....|....
gi 1958765569 33971 NEFGSDSATVNINI 33984
Cdd:cd05762      78 NKLGSRQAQVNLTV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
28479-28560 2.26e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 59.67  E-value: 2.26e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28479 GLVIKSGDSLRIKALVQGRPVPRVTWFKDG--VEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEI 28556
Cdd:cd20974       9 SVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTA 88

                    ....
gi 1958765569 28557 TVKV 28560
Cdd:cd20974      89 ELLV 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
33700-33787 2.35e-09

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 59.43  E-value: 2.35e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33700 FISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRsrNMYTLEIRNASVSDSGKYTVKAKNFRGQC 33779
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTL--ENGSLQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569 33780 SATASLTV 33787
Cdd:cd20952      80 TWSAVLDV 87
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
13918-13996 2.36e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 59.47  E-value: 2.36e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13918 VIVPNPIKILVPSTGYPRPKATWTFGDQVLEAGD-RVKIKTISAYAELIISPSERPDKGIYTLTLENPVKSISGEIDVNV 13996
Cdd:cd05894       7 VVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
17738-17818 2.38e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.44  E-value: 2.38e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17738 REQHIKVGDTLRLSAIIKGVPFPKVTWKKEDRE---APTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSV 17814
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  17815 KVLV 17818
Cdd:smart00410    82 TLTV 85
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4387-4476 2.40e-09

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 59.73  E-value: 2.40e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNK-HSLELSNLTVQDRGVYSCKASNKF 4465
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGvHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  4466 GADICQAELTI 4476
Cdd:cd20990      81 GQNSFNLELVV 91
fn3 pfam00041
Fibronectin type III domain;
31338-31423 2.42e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.42e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31338 SVPGKPTITAVTKDSCVVAWKPPaSDGGAKIRNYYLEKREKKQNKWIAVTTEEIRETVFSVQNLIEGLEYEFRVKCENLG 31417
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 31418 GESEWS 31423
Cdd:pfam00041    80 GEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
32111-32170 2.45e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.58  E-value: 2.45e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32111 QVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 32170
Cdd:pfam07679    31 EVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4759-4836 2.47e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.12  E-value: 2.47e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4759 PPTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAEN 4836
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
31767-31971 2.55e-09

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 63.80  E-value: 2.55e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFG--------------IVHRCVETSSKKtFMAKFVKvkgtdqvlvkkEISILNIARHRNILYLHESFESMEEL 31832
Cdd:cd05084       2 ERIGRGNFGevfsgrlradntpvAVKSCRETLPPD-LKAKFLQ-----------EARILKQYSHPNIVRLIGVCTQKQPI 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31833 VMIFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNsIIKIIEFGQARQLKP 31912
Cdd:cd05084      70 YIVMELVQGGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLV-TEKN-VLKISDFGMSREEED 147
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31913 GdnfrlLFTAP--------EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05084     148 G-----VYAATggmkqipvKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAV 210
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7580-7666 2.55e-09

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 59.33  E-value: 2.55e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7580 IRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIissPKCQPS-FADNvcTLTLSSLEPSDTGAYTCVAANVAGQD 7658
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL---PKGRYEiLDDH--SLKIRKVTAGDMGSYTCVAENMVGKI 75

                    ....*...
gi 1958765569  7659 ESSALLTV 7666
Cdd:cd05725      76 EASATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
12976-13047 2.57e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.12  E-value: 2.57e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12976 VFTKNLANLEVSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCR 13047
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATgSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
fn3 pfam00041
Fibronectin type III domain;
30751-30825 2.59e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.59e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 30751 DIQTRSVRVSWRPPaDDGGADILGYILERREV---PKAAWYTIDSRVrgTSLVVKGLKENVEYHFRVSAENQFGISKP 30825
Cdd:pfam00041    10 DVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnsgEPWNEITVPGTT--TSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
24034-24120 2.61e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.61e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24034 DPPGTPEAIIVKRNEITLQWTKPVyDGGSMITGYIVEKRDLPEGRWMKASFTNVIETQFTVSGLTEDQRYEFRVIAKNAA 24113
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*..
gi 1958765569 24114 GaISKPS 24120
Cdd:pfam00041    80 G-EGPPS 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
1516-1607 2.64e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 59.67  E-value: 2.64e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGTKGEAALKIDSTISQDSAWYTATAINK 1595
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  1596 AGRDTTRCKVNI 1607
Cdd:cd20974      81 SGQATSTAELLV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9292-9380 2.65e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 59.43  E-value: 2.65e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTK-GKWRQLNQGGRILIHQKGDESkLEIRDTTKTDSGLYRCVAFNKHG 9370
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLnGKPVRPDSAHKMLVRENGRHS-LIIEPVTKRDAGIYTCIARNRAG 81
                            90
                    ....*....|
gi 1958765569  9371 EIESNVNLQV 9380
Cdd:cd05744      82 ENSFNAELVV 91
fn3 pfam00041
Fibronectin type III domain;
20787-20873 2.66e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 2.66e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20787 DPPGKPEVISVTRNSVTLIWTEPKYDGGHkLTGYIVEKRDLPSKSWMkaNHVNVPD--CAFTVTDLVEGGKYEFRIRAKN 20864
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEPW--NEITVPGttTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*....
gi 1958765569 20865 TAGaISAPS 20873
Cdd:pfam00041    78 GGG-EGPPS 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
23753-23829 2.70e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 59.08  E-value: 2.70e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 23753 VQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTT-RINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIEI 23829
Cdd:cd05894       7 VVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
16332-16421 2.71e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 59.67  E-value: 2.71e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16332 LICKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKAMKdgihdIPEdAQLETAENSSVIVIPECTRAHSGKYSITAKNKAGQ 16411
Cdd:cd20974      10 VVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTST-----LPG-VQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQ 83
                            90
                    ....*....|
gi 1958765569 16412 KTANCRVKVM 16421
Cdd:cd20974      84 ATSTAELLVL 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6654-6715 2.74e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 58.88  E-value: 2.74e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  6654 VLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAG 6715
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1417-1508 2.75e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 59.36  E-value: 2.75e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVI--KEDGTQSLIIVPALPSDSGEWTVVAQN 1494
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKieSEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  1495 RAGKSTISVTLTVE 1508
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1417-1507 2.75e-09

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 59.34  E-value: 2.75e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKE-DGTQSLIIVPALPSDSGEWTVVAQNR 1495
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  1496 AGKSTISVTLTV 1507
Cdd:cd05893      81 QGRISCTGRLMV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7498-7563 2.76e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 58.88  E-value: 2.76e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7498 FTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGKSS 7563
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
31761-31959 2.80e-09

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 64.07  E-value: 2.80e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAE-DLGRGEFGIVHRCVETSSKKTFMAKFVKVKgtdqVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd13991       5 VHWATHQlRIGRGSFGEVHRMEDKQTGFQCAVKKVRLE----VFRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLK 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSIIKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd13991      81 EGGSLGQLIKEQG-CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLL-SSDGSDAFLCDFGHAECLDPDGLGKSL 158
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569 31920 FTAPE------YYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd13991     159 FTGDYipgtetHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
18430-18511 2.82e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 59.67  E-value: 2.82e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18430 ITVRVGQTIRILARVKGRPEPDITWSKEGKV--LVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:cd20974      10 VVVLEGSTATFEAHVSGKPVPEVSWFRDGQVisTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAE 89

                    ....
gi 1958765569 18508 VNVL 18511
Cdd:cd20974      90 LLVL 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1416-1494 2.86e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.12  E-value: 2.86e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  1416 KPVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIkEDGTQSLIIVPALPSDSGEWTVVAQN 1494
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSL-SGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
32885-32975 2.86e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 59.52  E-value: 2.86e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32885 APRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNYK 32964
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569 32965 GEASDYATLDV 32975
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
17044-17124 2.90e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 59.08  E-value: 2.90e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17044 DRIVVHAGGVIRIIAYVSGKPPPTVTWNMNERALPQ---EATIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTI 17120
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTAtegRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 17121 IVDV 17124
Cdd:cd05894      83 FVKV 86
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5424-5504 2.98e-09

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 59.14  E-value: 2.98e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5424 IDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGrsSCKASIN 5503
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG--EKSATIN 79

                    .
gi 1958765569  5504 V 5504
Cdd:cd05748      80 V 80
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
19411-19507 2.98e-09

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 59.58  E-value: 2.98e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19411 PPKIL-MPEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSS 19489
Cdd:cd05762       1 PPQIIqFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*...
gi 1958765569 19490 GTDTQKIKVTVMDAPGPP 19507
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPP 98
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
33697-33787 2.99e-09

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 2.99e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33697 APSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRnMYTLEIRNASVSDSGKYTVKAKNFR 33776
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAG-VGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569 33777 GQCSATASLTV 33787
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
33898-33984 3.01e-09

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 59.17  E-value: 3.01e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENTDDLttLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:cd05763       6 PHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARERRMHVMPEDDV--FFIVDVKIEDTGVYSCTAQNSAGSIS 83

                    ....*..
gi 1958765569 33978 ATVNINI 33984
Cdd:cd05763      84 ANATLTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7386-7464 3.06e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.73  E-value: 3.06e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7386 PPRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDkGEVIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKN 7464
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKN-GEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1516-1608 3.09e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 59.36  E-value: 3.09e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRI-RIEGTKGEAALKIDSTISQDSAWYTATAIN 1594
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKyKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  1595 KAGRDTTRCKVNIE 1608
Cdd:cd20951      81 IHGEASSSASVVVE 94
I-set pfam07679
Immunoglobulin I-set domain;
20213-20295 3.22e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 3.22e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20213 KTLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIV 20292
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 20293 VKV 20295
Cdd:pfam07679    88 LTV 90
fn3 pfam00041
Fibronectin type III domain;
25315-25399 3.27e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 3.27e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25315 GPPEGpLKVTGVTAEKCYLAWNPPLqDGGASISHYIIEKRETSRLS-WTQVSTEVQALNYKVTKLLPGNEYIFRVMAVNK 25393
Cdd:pfam00041     1 SAPSN-LTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 25394 YGVGEP 25399
Cdd:pfam00041    79 GGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
15521-15597 3.27e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 3.27e-09
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  15521 RVADTSSTTIELEWEPPAF-NGGGEIMGYFVDKQLVGTnEWSRCTEKmVKVRQFTVKEIREGADYKLRVSAVNAAGEG 15597
Cdd:smart00060     8 RVTDVTSTSVTLSWEPPPDdGITGYIVGYRVEYREEGS-EWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
14396-14481 3.30e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 3.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14396 GPPTRLEPSDITKDAVTLTWcEPDDDGGSPITGYWVERLDPDT-DKWVRCNKMPVKdTTYRVKGLTNKKKYRFRVLAENL 14474
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSgEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 14475 AGPGKPS 14481
Cdd:pfam00041    79 GGEGPPS 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3577-3667 3.34e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 59.36  E-value: 3.34e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPL--YTNVCYTIIHNPDGSGTFIVNDPQRGDSGLYICKAEN 3654
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569  3655 LWGTSTCTAELLV 3667
Cdd:cd20951      81 IHGEASSSASVVV 93
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
31765-31971 3.35e-09

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 63.74  E-value: 3.35e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVH--RCVETSSKKTFMA-KFVKVKGTDQVLVK--KEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05065       8 IEEVIGAGEFGEVCrgRLKLPGKREIFVAiKTLKSGYTEKQRRDflSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFM 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 S--GLDIFERINTSAFELneREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLK-----P 31912
Cdd:cd05065      88 EngALDSFLRQNDGQFTV--IQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNS--NLVCKVSDFGLSRFLEddtsdP 163
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31913 GDNFRLLFTAP-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05065     164 TYTSSLGGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQDVINAI 224
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
19804-19884 3.38e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.73  E-value: 3.38e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19804 PPRIELSvemKSLLTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAE 19883
Cdd:pfam13927     1 KPVITVS---PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 19884 N 19884
Cdd:pfam13927    78 N 78
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30856-31045 3.38e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.18  E-value: 3.38e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30856 SSVSLSWSRPKDDGGSRVTGYYIERKETSTDKWVRHNKTQITTTMYTVTgLVPDAEYQFRIIAQNDVGlseTSPASEPVV 30935
Cdd:COG3401     150 VDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGD-IEPGTTYYYRVAATDTGG---ESAPSNEVS 225
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30936 CKDPFDKPSQPGELEILSISKDSVILQWEKPECDGgkeILGYWVEYRQSGDSAWKKSNKerIKDRQFTIGGLLEATEYEF 31015
Cdd:COG3401     226 VTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYY 300
                           170       180       190
                    ....*....|....*....|....*....|
gi 1958765569 31016 RVFAENETGLSRPRRTAMSVKTKLTSGEAP 31045
Cdd:COG3401     301 RVTAVDAAGNESAPSNVVSVTTDLTPPAAP 330
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
33698-33787 3.42e-09

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 59.01  E-value: 3.42e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNN--LPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNF 33775
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNemLQYNTDRISLYQDNCGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569 33776 RGQCSATASLTV 33787
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6539-6625 3.44e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 59.13  E-value: 3.44e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6539 PAVIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNV 6618
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....*..
gi 1958765569  6619 GKSSCTA 6625
Cdd:cd20972      81 GSDTTSA 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
24146-24228 3.57e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 59.29  E-value: 3.57e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24146 TIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESA--RCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPV 24223
Cdd:cd20974       9 SVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTA 88

                    ....*
gi 1958765569 24224 NVKVL 24228
Cdd:cd20974      89 ELLVL 93
I-set pfam07679
Immunoglobulin I-set domain;
12887-12959 3.62e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 3.62e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 12887 EFLRPLTDLQVKEKETARFECEIS-KENVKVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEV 12959
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVA 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
20504-20584 3.63e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.06  E-value: 3.63e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20504 YLAKENSNFRLKIPIKGKPAPSVSWKK-GEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSI 20582
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  20583 KV 20584
Cdd:smart00410    84 TV 85
fn3 pfam00041
Fibronectin type III domain;
27083-27165 3.64e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 3.64e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27083 GPPTGPVAiSDITEESVTLKWEPPKyDGGSHVTNYIVLKRET-STAVWTEVSATVARTMIKVMKLTTGEEYQFRIKAENR 27161
Cdd:pfam00041     1 SAPSNLTV-TDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....
gi 1958765569 27162 FGIS 27165
Cdd:pfam00041    79 GGEG 82
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
31767-32014 3.66e-09

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 63.66  E-value: 3.66e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDqvlVKKEISILNIARHRNILYLHESFE---------------SMEE 31831
Cdd:cd14047      12 ELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEK---AEREVKALAKLDHPNIVRYNGCWDgfdydpetsssnssrSKTK 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMI-FEFISGLDIFERINTSAFELNER-EVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQ 31909
Cdd:cd14047      89 CLFIqMEFCEKGTLESWIEKRNGEKLDKvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK--VKIGDFGLVTS 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LK-PGDNFRLLFTaPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETnqQMIENIMNAEYT--FDEEAFQEI 31986
Cdd:cd14047     167 LKnDGKRTKSKGT-LSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKS--KFWTDLRNGILPdiFDKRYKIEK 243
                           250       260
                    ....*....|....*....|....*...
gi 1958765569 31987 SleamdFIDRLLVKERKSRMTASEALKH 32014
Cdd:cd14047     244 T-----IIKKMLSKKPEDRPNASEILRT 266
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
9181-9271 3.66e-09

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 3.66e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9181 PPVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREI-KPSDRcsFSFASGTAVLELKDTAKADSGDYVCKASNV 9259
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADR--STCEAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  9260 AGSDTSKCKVTI 9271
Cdd:cd20976      79 AGQVSCSAWVTV 90
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
31769-31905 3.78e-09

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 60.53  E-value: 3.78e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGT-DQVLVKKEISILNIAR--HRNILYLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd13968       1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNeEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSafELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFG 31905
Cdd:cd13968      81 AYTQEE--ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGN--VKLIDFG 136
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
26707-26966 3.82e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 66.12  E-value: 3.82e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26707 TLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIdstdsrtsltIENANRNDSGKYTLT-IQNV-----LSAASM 26780
Cdd:COG4733     454 TVQSVAGRTLTVSTAYSETPEAGAVWAFGPDELETQLFR----------VVSIEENEDGTYTITaVQHApekyaAIDAGA 523
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26781 TFVVKVLDspgPPANITVREVT--------KETAVLSWDVPENDGGapvknYHIEKREASKkAWVSVTNNcSRLSYKVTN 26852
Cdd:COG4733     524 FDDVPPQW---PPVNVTTSESLsvvaqgtaVTTLTVSWDAPAGAVA-----YEVEWRRDDG-NWVSVPRT-SGTSFEVPG 593
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26853 LQEGaVYYFRVSGENEFGVGVPAETKEGVKITEKPSPPEK-LGVTSVSKD-SVSLSWLKPEhdgGSRILHYVVEALEKGq 26930
Cdd:COG4733     594 IYAG-DYEVRVRAINALGVSSAWAASSETTVTGKTAPPPApTGLTATGGLgGITLSWSFPV---DADTLRTEIRYSTTG- 668
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|
gi 1958765569 26931 kNW----VKCAVVKTTHHVVSGLREGHEYFFRVFAENQAG 26966
Cdd:COG4733     669 -DWasatVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
9292-9367 3.83e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.73  E-value: 3.83e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFN 9367
Cdd:pfam13927     4 ITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNG-EPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
4588-4656 3.85e-09

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 59.17  E-value: 3.85e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNN-KELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDS 4656
Cdd:cd05763      14 GSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSIS 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5423-5504 3.88e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.67  E-value: 3.88e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5423 SIDVTQGDPATLQVKFSGTKEISAKWFKDGQE-LTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKAS 5501
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   5502 INV 5504
Cdd:smart00410    83 LTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7951-8028 3.91e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.73  E-value: 3.91e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7951 PPSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASN 8028
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
19128-19207 4.03e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 58.81  E-value: 4.03e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGID-NVVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVK 19206
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPlRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 19207 V 19207
Cdd:pfam07679    90 V 90
fn3 pfam00041
Fibronectin type III domain;
13603-13687 4.09e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 4.09e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13603 GPVRNLEVTETFDGEVSLAWEEPlTDGGSKIIGYVVERRDIKR-KTWVLVTDRADSCEFTVTGLQKGgVEYLFRVSARNR 13681
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPG-TEYEVRVQAVNG 78

                    ....*.
gi 1958765569 13682 VGTGEP 13687
Cdd:pfam00041    79 GGEGPP 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
9084-9162 4.10e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.35  E-value: 4.10e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9084 PPSFTKKLSETIEEtEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATN 9162
Cdd:pfam13927     1 KPVITVSPSSVTVR-EGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
6-97 4.11e-09

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 59.06  E-value: 4.11e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQS--VVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTstlpGVQ--ISFSDGRArLMIPAVTKANSGRYSLR 81
Cdd:cd20970       1 PVISTPQPSftVTAREGENATFMCRAEGSPEPEISWTRNGNLIIE----FNTryIVRENGTT-LTIRNIRRSDMGIYLCI 75
                            90
                    ....*....|....*.
gi 1958765569    82 ATNGSGQATSTAELLV 97
Cdd:cd20970      76 ASNGVPGSVEKRITLQ 91
I-set pfam07679
Immunoglobulin I-set domain;
13153-13241 4.11e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 58.81  E-value: 4.11e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13153 RIVVPLKDTKVKEQQEAVFNCEVntEGA---KAKWFRNDEAIFDSSKYIILQKDLVYTLRIRDARLDDQANFSVSLTNHR 13229
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTV--TGTpdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                            90
                    ....*....|..
gi 1958765569 13230 GEnVKSAANLIV 13241
Cdd:pfam07679    80 GE-AEASAELTV 90
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
14207-14292 4.14e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 58.94  E-value: 4.14e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14207 KLLAGLTVKAGTKIELPATVTGKPEPKITWT-KADTLLRPDQRITIEnvpkKSTVTITDSKRSDTGTYIIEAVNVCGRAT 14285
Cdd:cd20978       6 KPEKNVVVKGGQDVTLPCQVTGVPQPKITWLhNGKPLQGPMERATVE----DGTLTIINVQPEDTGYYGCVATNEIGDIY 81

                    ....*..
gi 1958765569 14286 AVVEVNV 14292
Cdd:cd20978      82 TETLLHV 88
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
27398-27474 4.20e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 58.70  E-value: 4.20e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 27398 AGTSVKLRAGISGKPEPTIEWYKDDKEL-QTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRVQI 27474
Cdd:cd05894       9 AGNKLRLDVPISGEPAPTVTWSRGDKAFtATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
31769-31959 4.20e-09

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 63.47  E-value: 4.20e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVetsskktFMAKFVKVKGTDQ----------VLVKKEISILNIARHRNILYLHESFESMEELVMIFEF 31838
Cdd:cd14148       2 IGVGGFGKVYKGL-------WRGEEVAVKAARQdpdediavtaENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEY 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERIntSAFELNEREVVSYVRQVCEALEFLHSQN---IGHFDIRPENIIYQTR------KNSIIKIIEFGQARQ 31909
Cdd:cd14148      75 ARGGALNRAL--AGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPienddlSGKTLKITDFGLARE 152
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31910 LKPGDNFRLLFTAPeYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd14148     153 WHKTTKMSAAGTYA-WMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
5986-6066 4.33e-09

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 58.77  E-value: 4.33e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5986 VDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFEN-NVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYL 6064
Cdd:cd05891      11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTV 90

                    ..
gi 1958765569  6065 RV 6066
Cdd:cd05891      91 SV 92
fn3 pfam00041
Fibronectin type III domain;
28962-29045 4.34e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 4.34e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28962 GPPGPITFKDVTRGSATLMWDAPLlDGGARIHHYVIEKREASR-RSWQVVSEKCTRQILKVSDLTEGVPYYFRVSAENEY 29040
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 29041 GVGEP 29045
Cdd:pfam00041    80 GEGPP 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9581-9665 4.36e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 58.66  E-value: 4.36e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9581 PAWERHLQDVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKPQGRVKTEV-EHKVHKLTIADVRAEDQGRYTC----KH 9654
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSgLPTPDLFWQLNGKPVRPDSAHKMLVrENGRHSLIIEPVTKRDAGIYTCiarnRA 80
                            90
                    ....*....|.
gi 1958765569  9655 EDLETSAELRI 9665
Cdd:cd05744      81 GENSFNAELVV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4777-4843 4.38e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 58.11  E-value: 4.38e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4777 VTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEAGSQTS 4843
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7199-7290 4.40e-09

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 59.11  E-value: 4.40e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7199 PPKFIKKLdTSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMS-FVNS----VALLTINEASVEDTGDYIC 7273
Cdd:cd20956       1 APVLLETF-SEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGdYVTSdgdvVSYVNISSVRVEDGGEYTC 79
                            90
                    ....*....|....*..
gi 1958765569  7274 EAHNGVGHASCSTALKV 7290
Cdd:cd20956      80 TATNDVGSVSHSARINV 96
fn3 pfam00041
Fibronectin type III domain;
23936-24021 4.43e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 4.43e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23936 GPPGTPFVTAVSKDSMVVQWHEPiNNGGSPVIGYHLERKERNSILWTKVNKTIIHDTQFKALNLEEGIEYEFRVYAENIV 24015
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 24016 GVGKAS 24021
Cdd:pfam00041    80 GEGPPS 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3310-3391 4.44e-09

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 58.74  E-value: 4.44e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3310 PLQDAVTSEGRPARFQCQVSG-TDLKVSWYCRDKKIKPSRFFRMTQFEDTY-QLEIAEAFPEDEGTYAFVANNAVGQVSS 3387
Cdd:cd20973       3 TLRDKEVVEGSAARFDCKVEGyPDPEVKWMKDDNPIVESRRFQIDQDEDGLcSLIISDVCGDDSGKYTCKAVNSLGEATC 82

                    ....
gi 1958765569  3388 TATL 3391
Cdd:cd20973      83 SAEL 86
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
24546-24624 4.54e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 58.70  E-value: 4.54e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24546 IVVRAGGSARIHIPFKGRPTPEITWSKEEGEFTD---KVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTV 24622
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTAtegRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 24623 KV 24624
Cdd:cd05894      85 KV 86
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
1254-1337 4.54e-09

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 58.80  E-value: 4.54e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1254 KNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRR-GERYQMDflqDGRASLRIPVVLPEDEGIYTAFASNIKGNAICS 1332
Cdd:cd20976       9 KDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYaADRSTCE---AGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCS 85

                    ....*
gi 1958765569  1333 GKLYV 1337
Cdd:cd20976      86 AWVTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
28267-28642 4.56e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 66.12  E-value: 4.56e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28267 RIPGPPGKPVIYNVTS-DGMSLTwdapvydggseVTGFHVEKKERNSIlWQrVNTSPISGREYRATGLIEGLDYQFRVYA 28345
Cdd:COG4733     442 RVRLPDGTSVARTVQSvAGRTLT-----------VSTAYSETPEAGAV-WA-FGPDELETQLFRVVSIEENEDGTYTITA 508
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28346 ensaglsSPSDPSKFTL----AVSPVDPPGTPDYIDVT-----------RETITLKWNPPLRDggskiVAYSIEKRQGSD 28410
Cdd:COG4733     509 -------VQHAPEKYAAidagAFDDVPPQWPPVNVTTSeslsvvaqgtaVTTLTVSWDAPAGA-----VAYEVEWRRDDG 576
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28411 RWVrcNFTDVSECQYTVSGLSPGDrYEFRIIARNAVGTISPPSQSSGLIMTRDENVPPTVefgpeyfDGLVIKSGDSlri 28490
Cdd:COG4733     577 NWV--SVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVSSAWAASSETTVTGKTAPPPAP-------TGLTATGGLG--- 643
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28491 kaLVQGRPVPRVTWFKDGVEIER-----RMNMEITDVLGSTSLFVR-DATRDHRGVYTVEAKNVSG-----STKAEITVK 28559
Cdd:COG4733     644 --GITLSWSFPVDADTLRTEIRYsttgdWASATVAQALYPGNTYTLaGLKAGQTYYYRARAVDRSGnvsawWVSGQASAD 721
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28560 VQDTPGKVVGPIRFTNITGEKMTLWWEAPLNDGCAPVTHYIIEKRETSRLAWALIEDHCEAQSYTAIKLITGNEYQFRVS 28639
Cdd:COG4733     722 AAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVAATVAESATAAAAT 801

                    ...
gi 1958765569 28640 AVN 28642
Cdd:COG4733     802 GTA 804
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8988-9078 4.66e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 58.56  E-value: 4.66e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8988 PPFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIrSGGNYQISYLENSahLTIVKVDKGDSGQYTCYAINEV 9067
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDGT--LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  9068 GKDSCTAQLNI 9078
Cdd:cd20978      78 GDIYTETLLHV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4666-4743 4.71e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.35  E-value: 4.71e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4666 PPSFIKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVAN 4743
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8721-8789 4.73e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 58.11  E-value: 4.73e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8721 LILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIEN-ASGKDSCSA 8789
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8906-8982 4.75e-09

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 58.70  E-value: 4.75e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8906 VGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRslaGQYSCTVTNPIGSASSSAKLIL 8982
Cdd:cd20957      15 FGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDK---GMYQCFVRNDGDSAQATAELKL 88
I-set pfam07679
Immunoglobulin I-set domain;
2494-2577 4.81e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 58.81  E-value: 4.81e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2494 KIIRGLRDLTCTETQNVVFEVELS-HSGIDVVWNFKGQEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGEYAFYA----GE 2568
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGE 81

                    ....*....
gi 1958765569  2569 NTTSGKLTV 2577
Cdd:pfam07679    82 AEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
17340-17420 4.81e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.67  E-value: 4.81e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17340 LTVRVGEAFALTGRYSGKPKPKVDWFKDEAD-VLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFCQV 17418
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  17419 NV 17420
Cdd:smart00410    84 TV 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
9084-9175 4.89e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 58.75  E-value: 4.89e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9084 PPSFTKKLsETIEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATND 9163
Cdd:cd20972       1 PPQFIQKL-RSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  9164 AGSALCTSSIVI 9175
Cdd:cd20972      80 VGSDTTSAEIFV 91
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
28878-28957 4.91e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 58.70  E-value: 4.91e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28878 THIVRAGASIRLFIAYQGRPTPTAVWSKPDSNL---SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFT 28954
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFtatEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                    ...
gi 1958765569 28955 VKV 28957
Cdd:cd05894      84 VKV 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7208-7290 4.94e-09

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 58.67  E-value: 4.94e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7208 TSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKyNMSFVNSVALLTINEASVEDTGDYICEAHNGV-GHASCST 7286
Cdd:cd20970      10 FTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTTLTIRNIRRSDMGIYLCIASNGVpGSVEKRI 88

                    ....
gi 1958765569  7287 ALKV 7290
Cdd:cd20970      89 TLQV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
21297-21376 5.05e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 58.31  E-value: 5.05e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21297 TLVVRAGLSIRIFVPIKGRPAPEVTWTKD---NINLKHRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVN 21373
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRGdkaFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                    ...
gi 1958765569 21374 VRV 21376
Cdd:cd05894      84 VKV 86
fn3 pfam00041
Fibronectin type III domain;
24232-24316 5.07e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 5.07e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24232 GPPEGpVQVTGVTSEKCTLAWSPPLqDGGSDISHYVVEKRETSRL-AWTVVASEVVTNSLKVTKLLEGNEYIFRIMAVNK 24310
Cdd:pfam00041     1 SAPSN-LTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 24311 YGVGEP 24316
Cdd:pfam00041    79 GGEGPP 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6728-6805 5.09e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.35  E-value: 5.09e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6728 PPSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSN 6805
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5610-5693 5.10e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 5.10e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5610 PQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAAR-SVWKDDTSTILELFSAKAADSGTYICQLSNDVGTTSSK 5688
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   5689 ATIFV 5693
Cdd:smart00410    81 TTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6258-6336 5.14e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.35  E-value: 5.14e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6258 PPKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQN 6336
Cdd:pfam13927     1 KPVITVSPS-SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8712-8793 5.15e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 5.15e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   8712 DYSIEKGKPLILEGTFSGTPPISVTWKKNGVN-VTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKDSCSAQ 8790
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   8791 ILI 8793
Cdd:smart00410    83 LTV 85
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11138-11611 5.24e-09

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 65.18  E-value: 5.24e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11138 KPEVPPAKVPEvPKKPvveEKPVIEEKPaIPVAEKVESPPTEVYEEPE----EVAAQEEEPAPVVEEEEYEAPPPPAPEI 11213
Cdd:NF033839    158 KPETPQPENPE-HQKP---TTPAPDTKP-SPQPEGKKPSVPDINQEKEkaklAVATYMSKILDDIQKHHLQKEKHRQIVA 232
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11214 PVPQVPEEPKKVVPEKKYPVikkpeppppkvpevskkpapmkkvPVVKKPEPPEAEVPEVPKKLAPVKKEPVPVTKKPEV 11293
Cdd:NF033839    233 LIKELDELKKQALSEIDNVN------------------------TKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPG 288
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11294 LPEkvPEAPKkitPEKRESapvpeepeappapveeiPEetiyeekatiTIGRKETPPVEEREIERFIQPEEPGMEPQPE- 11372
Cdd:NF033839    289 NKK--PSAPK---PGMQPS-----------------PQ----------PEKKEVKPEPETPKPEVKPQLEKPKPEVKPQp 336
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11373 ETPVQE--PEPEKkviEKPKLKPRPpirapSPPKEDVKEKifqlkavskkkvPEKPEVVEKVEPTPLKvPTAEKKVRKLL 11450
Cdd:NF033839    337 EKPKPEvkPQLET---PKPEVKPQP-----EKPKPEVKPQ------------PEKPKPEVKPQPETPK-PEVKPQPEKPK 395
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11451 PEPKPQPKEevvlksvlrkrpeeeepkvepkkvekvkkpeeppppPKAVEVEAPPEPKPKERKVPEPTKvPEIKPAIPLP 11530
Cdd:NF033839    396 PEVKPQPEK------------------------------------PKPEVKPQPEKPKPEVKPQPEKPK-PEVKPQPEKP 438
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11531 GPEPKPKPEPEVKTMKAPPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKPKGPIKgvAKKTPSPIEAERKKLRPGSGGE 11610
Cdd:NF033839    439 KPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDK--KPSTPNNLSKDKQPSNQASTNE 516

                    .
gi 1958765569 11611 K 11611
Cdd:NF033839    517 K 517
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
1042-1128 5.39e-09

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 58.35  E-value: 5.39e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1042 SKPVVQK-LVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQtGECRLVISMTFADDAGEYTIVIRNKHGE 1120
Cdd:cd20973       1 IQTLRDKeVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDED-GLCSLIISDVCGDDSGKYTCKAVNSLGE 79

                    ....*...
gi 1958765569  1121 TSASASLL 1128
Cdd:cd20973      80 ATCSAELT 87
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
13934-14391 5.45e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 65.74  E-value: 5.45e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13934 PRPKATWTFGDQVLEAGdRVKIKTIsayaeliispsERPDKGIYTLTL--ENPVK--SI-SGEID--------VNVIARP 14000
Cdd:COG4733     473 PEAGAVWAFGPDELETQ-LFRVVSI-----------EENEDGTYTITAvqHAPEKyaAIdAGAFDdvppqwppVNVTTSE 540
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14001 SAPKELKFSDVTkdSVHLTWEPPDDDggsplTGYVVEKRDmSRKTWTKVMDfVTDLEFTVPDLVQGkEYLFKVCARNKCG 14080
Cdd:COG4733     541 SLSVVAQGTAVT--TLTVSWDAPAGA-----VAYEVEWRR-DDGNWVSVPR-TSGTSFEVPGIYAG-DYEVRVRAINALG 610
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14081 -PGEPAYTDEpVNMSAPATVPDPPENVKWRDRTaNSIFLTWDPPKNDGGSRIKGYIVEKCPRGSDkwVACGEPVPDTKME 14159
Cdd:COG4733     611 vSSAWAASSE-TTVTGKTAPPPAPTGLTATGGL-GGITLSWSFPVDADTLRTEIRYSTTGDWASA--TVAQALYPGNTYT 686
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14160 VTGLEEGKWYAYRVKALNRQGasKPSKPTEEIQAVDTQEAPEIFLDVKLLAGLTVKAGTKIELPATVTGKPEPKITWTKA 14239
Cdd:COG4733     687 LAGLKAGQTYYYRARAVDRSG--NVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTA 764
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14240 DTLLRPDQRITIENvpkkstVTITDSKRSDTGTYIIEAVnvcGRATAVVEVNVLDKPGPPAAFDITDVTNEScllTWNPP 14319
Cdd:COG4733     765 QIDTAVLFAGVATA------AAIGAEARVAATVAESATA---AAATGTAADAAGDASGGVTAGTSGTTGAGD---TAAST 832
                           410       420       430       440       450       460       470
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 14320 RDDGGSKITNYVVerkaTDSDVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAENMYGVGEPVQATPIIAKYQ 14391
Cdd:COG4733     833 TRVAAAVVLAGVV----VYGDAIIESGNTGDIVATGDIASAAAGAVATTVSGTTAADVSAVADSTAASLTAI 900
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8628-8696 5.48e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 57.72  E-value: 5.48e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8628 VTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAGRASCTT 8696
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
31760-31959 5.58e-09

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 63.14  E-value: 5.58e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIAEDLGRGEFGIVHRCV----ETSSKKtfmAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELV 31833
Cdd:cd14145       5 FSELVLEEIIGIGGFGKVYRAIwigdEVAVKA---ARHDPDEDISQTIenVRQEAKLFAMLKHPNIIALRGVCLKEPNLC 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIfERInTSAFELNEREVVSYVRQVCEALEFLHSQNIG---HFDIRPENIIYQTR------KNSIIKIIEF 31904
Cdd:cd14145      82 LVMEFARGGPL-NRV-LSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKvengdlSNKILKITDF 159
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31905 GQARQLKPGDNFRLLFTAPeYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd14145     160 GLAREWHRTTKMSAAGTYA-WMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7576-7666 5.63e-09

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 58.42  E-value: 5.63e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7576 PPSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSP---KCQPSFADnvctLTLSSLEPSDTGAYTCVAA 7652
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAdrsTCEAGVGE----LHIQDVLPEDHGTYTCLAK 76
                            90
                    ....*....|....
gi 1958765569  7653 NVAGQDESSALLTV 7666
Cdd:cd20976      77 NAAGQVSCSAWVTV 90
fn3 pfam00041
Fibronectin type III domain;
14297-14380 5.65e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 5.65e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14297 GPPAAFDITDVTNESCLLTWNPPrDDGGSKITNYVVERKATDS-DVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAENMY 14375
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 14376 GVGEP 14380
Cdd:pfam00041    80 GEGPP 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
32200-32280 5.67e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.96  E-value: 5.67e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32200 PPEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDdkkYTFESDKGLYQLTINSVTTDDDAEYAVVAR 32279
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGST---RSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 32280 N 32280
Cdd:pfam13927    78 N 78
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
19128-19208 5.75e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 58.52  E-value: 5.75e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVG--IDNVVRKG-QVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVN 19204
Cdd:cd20974      10 VVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGvQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAE 89

                    ....
gi 1958765569 19205 VKVL 19208
Cdd:cd20974      90 LLVL 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5790-5878 5.77e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 58.36  E-value: 5.77e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5790 PPIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANEG 5869
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....*....
gi 1958765569  5870 GSCACTARV 5878
Cdd:cd20972      81 GSDTTSAEI 89
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
31049-31132 5.80e-09

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 58.18  E-value: 5.80e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31049 KEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRkYKMSSDgrtHTLTVMTEEQEDEGVYTCVATNEVGEVET 31128
Cdd:cd05725       2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGR-YEILDD---HSLKIRKVTAGDMGSYTCVAENMVGKIEA 77

                    ....
gi 1958765569 31129 SSKL 31132
Cdd:cd05725      78 SATL 81
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
20900-20981 5.85e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 5.85e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20900 LTVKAGDSIVLSaISILGKPLPKSSWSK-AGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEHVK 20978
Cdd:smart00410     4 VTVKEGESVTLS-CEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  20979 VSV 20981
Cdd:smart00410    83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
17823-17906 5.93e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 5.93e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17823 GPPRDLEVSEIRKDSCYLTWKEPlDDGGSVVTNYVVERKDV-ATAQWSPLSTTSKKKSHMAKHLNEGNQYLFRVAAENQY 17901
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 17902 GRGPF 17906
Cdd:pfam00041    80 GEGPP 84
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
113-188 6.07e-09

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 57.98  E-value: 6.07e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569   113 MTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATST 188
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSAT 77
PTZ00121 PTZ00121
MAEBL; Provisional
32984-33612 6.31e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.93  E-value: 6.31e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32984 ASQRRDEEVPKSVFPELTKTEAYAISSFKRTSEMEAASSVRevKSQMTETRESLSSYEHHVSAEMKSAASEEKSLEEkat 33063
Cdd:PTZ00121   1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR--KAEEVRKAEELRKAEDARKAEAARKAEEERKAEE--- 1216
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33064 VRKIKTTLAARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTA-KYKSTFEISSVQASDEGN 33142
Cdd:PTZ00121   1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKKKADEAK 1296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33143 YSVVVENTD---GKQEAQFTLTVQKAKAVEKAVTSPPRVKSPEPRVKSPETVKSPKRVKSPELVASHPKAVSPTETKPTE 33219
Cdd:PTZ00121   1297 KAEEKKKADeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33220 KGQqlpVPAPPKitqslKAEASRDIAKLTCAVESSALCAKEVAWYKDGKKLKEnghfqfhysadgtyELKihnlsesdcg 33299
Cdd:PTZ00121   1377 KKK---ADAAKK-----KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD--------------EAK---------- 1424
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33300 eyvceVSGEGGTSKTSFQFTGQSFKSIHEQVSSTTETKKSVQKTAESAEAKKATQKTAESAEAKKATQKTAESAEAKKPA 33379
Cdd:PTZ00121   1425 -----KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33380 QKTAESAEAKKPAQKTAEPTEAKKQEPIAPESVSSKpvivtglrdttvsSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQS 33459
Cdd:PTZ00121   1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK-------------ADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33460 SKYKLSNDKEEFIL---EILKtetsdgglyscTVANSAGSVSSSCKLTIKAVKDTEAQKVSTQKTSEVTAKKKESVQQEI 33536
Cdd:PTZ00121   1567 EEAKKAEEDKNMALrkaEEAK-----------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
                           570       580       590       600       610       620       630
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33537 SQKVLTSEEikmsEVKSHETLAIKEEASKVLIAEEVKKSAAASLEKSIVHEEVTKTSQASEEVKTHAEIKALSTQM 33612
Cdd:PTZ00121   1636 EQLKKKEAE----EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3312-3392 6.33e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 6.33e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3312 QDAVTSEGRPARFQCQVSGT-DLKVSWYCRD-KKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAVGQVSSTA 3389
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSpPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569   3390 TLR 3392
Cdd:smart00410    82 TLT 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4949-5028 6.50e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 58.28  E-value: 6.50e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVE-GTASLEISRVDMNDAGNFTCRATNSV 5027
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVREnGRHSLIIEPVTKRDAGIYTCIARNRA 80

                    .
gi 1958765569  5028 G 5028
Cdd:cd05744      81 G 81
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
32209-32293 6.51e-09

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 58.40  E-value: 6.51e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32209 NKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDdkKYTFESDKGlyQLTINSVTTDDDAEYAVVARNKHGEDSCK 32288
Cdd:cd05730      12 NATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE--KYSFNEDGS--EMTILDVDKLDEAEYTCIAENKAGEQEAE 87

                    ....*
gi 1958765569 32289 AKLTV 32293
Cdd:cd05730      88 IHLKV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9588-9665 6.51e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 6.51e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9588 QDVTLKEGQTCTMTCQFS-VPNVKSEWFRNG-RVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTC----KHEDLETSA 9661
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCaatnSSGSASSGT 81

                     ....
gi 1958765569   9662 ELRI 9665
Cdd:smart00410    82 TLTV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
32319-32396 6.62e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 58.17  E-value: 6.62e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 32319 EGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGldyyALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:cd20978      15 GGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDG----TLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12191-12258 6.63e-09

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 58.02  E-value: 6.63e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12191 EIILKCEVSK-DVPVKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTCDCGTDTTKANVTV 12258
Cdd:cd20967      14 KIRLTVELADpDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
14213-14279 6.69e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.96  E-value: 6.69e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 14213 TVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVN 14279
Cdd:pfam13927    12 TVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
33699-33787 6.87e-09

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 58.11  E-value: 6.87e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33699 SFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQ 33778
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                    ....*....
gi 1958765569 33779 CSATASLTV 33787
Cdd:cd20949      81 ASDMQERTV 89
fn3 pfam00041
Fibronectin type III domain;
28170-28254 7.07e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 7.07e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28170 SKPKGPiRFDEIKADSAIMSWDIPEDdGGGEITCYSIEKREA-SQTNWKMVCSSVARTTFKVSNLVKDSEYQFRVRAENR 28248
Cdd:pfam00041     1 SAPSNL-TVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 28249 YGVSEP 28254
Cdd:pfam00041    79 GGEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
28494-28557 7.14e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 57.72  E-value: 7.14e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 28494 VQGRPVPRVTWFKDGVEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEIT 28557
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
33079-33160 7.29e-09

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 57.98  E-value: 7.29e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33079 PRSITVHEGESARFSCD-TDGEPVPTVTWLRGGQVVSTSARHQVTTA-KYKSTFEISSVQASDEGNYSVVVENTDGKQEA 33156
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSaSTGSPGPDVTWSKEGGTLIESLKVKHDNGrTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

                    ....
gi 1958765569 33157 QFTL 33160
Cdd:pfam00047    83 STSL 86
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
31763-31955 7.34e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 63.62  E-value: 7.34e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31763 YMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHR-----NILYLHESFESMEELVMIFE 31837
Cdd:cd14211       1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31838 FISgLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIY--QTRKNSIIKIIEFGQARQLKPGd 31914
Cdd:cd14211      81 MLE-QNLYDFLKQNKFSpLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLvdPVRQPYRVKVIDFGSASHVSKA- 158
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 1958765569 31915 nFRLLFTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSG 31955
Cdd:cd14211     159 -VCSTYLQSRYYrAPEIILGLPFCEAIDMWSLGCVIAELFLG 199
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7867-7945 7.70e-09

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 57.79  E-value: 7.70e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7867 AAIGEPTTLQCKVDGTPEIRISWYKEHTKLrsaPAYKMQFKNNvASLVINKVDHSDVGEYTCKAENSVGAVASSAVLVI 7945
Cdd:cd05725       9 VLVDDSAEFQCEVGGDPVPTVRWRKEDGEL---PKGRYEILDD-HSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
24823-24913 7.76e-09

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 58.03  E-value: 7.76e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24823 QPSF-KLPFNTYSVQaGEDLKIEIPVIGRPRPKISWVKDGEPLRQTT-RVNVEetATSTILHIKESSKDDFGKYSVTATN 24900
Cdd:cd20976       1 APSFsSVPKDLEAVE-GQDFVAQCSARGKPVPRITWIRNAQPLQYAAdRSTCE--AGVGELHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|...
gi 1958765569 24901 NAGTATENLSVIV 24913
Cdd:cd20976      78 AAGQVSCSAWVTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
25361-25610 7.89e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 65.35  E-value: 7.89e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25361 WTQVSTEVQALNYKVTKLLPGNEYIFRVMAV----NKYGVGE--PLESEPVIACNPYKLPGPPSTPEASAITKDSMVLTW 25434
Cdd:COG4733     479 WAFGPDELETQLFRVVSIEENEDGTYTITAVqhapEKYAAIDagAFDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSW 558
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25435 TRPVDDGGAEIEGYilekrdKEGIRWTkcNKKTLTDLRFRVTGLTEGhSYEFRVAAENAAGV-GEPSEPSVFYRACDALY 25513
Cdd:COG4733     559 DAPAGAVAYEVEWR------RDDGNWV--SVPRTSGTSFEVPGIYAG-DYEVRVRAINALGVsSAWAASSETTVTGKTAP 629
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25514 PPGPPSnpkVTDTSRS-SVSLAWNKPIydgGAPVRGYviELKEAAADEWTTCT-PPSGLQGKQFTVTKLKENTEYNFRIC 25591
Cdd:COG4733     630 PPAPTG---LTATGGLgGITLSWSFPV---DADTLRT--EIRYSTTGDWASATvAQALYPGNTYTLAGLKAGQTYYYRAR 701
                           250
                    ....*....|....*....
gi 1958765569 25592 AFNTEGVGEPATIPGSVVA 25610
Cdd:COG4733     702 AVDRSGNVSAWWVSGQASA 720
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8140-8218 7.96e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 57.98  E-value: 7.96e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8140 PPRFIKKLdQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:cd20972       1 PPQFIQKL-RSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATN 78
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
3478-3540 7.97e-09

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 58.04  E-value: 7.97e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  3478 AKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYG 3540
Cdd:cd05736      18 ASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
6922-6997 8.10e-09

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 57.89  E-value: 8.10e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6922 EPLEASV--GDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYrtYFTNNVATLVFNKVGINDSGEYTCVAENSIGTAA 6997
Cdd:cd20952       5 GPQNQTVavGGTVVLNCQATGEPVPTISWLKDGVPLLGKDER--ITTLENGSLQIKGAEKSDTGEYTCVALNLSGEAT 80
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
6636-6725 8.12e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 57.79  E-value: 8.12e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6636 PSFTRR-LKDIGGVLGTSCVLECKVAGSSPISIAWFHeKTKIVSGAKYQTTFSDNvcTLQLNSLDSSDMGSYTCVAANVA 6714
Cdd:cd20978       1 PKFIQKpEKNVVVKGGQDVTLPCQVTGVPQPKITWLH-NGKPLQGPMERATVEDG--TLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  6715 GSDECRALLTV 6725
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
1803-1887 8.17e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 58.14  E-value: 8.17e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1803 IVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRV-RYDGIHYLDIVDCKSYDTGEVKVTAENPEGVT 1881
Cdd:cd05747       6 ILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQItSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQ 85

                    ....*.
gi 1958765569  1882 EHKVKL 1887
Cdd:cd05747      86 EAQFTL 91
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5508-5600 8.19e-09

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 58.27  E-value: 8.19e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5508 IIPPSFtkklRKMDSIKGSFIDLECIVA-GSHPISIQWFKDDQEISASDKYKFSFHDN-TAFLEISQLEGTDSGTYTCSA 5585
Cdd:cd20959       4 IIPFAF----GEGAAQVGMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRrSSILSIDSLEASHAGNYTCHA 79
                            90
                    ....*....|....*
gi 1958765569  5586 TNKAGHSQCSGHLTV 5600
Cdd:cd20959      80 RNSAGSASYTAPLTV 94
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12893-12970 8.30e-09

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 57.64  E-value: 8.30e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 12893 TDLQVKEKETARFECEISKENVKVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEVRTARTSGMLTV 12970
Cdd:cd20967       5 PAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
16638-16725 8.31e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.90  E-value: 8.31e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16638 MEVEEGTDVNIVAKIKGVPFPTLTWFKappkkpDSKEPVVYDTHVNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTA 16717
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYK------QGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA 77

                     ....*...
gi 1958765569  16718 SKEMRLNV 16725
Cdd:smart00410    78 SSGTTLTV 85
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
31756-32017 8.35e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 63.89  E-value: 8.35e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31756 TKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK---EISILNIARHRNILYL------HESF 31826
Cdd:cd07876      16 TFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRayrELVLLKCVNHKNIISLlnvftpQKSL 95
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31827 ESMEELVMIFEFISGlDIFERINtsaFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQ 31906
Cdd:cd07876      96 EEFQDVYLVMELMDA-NLCQVIH---MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIV--VKSDCTLKILDFGL 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARqlKPGDNFRLL-FTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETN----QQMIENI-------MN 31973
Cdd:cd07876     170 AR--TACTNFMMTpYVVTRYYrAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHidqwNKVIEQLgtpsaefMN 247
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31974 A------EYTFDEEAFQEISLE---------------------AMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07876     248 RlqptvrNYVENRPQYPGISFEelfpdwifpseserdklktsqARDLLSKMLVIDPDKRISVDEALRHPYI 318
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6165-6242 8.54e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.58  E-value: 8.54e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6165 PPSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTN 6242
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
22854-22939 8.94e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 8.94e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22854 GPPGTPFVTLASKDSMEVQWHEPvSDGGSRVIGYHLERKERNSILWVKLNKTPIPQTKFKTTGLEEGIEYEFRVSAENIV 22933
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 22934 GIGKPS 22939
Cdd:pfam00041    80 GEGPPS 85
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
31767-31954 9.15e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 62.73  E-value: 9.15e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCvETSSKKTFMAKFVKVK----GTDQVL--VKKEISILNIARHRNIL-YLHESFES-MEELVMIFEF 31838
Cdd:cd14205      10 QQLGKGNFGSVEMC-RYDPLQDNTGEVVAVKklqhSTEEHLrdFEREIEILKSLQHDNIVkYKGVCYSAgRRNLRLIMEY 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLkPGDNFRL 31918
Cdd:cd14205      89 LPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENR--VKIGDFGLTKVL-PQDKEYY 165
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1958765569 31919 LFTAPE-----YYAPEVHQHDVVSSATDMWSLGTLVYVLLS 31954
Cdd:cd14205     166 KVKEPGespifWYAPESLTESKFSVASDVWSFGVVLYELFT 206
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
19947-20183 9.19e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 64.97  E-value: 9.19e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19947 WAQVSATVPITSCTVEKLIEGHEYQFRICA----ENKYGVGDpifTEPVIAKNPYDPP-----GRCDPPVISNITKDHMT 20017
Cdd:COG4733     479 WAFGPDELETQLFRVVSIEENEDGTYTITAvqhaPEKYAAID---AGAFDDVPPQWPPvnvttSESLSVVAQGTAVTTLT 555
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20018 VSWKAPADDggspiTGYLVEKReTQAVNWTKVNRkpVIERTLKATGLQEGTeYEFRVTAINKAG-PGKPSDASKAVYAQD 20096
Cdd:COG4733     556 VSWDAPAGA-----VAYEVEWR-RDDGNWVSVPR--TSGTSFEVPGIYAGD-YEVRVRAINALGvSSAWAASSETTVTGK 626
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20097 PLYPPGPPAFpkvydTTRS---SVSLSWGKPAfdgGSPIIGYlvEVKRADSDHWVRCNLPEKLQKTR-FEVTGLMENTEY 20172
Cdd:COG4733     627 TAPPPAPTGL-----TATGglgGITLSWSFPV---DADTLRT--EIRYSTTGDWASATVAQALYPGNtYTLAGLKAGQTY 696
                           250
                    ....*....|.
gi 1958765569 20173 QFRVYAVNKIG 20183
Cdd:COG4733     697 YYRARAVDRSG 707
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8797-8886 9.40e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 57.79  E-value: 9.40e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKqlEPLKVTV---GDSASLQCQLAGTPEIGVSW-YKGDTKLRPTTTckMHFKNNvaTLVFTQVDSNDSGEYICRAE 8872
Cdd:cd20978       1 PKFIQ--KPEKNVVvkgGQDVTLPCQVTGVPQPKITWlHNGKPLQGPMER--ATVEDG--TLTIINVQPEDTGYYGCVAT 74
                            90
                    ....*....|....
gi 1958765569  8873 NSVGEVSSSTFLTV 8886
Cdd:cd20978      75 NEIGDIYTETLLHV 88
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
906-989 9.52e-09

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 57.92  E-value: 9.52e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   906 LKNVTVVEGESVTLECHISGYPSPKVTWYREDYQI---ESSIDFQITFQS--GIARLMIREAFAEDSGRFTCSAVNEAGT 980
Cdd:cd05732       8 LENQTAVELEQITLTCEAEGDPIPEITWRRATRGIsfeEGDLDGRIVVRGhaRVSSLTLKDVQLTDAGRYDCEASNRIGG 87

                    ....*....
gi 1958765569   981 VSTSCYLAV 989
Cdd:cd05732      88 DQQSMYLEV 96
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8988-9078 9.58e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 57.98  E-value: 9.58e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8988 PPFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEV 9067
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  9068 GKDSCTAQLNI 9078
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7294-7373 9.59e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 57.79  E-value: 9.59e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPP-VGALKGSDVILQCEISGTPPFEVVWVKDRKQV-RSSKKFKVTsknfDTSLHIFNLEAPDIGEYHCKATNE 7371
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLqGPMERATVE----DGTLTIINVQPEDTGYYGCVATNE 76

                    ..
gi 1958765569  7372 VG 7373
Cdd:cd20978      77 IG 78
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
28085-28154 9.75e-09

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 58.00  E-value: 9.75e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 28085 ISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENK-ITLSIKNVKKENGGKYTVILDNAV 28154
Cdd:cd05729      14 HALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKgWSLIIERAIPRDKGKYTCIVENEY 84
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
1807-1889 9.85e-09

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 57.73  E-value: 9.85e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIHY-LDIVDCKSYDTGEVKVTAENPEGVTEHKV 1885
Cdd:cd20949       6 AYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADgLLINKVTQDDTGEYTCRAYQVNSIASDMQ 85

                    ....
gi 1958765569  1886 KLEI 1889
Cdd:cd20949      86 ERTV 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
25907-25997 1.01e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 57.75  E-value: 1.01e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25907 PSVELPFNTFNVKANDQLKIDIPFKGRPQATVAWKKDGQVLRETT--RVNVSSSKIVTTLSIKEASREDVGTYELCVSNT 25984
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 25985 AGSITVPITVIVL 25997
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8421-8502 1.02e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 57.75  E-value: 1.02e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8421 PATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  8501 GK 8502
Cdd:cd05747      83 GK 84
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
31045-31137 1.02e-08

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 57.95  E-value: 1.02e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31045 PGVRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELV------QSRKYkMSSDGRTHTLTVM--TEEQEDEGVYT 31116
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLEtdkddpRSHRI-VLPSGSLFFLRVVhgRKGRSDEGVYV 79
                            90       100
                    ....*....|....*....|.
gi 1958765569 31117 CVATNEVGEVeTSSKLLLQAA 31137
Cdd:cd07693      80 CVAHNSLGEA-VSRNASLEVA 99
fn3 pfam00041
Fibronectin type III domain;
19502-19589 1.02e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 1.02e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19502 DAPGPPQppfdISEIDADACSLSWHIPlEDGGSNITNYIVEKCDVSRGD-WVTALASVTKTSCRVGKLIPGQEYIFRVRA 19580
Cdd:pfam00041     1 SAPSNLT----VTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75

                    ....*....
gi 1958765569 19581 ENRFGISEP 19589
Cdd:pfam00041    76 VNGGGEGPP 84
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4573-4653 1.04e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 57.79  E-value: 1.04e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4573 PSFVKKVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTvRMSFANSeaILDITDVKVDDSGTYSCEATNDA 4652
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPME-RATVEDG--TLTIINVQPEDTGYYGCVATNEI 77

                    .
gi 1958765569  4653 G 4653
Cdd:cd20978      78 G 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6445-6523 1.05e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.19  E-value: 1.05e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6445 PPKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEkEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKN 6523
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKN-GEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5136-5215 1.06e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 57.79  E-value: 1.06e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5136 TFTEKLEPSQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKhKMSFVESTavLRLTDVAIEDSGEYMCEAQNEAG 5215
Cdd:cd20978       2 KFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPME-RATVEDGT--LTIINVQPEDTGYYGCVATNEIG 78
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
31765-31959 1.08e-08

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 62.37  E-value: 1.08e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHR-------CVetsskktfmaKFVKVKGTDQ---VLVKKEISILNIARHRNILYLHESFESMEELVM 31834
Cdd:cd14063       4 IKEVIGKGRFGRVHRgrwhgdvAI----------KLLNIDYLNEeqlEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAI 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd14063      74 VTSLCKGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVVITDFGLFSLSGLLQPGR 153
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31915 NFRLLFTAPE---YYAPEV---------HQHDV-VSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd14063     154 REDTLVIPNGwlcYLAPEIiralspdldFEESLpFTKASDVYAFGTVWYELLAGRWPF 211
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
2-88 1.08e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 57.75  E-value: 1.08e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     2 TTQAPTFTQPlQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLpgVQISFSDGRARLMIPAVTKANSGRYSLR 81
Cdd:cd05747       1 TLPATILTKP-RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQR--HQITSTEYKSTFEISKVQMSDEGNYTVV 77

                    ....*..
gi 1958765569    82 ATNGSGQ 88
Cdd:cd05747      78 VENSEGK 84
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
1038-1127 1.09e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 57.79  E-value: 1.09e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGS-VVFECQIGGNPKPHVYWKKSGVPLT-TGYRYKVSYNkqtgecRLVISMTFADDAGEYTIVIR 1115
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQdVTLPCQVTGVPQPKITWLHNGKPLQgPMERATVEDG------TLTIINVQPEDTGYYGCVAT 74
                            90
                    ....*....|..
gi 1958765569  1116 NKHGETSASASL 1127
Cdd:cd20978      75 NEIGDIYTETLL 86
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
8061-8139 1.10e-08

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 57.66  E-value: 1.10e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8061 LGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQLGVQE 8139
Cdd:cd05736      14 PGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
fn3 pfam00041
Fibronectin type III domain;
31236-31321 1.12e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 1.12e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31236 DKPTGPIVIEaLLKNSVVISWKAPADDGGSwITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQNT 31315
Cdd:pfam00041     1 SAPSNLTVTD-VTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 31316 FGISEP 31321
Cdd:pfam00041    79 GGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
13247-13330 1.12e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 57.65  E-value: 1.12e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13247 RIIEPLKDIETMEKKSVTFWCKVN---RLNVTlkWTKNGEEVAFDNRISYRIDKYKHSLIIKDCGFPDEGEYIVTA---- 13319
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtpDPEVS--WFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsa 79
                            90
                    ....*....|.
gi 1958765569 13320 GQDKSVAELLI 13330
Cdd:pfam07679    80 GEAEASAELTV 90
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2601-2664 1.13e-08

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 57.25  E-value: 1.13e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2601 CEVANPESEGEWLKDGKHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYTYKVATSKTSAKLKV 2664
Cdd:cd20967      19 VELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6914-7002 1.15e-08

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 57.58  E-value: 1.15e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6914 PPyFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLrstPEYR--TYFTNnvATLVFNKV-GINDSGEYTCVAE 6990
Cdd:cd20958       1 PP-FIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRL---PLNHrqRVFPN--GTLVIENVqRSSDEGEYTCTAR 74
                            90
                    ....*....|..
gi 1958765569  6991 NSIGTAASKTVF 7002
Cdd:cd20958      75 NQQGQSASRSVF 86
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6541-6629 1.16e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 57.82  E-value: 1.16e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6541 VIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQ---KHKF-SFYNkISSLKILSVEKEDAGTYTFQVQN 6616
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIeSEYG-VHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569  6617 NVGKSSCTAVVDV 6629
Cdd:cd20951      81 IHGEASSSASVVV 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
25918-25996 1.17e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.52  E-value: 1.17e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25918 VKANDQLKIDIPFKGRPQATVAWKKDG-QVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIV 25996
Cdd:smart00410     6 VKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
24145-24227 1.18e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 57.54  E-value: 1.18e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24145 DTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEE-SARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPV 24223
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTAtEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 24224 NVKV 24227
Cdd:cd05894      83 FVKV 86
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7109-7189 1.19e-08

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 57.73  E-value: 1.19e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7109 FDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQA--TNDVG 7186
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAyqVNSIA 81

                    ...
gi 1958765569  7187 KDM 7189
Cdd:cd20949      82 SDM 84
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
4296-4381 1.19e-08

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 57.52  E-value: 1.19e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4296 RRIEPLEVALGHLAKFTCEIQGA-PNVRFQWFKAGREI--YESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYGS 4372
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEATSEnPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGK 83

                    ....*....
gi 1958765569  4373 VSCTATLTV 4381
Cdd:cd05750      84 DTVTGNVTV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
17742-17819 1.19e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 57.75  E-value: 1.19e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17742 IKVGDTLRLSAIIKGVPFPKVTWKKEDREAPT----KAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVL 17817
Cdd:cd20974      12 VLEGSTATFEAHVSGKPVPEVSWFRDGQVISTstlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELL 91

                    ..
gi 1958765569 17818 VL 17819
Cdd:cd20974      92 VL 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
28482-28558 1.21e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 57.59  E-value: 1.21e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 28482 IKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSG--STKAEITV 28558
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGsdTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4862-4942 1.22e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.52  E-value: 1.22e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   4862 IQVTAGDPATLEYTVSGTPELKPKWYKDG-RPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTF 4940
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569   4941 TV 4942
Cdd:smart00410    84 TV 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
1041-1127 1.22e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 57.75  E-value: 1.22e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1041 ISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYN--KQTGEcrlvISMTFADDAGEYTIVIRNKH 1118
Cdd:cd05747       7 LTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTeyKSTFE----ISKVQMSDEGNYTVVVENSE 82

                    ....*....
gi 1958765569  1119 GETSASASL 1127
Cdd:cd05747      83 GKQEAQFTL 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
26299-26399 1.22e-08

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 58.04  E-value: 1.22e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26299 PRImmdVKFRDVIVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKN 26378
Cdd:cd05762       2 PQI---IQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVEN 78
                            90       100
                    ....*....|....*....|.
gi 1958765569 26379 VAGTRTMAVNCKVLDKPGPPA 26399
Cdd:cd05762      79 KLGSRQAQVNLTVVDKPDPPA 99
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
23052-23137 1.28e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 57.75  E-value: 1.28e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23052 PPRISMDPKykdTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAK 23131
Cdd:cd05747       3 PATILTKPR---SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVE 79

                    ....*.
gi 1958765569 23132 NVAGEK 23137
Cdd:cd05747      80 NSEGKQ 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7200-7290 1.32e-08

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 57.47  E-value: 1.32e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDTSKVAkQGESIQLECKISGSPEIKVVWFRNDselhESWKYNMSFVN-------SVALLtINEASVEDTGDYI 7272
Cdd:cd05892       1 PMFIQKPQNKKVL-EGDPVRLECQISAIPPPQIFWKKNN----EMLQYNTDRISlyqdncgRICLL-IQNANKKDAGWYT 74
                            90
                    ....*....|....*...
gi 1958765569  7273 CEAHNGVGHASCSTALKV 7290
Cdd:cd05892      75 VSAVNEAGVVSCNARLDV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9092-9175 1.32e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 1.32e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   9092 SETIEETEGNSFKLEGRVAGSQPITIAWYKNNVE-IHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATNDAGSALCT 9170
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   9171 SSIVI 9175
Cdd:smart00410    81 TTLTV 85
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
899-989 1.32e-08

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 57.19  E-value: 1.32e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTlVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDfQITFQSGIarLMIREAF-AEDSGRFTCSAVNE 977
Cdd:cd20958       1 PPF-IRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR-QRVFPNGT--LVIENVQrSSDEGEYTCTARNQ 76
                            90
                    ....*....|...
gi 1958765569   978 AG-TVSTSCYLAV 989
Cdd:cd20958      77 QGqSASRSVFVKV 89
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5607-5693 1.33e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 57.02  E-value: 1.33e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5607 VEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARsVWKDDTstiLELFSAKAADSGTYICQLSNDVGTTS 5686
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYE-ILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  5687 SKATIFV 5693
Cdd:cd05725      77 ASATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
28467-28547 1.34e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.19  E-value: 1.34e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28467 PPTVEFGPEyfdGLVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAK 28546
Cdd:pfam13927     1 KPVITVSPS---SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 28547 N 28547
Cdd:pfam13927    78 N 78
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
6923-7002 1.35e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 57.20  E-value: 1.35e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6923 PLEASVGDSVSLQCQV-AGTPEITVSWFK-GDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTAASKT 7000
Cdd:pfam00047     5 TVTVLEGDSATLTCSAsTGSPGPDVTWSKeGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84

                    ..
gi 1958765569  7001 VF 7002
Cdd:pfam00047    85 SL 86
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
14908-14988 1.35e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 57.16  E-value: 1.35e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14908 IVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASD-RLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASINV 14986
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 14987 KV 14988
Cdd:cd05894      85 KV 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
24146-24227 1.35e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 1.35e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  24146 TIVVNAGETFRLEADVHGKPLPTIEWLR-GDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVN 24224
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  24225 VKV 24227
Cdd:smart00410    83 LTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1430-1507 1.41e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 1.41e-08
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   1430 EGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRAGKSTISVTLTV 1507
Cdd:smart00410     8 EGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1037-1128 1.42e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 57.59  E-value: 1.42e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1037 APFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSynkQTGECR-LVISMTFADDAGEYTIVIR 1115
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIH---QEGDLHsLIIAEAFEEDTGRYSCLAT 77
                            90
                    ....*....|...
gi 1958765569  1116 NKHGETSASASLL 1128
Cdd:cd20972      78 NSVGSDTTSAEIF 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
14340-14576 1.42e-08

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 64.58  E-value: 1.42e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14340 DVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAenmygvgepVQATP----IIAKYQFDPPGPP-----------TRLEPS 14404
Cdd:COG4733     477 AVWAFGPDELETQLFRVVSIEENEDGTYTITA---------VQHAPekyaAIDAGAFDDVPPQwppvnvttsesLSVVAQ 547
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14405 DITKDAVTLTWcepddDGGSPITGYWVErLDPDTDKWVrcNKMPVKDTTYRVKGLTNKKkYRFRVLAENLAG-PGKPSRS 14483
Cdd:COG4733     548 GTAVTTLTVSW-----DAPAGAVAYEVE-WRRDDGNWV--SVPRTSGTSFEVPGIYAGD-YEVRVRAINALGvSSAWAAS 618
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14484 TEPILIKDPIDPPWPPGKPTVKDIGktSLVLNWTKPEHDGGAKIESYViemlkTGTDDW----VRVAEGvPTTEHLLTGL 14559
Cdd:COG4733     619 SETTVTGKTAPPPAPTGLTATGGLG--GITLSWSFPVDADTLRTEIRY-----STTGDWasatVAQALY-PGNTYTLAGL 690
                           250
                    ....*....|....*..
gi 1958765569 14560 MEGQEYSFRVRAVNKAG 14576
Cdd:COG4733     691 KAGQTYYYRARAVDRSG 707
fn3 pfam00041
Fibronectin type III domain;
18317-18402 1.46e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 1.46e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18317 GPPINPKLKDKTKESADLVWTKPlSDGGSPILGYVVECQKPGTTQ-WDRINKDEliRQCAFRVPGLIEGNEYRFRIRAAN 18395
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 18396 IVGEGEP 18402
Cdd:pfam00041    78 GGGEGPP 84
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
33416-33505 1.47e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 57.52  E-value: 1.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSD--SVAKFVIKVTGEPQPTVTWTKDGKAI-AQSSKYKLSNDKEEfiLEILKTETSDGGLYSCTVAN 33492
Cdd:cd20970       1 PVISTPQPSFTVTARegENATFMCRAEGSPEPEISWTRNGNLIiEFNTRYIVRENGTT--LTIRNIRRSDMGIYLCIASN 78
                            90
                    ....*....|....
gi 1958765569 33493 SA-GSVSSSCKLTI 33505
Cdd:cd20970      79 GVpGSVEKRITLQV 92
I-set pfam07679
Immunoglobulin I-set domain;
30262-30340 1.48e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 57.27  E-value: 1.48e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 30262 VPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKVVI 30340
Cdd:pfam07679    12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
8235-8321 1.50e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 57.08  E-value: 1.50e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETL--KGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENlltSIHILNVDTADIGEYQCKATND 8312
Cdd:cd04969       1 PDFELNPVKKKILaaKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDG---SLKIKNVTKSDEGKYTCFAVNF 77

                    ....*....
gi 1958765569  8313 VGSDTCVGS 8321
Cdd:cd04969      78 FGKANSTGS 86
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
31769-31971 1.51e-08

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 61.91  E-value: 1.51e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHR-CVETSSKK--TFMAKFVKVKGTDQVLVK--KEISILNIARHRNILYLHESFESMEELVMIFEFIS--G 31841
Cdd:cd05063      13 IGAGEFGEVFRgILKMPGRKevAVAIKTLKPGYTEKQRQDflSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMEngA 92
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFelNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKpgDNFRLLFT 31921
Cdd:cd05063      93 LDKYLRDHDGEF--SSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNS--NLECKVSDFGLSRVLE--DDPEGTYT 166
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31922 AP------EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05063     167 TSggkipiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAI 223
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8796-8886 1.52e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 57.21  E-value: 1.52e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8796 PPYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSV 8875
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8876 GEVSSSTFLTV 8886
Cdd:cd20972      81 GSDTTSAEIFV 91
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
31767-32019 1.57e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 62.00  E-value: 1.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKkTFMAkfVK-----VKGTDQV-------LVKKEISILNIARHRNILYlHES-----FE-- 31827
Cdd:cd06616      12 GEIGRGAFGTVNKMLHKPSG-TIMA--VKrirstVDEKEQKrllmdldVVMRSSDCPYIVKFYGALF-REGdcwicMElm 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31828 --SMEELVMIfefisgldIFERINTsafELNErEVVSYVR-QVCEALEFLHSQ-NIGHFDIRPENIIYQTRKNsiIKIIE 31903
Cdd:cd06616      88 diSLDKFYKY--------VYEVLDS---VIPE-EILGKIAvATVKALNYLKEElKIIHRDVKPSNILLDRNGN--IKLCD 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31904 FGQARQL------------KPgdnfrllFTAPEYYAPEVHQ--HDVVSsatDMWSLGTLVYVLLSGINPF-----LAETN 31964
Cdd:cd06616     154 FGISGQLvdsiaktrdagcRP-------YMAPERIDPSASRdgYDVRS---DVWSLGITLYEVATGKFPYpkwnsVFDQL 223
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31965 QQMIEN---IMNAEYTFdeeafqEISLEAMDFIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd06616     224 TQVVKGdppILSNSEER------EFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKM 275
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
31767-31971 1.58e-08

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 62.10  E-value: 1.58e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHR--CVETSSKKTFMAKFVKV--KGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05049      11 RELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTlkDASSPDARKdfeREAELLTNLQHENIVKFYGVCTEGDPLLMVFEYM 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDI--FERIN-----------TSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQ 31906
Cdd:cd05049      91 EHGDLnkFLRSHgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGT--NLVVKIGDFGM 168
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31907 ARQLKPGDNFRLLFTA--P-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05049     169 SRDIYSTDYYRVGGHTmlPiRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTEVIECI 237
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
3461-3550 1.58e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 57.02  E-value: 1.58e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEI-SDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLT-PSADYKFvfdgNNHSLIILFTRFQDEGEYTCMASNE 3538
Cdd:cd20978       1 PKFIQKPeKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQgPMERATV----EDGTLTIINVQPEDTGYYGCVATNE 76
                            90
                    ....*....|..
gi 1958765569  3539 YGRAVCSAHLKV 3550
Cdd:cd20978      77 IGDIYTETLLHV 88
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
33441-33504 1.58e-08

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 56.42  E-value: 1.58e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 33441 GEPQPTVTWTKDGKAIAQSSKYKLSndkEEFILEILKTETSDGGLYSCTVANSAGSVSSSCKLT 33504
Cdd:cd05746       9 GDPEPTITWNKDGVQVTESGKFHIS---PEGYLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
24834-24913 1.59e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 57.43  E-value: 1.59e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24834 SVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTT---RVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLS 24910
Cdd:cd20951      11 TVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSAS 90

                    ...
gi 1958765569 24911 VIV 24913
Cdd:cd20951      91 VVV 93
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4759-4852 1.61e-08

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 57.66  E-value: 1.61e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4759 PPTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEA 4838
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*
gi 1958765569  4839 GS-QTSVGELIVKEP 4852
Cdd:cd05762      81 GSrQAQVNLTVVDKP 95
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7577-7666 1.63e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 57.12  E-value: 1.63e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIisspkcQPSFAD-------NVCTLTLSSLEPSDTGAYTC 7649
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPV------RPDSAHkmlvrenGRHSLIIEPVTKRDAGIYTC 74
                            90
                    ....*....|....*..
gi 1958765569  7650 VAANVAGQDESSALLTV 7666
Cdd:cd05744      75 IARNRAGENSFNAELVV 91
fn3 pfam00041
Fibronectin type III domain;
30056-30134 1.64e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 1.64e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30056 VNVKEVSRDSVTITWEIPTiDGGAPVNNYIIEKREA-AMRAFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENIYGIGEP 30134
Cdd:pfam00041     6 LTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1523-1607 1.66e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 1.66e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   1523 KNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKyPRIRIEGTKGEAALKIDSTISQDSAWYTATAINKAGRDTTR 1602
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   1603 CKVNI 1607
Cdd:smart00410    81 TTLTV 85
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
19417-19501 1.68e-08

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 57.24  E-value: 1.68e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19417 PEQITIKAGKKLRVEAHVYGKPNPICKWKK-GEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQK 19495
Cdd:cd05763       6 PHDITIRAGSTARLECAATGHPTPQIAWQKdGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISAN 85

                    ....*.
gi 1958765569 19496 IKVTVM 19501
Cdd:cd05763      86 ATLTVL 91
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
31769-31968 1.69e-08

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 61.70  E-value: 1.69e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRcVETSSKKTFMAkfVKVKGTDQVL------VKKEISILNIARHRNILYLHESFESMEELVMIFEFISGL 31842
Cdd:cd13978       1 LGSGGFGTVSK-ARHVSWFGMVA--IKCLHSSPNCieerkaLLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENG 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 D---IFERINTS-AFELNERevvsYVRQVCEALEFLHSQN--IGHFDIRPENIIYQtrKNSIIKIIEFGQA--------- 31907
Cdd:cd13978      78 SlksLLEREIQDvPWSLRFR----IIHEIALGMNFLHNMDppLLHHDLKPENILLD--NHFHVKISDFGLSklgmksisa 151
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31908 --RQLKPGDNFRLLFTAPEYYAPEVHQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQQMI 31968
Cdd:cd13978     152 nrRRGTENLGGTPIYMAPEAFDDFNKKPT---SKSDVYSFAIVIWAVLTRKEPFENAINPLLI 211
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5-97 1.69e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 57.26  E-value: 1.69e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     5 APTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVIstsTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATN 84
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL---QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|...
gi 1958765569    85 GSGQATSTAELLV 97
Cdd:cd20976      78 AAGQVSCSAWVTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5229-5316 1.71e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 57.12  E-value: 1.71e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQ-LVSLQILKFVASDAGEYQCRVTNEV 5307
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80

                    ....*....
gi 1958765569  5308 GSSTCSARV 5316
Cdd:cd05744      81 GENSFNAEL 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32893-32975 1.80e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.74  E-value: 1.80e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  32893 RSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVE-LQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNYKGEASDYA 32971
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  32972 TLDV 32975
Cdd:smart00410    82 TLTV 85
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
27388-27481 1.81e-08

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 57.27  E-value: 1.81e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27388 LEYTEVVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSAS 27467
Cdd:cd05762       5 IQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQ 84
                            90
                    ....*....|....
gi 1958765569 27468 ATIRVQILDKPGPP 27481
Cdd:cd05762      85 AQVNLTVVDKPDPP 98
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
31767-31970 1.81e-08

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 61.93  E-value: 1.81e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCvETSSKKTFMAK--FVKVKGTDQVLVK-----------------KEISILNIARHRNILYLHESFE 31827
Cdd:cd05095      11 EKLGEGQFGEVHLC-EAEGMEKFMDKdfALEVSENQPVLVAvkmlradanknarndflKEIKIMSRLKDPNIIRLLAVCI 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31828 SMEELVMIFEFISGLDIFERI------NTSAFELNEReVVSY------VRQVCEALEFLHSQNIGHFDIRPENIIyqTRK 31895
Cdd:cd05095      90 TDDPLCMITEYMENGDLNQFLsrqqpeGQLALPSNAL-TVSYsdlrfmAAQIASGMKYLSSLNFVHRDLATRNCL--VGK 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31896 NSIIKIIEFGQARQLKPGDNFRLLFTA--P-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGI--NPFLAETNQQMIEN 31970
Cdd:cd05095     167 NYTIKIADFGMSRNLYSGDYYRIQGRAvlPiRWMSWESILLGKFTTASDVWAFGVTLWETLTFCreQPYSQLSDEQVIEN 246
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
24544-24625 1.85e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 56.98  E-value: 1.85e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24544 KGIVVRAGGSARIHIPFKGRPTPEITWSKEeGEFTD-----KVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSA 24618
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRD-GQVIStstlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86

                    ....*..
gi 1958765569 24619 FVTVKVL 24625
Cdd:cd20974      87 TAELLVL 93
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
31768-32030 1.87e-08

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 62.38  E-value: 1.87e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31768 DLGRGEFGIVH--RCVETSS-----KKTFMAKFVKVKGTDqvlVKKEISILNIARHRNILYLHESF--ESMEELVMIFEF 31838
Cdd:cd06635      32 EIGHGSFGAVYfaRDVRTSEvvaikKMSYSGKQSNEKWQD---IIKEVKFLQRIKHPNSIEYKGCYlrEHTAWLVMEYCL 108
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFErinTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFrl 31918
Cdd:cd06635     109 GSASDLLE---VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT--EPGQVKLADFGSASIASPANSF-- 181
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 lFTAPEYYAPEV------HQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAfqEISLEAMD 31992
Cdd:cd06635     182 -VGTPYWMAPEVilamdeGQYD---GKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSN--EWSDYFRN 255
                           250       260       270
                    ....*....|....*....|....*....|....*....
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPW-LKQRMDRVSTKVIR 32030
Cdd:cd06635     256 FVDSCLQKIPQDRPTSEELLKHMFvLRERPETVLIDLIQ 294
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9103-9171 1.88e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 56.18  E-value: 1.88e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9103 FKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATNDAGSALCTS 9171
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
1521-1607 1.95e-08

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 57.14  E-value: 1.95e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1521 KLKNVNIKEGSRLEMKVRATG-NPNPDIVWLKNSDIIVPHKYPRIRIEGTKGEAALKIDSTISQDSAWYTATAINKAGRD 1599
Cdd:cd05750       5 EMKSQTVQEGSKLVLKCEATSeNPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKD 84

                    ....*...
gi 1958765569  1600 TTRCKVNI 1607
Cdd:cd05750      85 TVTGNVTV 92
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4949-5038 1.96e-08

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 57.03  E-value: 1.96e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIA-ASDRYQIAF-VEGTASLEISRVDMNDAGNFTCRATNS 5026
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRdLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  5027 VGSKDSRGALIV 5038
Cdd:cd05893      81 QGRISCTGRLMV 92
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
31767-31970 1.96e-08

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 61.87  E-value: 1.96e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKF-VKVKGTDQVLVK-----------------KEISILNIARHRNILYLHESFES 31828
Cdd:cd05096      11 EKLGEGQFGEVHLCEVVNPQDLPTLQFpFNVRKGRPLLVAvkilrpdanknarndflKEVKILSRLKDPNIIRLLGVCVD 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31829 MEELVMIFEFISGLDIFERIntSAFELNERE--------------VVSY------VRQVCEALEFLHSQNIGHFDIRPEN 31888
Cdd:cd05096      91 EDPLCMITEYMENGDLNQFL--SSHHLDDKEengndavppahclpAISYssllhvALQIASGMKYLSSLNFVHRDLATRN 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31889 IIyqTRKNSIIKIIEFGQARQLKPGDNFRLLFTA--P-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS--GINPFLAET 31963
Cdd:cd05096     169 CL--VGENLTIKIADFGMSRNLYAGDYYRIQGRAvlPiRWMAWECILMGKFTTASDVWAFGVTLWEILMlcKEQPYGELT 246

                    ....*..
gi 1958765569 31964 NQQMIEN 31970
Cdd:cd05096     247 DEQVIEN 253
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
23-92 1.99e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 56.18  E-value: 1.99e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    23 ATFEAHISGSPVPEVSWFRDGQVISTSTLPGvqISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATST 92
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDS--RRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
fn3 pfam00041
Fibronectin type III domain;
25018-25103 2.01e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 2.01e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25018 GPPGTPFVTSVSKDQMLVQWHEPvNDGGSKVIGYHLEQKEKNSILWVKLNKIPIQDTKFKTTGLDEGLEYEFRVSAENIV 25097
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*.
gi 1958765569 25098 GIGKPS 25103
Cdd:pfam00041    80 GEGPPS 85
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
1254-1337 2.02e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 56.63  E-value: 2.02e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1254 KNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGeRYQMdfLQDgrASLRIPVVLPEDEGIYTAFASNIKGNAICSG 1333
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEI--LDD--HSLKIRKVTAGDMGSYTCVAENMVGKIEASA 79

                    ....
gi 1958765569  1334 KLYV 1337
Cdd:cd05725      80 TLTV 83
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
31777-32017 2.04e-08

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 60.82  E-value: 2.04e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31777 VHRCVETSSKKTFMAKFVKVKGTDQVLVkkeiSILNIARHRNILYLHESFESMEELVMIFEFISGlDIFERINTSAfELN 31856
Cdd:cd14022       9 VFRAVHLHSGEELVCKVFDIGCYQESLA----PCFCLPAHSNINQITEIILGETKAYVFFERSYG-DMHSFVRTCK-KLR 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31857 EREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLK-PGDNFRLLFTAPEYYAPEVHQHDV 31935
Cdd:cd14022      83 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRgHDDSLSDKHGCPAYVSPEILNTSG 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31936 VSS--ATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRLLVKERKSRMTASEALK 32013
Cdd:cd14022     163 SYSgkAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPE----TLSPKAKCLIRSILRREPSERLTSQEILD 238

                    ....
gi 1958765569 32014 HPWL 32017
Cdd:cd14022     239 HPWF 242
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
909-982 2.12e-08

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 56.44  E-value: 2.12e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569   909 VTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVS 982
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6915-6998 2.13e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 57.05  E-value: 2.13e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKL--RSTPEYRTYFTN-NVATLVFNKVGINDSGEYTCVAEN 6991
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKIESEyGVHVLHIRRVTVEDSAVYSAVAKN 80

                    ....*..
gi 1958765569  6992 SIGTAAS 6998
Cdd:cd20951      81 IHGEASS 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5884-5973 2.17e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 56.98  E-value: 2.17e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQI--LEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNE 5961
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVisTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  5962 SGVERCYAFLLV 5973
Cdd:cd20974      81 SGQATSTAELLV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
31549-31630 2.23e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.74  E-value: 2.23e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31549 VHALRGEVVSIKIPFSGKPDPVITWQK-GQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFGIDQKTVE 31627
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISN-VTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  31628 LDV 31630
Cdd:smart00410    83 LTV 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
104-193 2.25e-08

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 56.70  E-value: 2.25e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDfQISQEGDLY---SLLIAEAYPEDSGTYSVNATN 180
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTD-RISLYQDNCgriCLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569   181 SVGRATSTADLLV 193
Cdd:cd05892      80 EAGVVSCNARLDV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
14220-14288 2.26e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 56.18  E-value: 2.26e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14220 IELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVN-VCGRATAVV 14288
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
31055-31132 2.26e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 56.80  E-value: 2.26e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31055 TTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKM----SSDGRTHTLTVMTEEQ-EDEGVYTCVATNEVGEVETS 31129
Cdd:cd20956      12 TLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgdyvTSDGDVVSYVNISSVRvEDGGEYTCTATNDVGSVSHS 91

                    ...
gi 1958765569 31130 SKL 31132
Cdd:cd20956      92 ARI 94
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
1041-1127 2.28e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 56.63  E-value: 2.28e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1041 ISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGyRYKVSYNKQtgecrLVISMTFADDAGEYTIVIRNKHGE 1120
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDHS-----LKIRKVTAGDMGSYTCVAENMVGK 74

                    ....*..
gi 1958765569  1121 TSASASL 1127
Cdd:cd05725      75 IEASATL 81
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10808-11022 2.28e-08

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 63.25  E-value: 2.28e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10808 PPAKVPEIPKKPEEKVSVPVPKKEKAPPAKVPEvPKKPVPEEKAPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKkv 10887
Cdd:NF033839    292 PSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQ-LEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQ-- 368
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10888 eaPPAKAPEVPPKEVTPEKKVPvvppkkpeapppkvpeppkevvpekkvsmvppKRPEAPPAKV---PEASK-EVVPE-- 10961
Cdd:NF033839    369 --PEKPKPEVKPQPETPKPEVK--------------------------------PQPEKPKPEVkpqPEKPKpEVKPQpe 414
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10962 -KKVSVAPKKKPEAPAVK-VPEAPKKVV---PEKKVPVAAPkKPEAPAAEV---PEVPKAAV-PQKKIPE 11022
Cdd:NF033839    415 kPKPEVKPQPEKPKPEVKpQPEKPKPEVkpqPEKPKPEVKP-QPETPKPEVkpqPEKPKPEVkPQPEKPK 483
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
31048-31129 2.30e-08

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 56.64  E-value: 2.30e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31048 RKEMADVTTKLGEAAQLSCQI-VGRPLPDIKWYRFGKELV-QSRKYKMSSDGRthtLTVMTEEQEDEGVYTCVATNEVGE 31125
Cdd:cd05724       1 RVEPSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNlDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGE 77

                    ....
gi 1958765569 31126 VETS 31129
Cdd:cd05724      78 RESR 81
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
6925-6995 2.30e-08

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 56.45  E-value: 2.30e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  6925 EASVGDSVSLQCQVAGTPEITVSWFKGDTKLRStpEYRTYFTNnvATLVFNKVGINDSGEYTCVAENSIGT 6995
Cdd:cd05728      10 EADIGSSLRWECKASGNPRPAYRWLKNGQPLAS--ENRIEVEA--GDLRITKLSLSDSGMYQCVAENKHGT 76
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
31043-31134 2.31e-08

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 56.65  E-value: 2.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31043 EAPGvrkemaDVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKM-SSDGRTHTLTVMTEEQEDEGVYTCVATN 31121
Cdd:cd20990       5 QAPG------DLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMlVRENGVHSLIIEPVTSRDAGIYTCIATN 78
                            90
                    ....*....|...
gi 1958765569 31122 EVGEVETSSKLLL 31134
Cdd:cd20990      79 RAGQNSFNLELVV 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4401-4476 2.35e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 56.81  E-value: 2.35e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4401 GKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRIT-DADNKHSLELSNLTVQDRGVYSCKASNKFGADICQAELTI 4476
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
31769-31957 2.38e-08

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 60.97  E-value: 2.38e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKkEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERI 31848
Cdd:cd14065       1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFLK-EVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31849 NTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPEN-IIYQTRKNSIIKIIEFGQARQL------KPGDNFRL-LF 31920
Cdd:cd14065      80 KSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNcLVREANRGRNAVVADFGLAREMpdektkKPDRKKRLtVV 159
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958765569 31921 TAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGIN 31957
Cdd:cd14065     160 GSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVP 196
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
12180-12258 2.39e-08

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 56.75  E-value: 2.39e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12180 KLHDKTGVEKDEIILKCEVSKDVPV---KWFKDGEEIVPSPKHSVKTDGLRRI--LKIKKAELKDKGEYTCDC----GTD 12250
Cdd:cd05750       5 EMKSQTVQEGSKLVLKCEATSENPSpryRWFKDGKELNRKRPKNIKIRNKKKNseLQINKAKLEDSGEYTCVVenilGKD 84

                    ....*...
gi 1958765569 12251 TTKANVTV 12258
Cdd:cd05750      85 TVTGNVTV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1249-1337 2.40e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.82  E-value: 2.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMdfLQDGRA-SLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd20972       4 FIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQI--HQEGDLhSLIIAEAFEEDTGRYSCLATNSVG 81
                            90
                    ....*....|
gi 1958765569  1328 NAICSGKLYV 1337
Cdd:cd20972      82 SDTTSAEIFV 91
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
31765-31972 2.41e-08

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 61.23  E-value: 2.41e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHR-CVETSSKKT-FMA-KFVKVKGTDQVLVK--KEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05033       8 IEKVIGGGEFGEVCSgSLKLPGKKEiDVAiKTLKSGYSDKQRLDflTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYM 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 S--GLDIFERINTSAFELNEreVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPGDnfr 31917
Cdd:cd05033      88 EngSLDKFLRENDGKFTVTQ--LVGMLRGIASGMKYLSEMNYVHRDLAARNIL--VNSDLVCKVSDFGLSRRLEDSE--- 160
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31918 llftaPEY-----------YAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIM 31972
Cdd:cd05033     161 -----ATYttkggkipirwTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQDVIKAVE 222
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8706-8793 2.42e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 56.66  E-value: 2.42e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8706 FVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQ---RCNITTTEKSAILEILSSTVEDSGQYNCYIENAS 8782
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|.
gi 1958765569  8783 GKDSCSAQILI 8793
Cdd:cd20951      83 GEASSSASVVV 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1683-1754 2.42e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.82  E-value: 2.42e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  1683 ECRLTpiGDPTMVVEWLHDGKPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:cd20972      22 ECRVT--GNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1055-1124 2.45e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 56.18  E-value: 2.45e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1055 VVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYnkQTGECRLVISMTFADDAGEYTIVIRNKHGETSAS 1124
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRS--ELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
103-193 2.45e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 56.87  E-value: 2.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   103 PPNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDfQISQEGDLYSLLIAEAYPEDSGTYSVNATNSV 182
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569   183 GRATSTADLLV 193
Cdd:cd20976      80 GQVSCSAWVTV 90
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
31769-32014 2.50e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 61.43  E-value: 2.50e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKV----KGTDQVLvkKEISILNIARHRNILYLHESF---------ESMEE--LV 31833
Cdd:cd14048      14 LGRGGFGVVFEAKNKVDDCNYAVKRIRLpnneLAREKVL--REVRALAKLDHPGIVRYFNAWlerppegwqEKMDEvyLY 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINTSAfELNERE---VVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQL 31910
Cdd:cd14048      92 IQMQLCRKENLKDWMNRRC-TMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSL--DDVVKVGDFGLVTAM 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNFRLLFTAPE-------------YYAPEVHQHDVVSSATDMWSLGTLVYVLlsgINPFlaETNQQMIENIMNAEYT 31977
Cdd:cd14048     169 DQGEPEQTVLTPMPayakhtgqvgtrlYMSPEQIHGNQYSEKVDIFALGLILFEL---IYSF--STQMERIRTLTDVRKL 243
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1958765569 31978 FDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKH 32014
Cdd:cd14048     244 KFPALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
3199-3288 2.52e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 56.74  E-value: 2.52e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHD-GQEYTLLLIEAFPEDAAVYTCEAKNDY 3277
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVReNGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  3278 GVATTSASLSV 3288
Cdd:cd05744      81 GENSFNAELVV 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
3589-3667 2.53e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 56.25  E-value: 2.53e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3589 APGIPAVFEYLVHGEPAPTVLWFKED--MPLYTnvcYTIIHNpdgsGTFIVNDPQRGDSGLYICKAENLWGTSTCTAELL 3666
Cdd:cd05725      10 LVDDSAEFQCEVGGDPVPTVRWRKEDgeLPKGR---YEILDD----HSLKIRKVTAGDMGSYTCVAENMVGKIEASATLT 82

                    .
gi 1958765569  3667 V 3667
Cdd:cd05725      83 V 83
I-set pfam07679
Immunoglobulin I-set domain;
31554-31630 2.55e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 56.50  E-value: 2.55e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31554 GEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFGIDQKTVELDV 31630
Cdd:pfam07679    15 GESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISN-VQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7669-7759 2.59e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.82  E-value: 2.59e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7669 PPSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTNDA 7748
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  7749 GSASCTTHLFV 7759
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
1807-1889 2.59e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 56.75  E-value: 2.59e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNG-QLIRKSKRFRVRYDGiHYLDIVDCKSYDTGEVKVTAEN-PEGVTEHK 1884
Cdd:cd20970       9 SFTVTAREGENATFMCRAEGSPEPEISWTRNGnLIIEFNTRYIVRENG-TTLTIRNIRRSDMGIYLCIASNgVPGSVEKR 87

                    ....*
gi 1958765569  1885 VKLEI 1889
Cdd:cd20970      88 ITLQV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
23464-23542 2.60e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 56.39  E-value: 2.60e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23464 INIRAGGSLRLFVPIKGRPTPEVKWGKVD-------GEIRdaaiIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSA 23536
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDkaftateGRVR----VESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHA 80

                    ....*.
gi 1958765569 23537 FVTVRV 23542
Cdd:cd05894      81 SLFVKV 86
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4684-4746 2.62e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 55.80  E-value: 2.62e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  4684 ALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEVG 4746
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
fn3 pfam00041
Fibronectin type III domain;
29753-29839 2.64e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 2.64e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29753 SQPGIPEGVGAGKEHIIIQWTKPEsDGGNEISNYLVDKREKKSL-RWTRVNKDYVVydTRLKVTSLMEGCDYQFRVTAVN 29831
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGePWNEITVPGTT--TSVTLTGLKPGTEYEVRVQAVN 77

                    ....*...
gi 1958765569 29832 SAGNSEPS 29839
Cdd:pfam00041    78 GGGEGPPS 85
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
31767-31975 2.65e-08

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 60.83  E-value: 2.65e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKV-KGTDQVLVKKEI----SILNIARHRNILYLHESFESmEELVMIFEFISG 31841
Cdd:cd05060       1 KELGHGNFGSVRKGVYLMKSGKEVEVAVKTlKQEHEKAGKKEFlreaSVMAQLDHPCIVRLIGVCKG-EPLMLVMELAPL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 --LDIFERINTsafELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLL 31919
Cdd:cd05060      80 gpLLKYLKKRR---EIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ--AKISDFGMSRALGAGSDYYRA 154
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31920 FTA---P-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIMNAE 31975
Cdd:cd05060     155 TTAgrwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESGE 215
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23749-23830 2.66e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.36  E-value: 2.66e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23749 SSYSVQVGQDLKIEVPISGRPKPSISWTKDGA-PLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAI 23827
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569  23828 EII 23830
Cdd:smart00410    82 TLT 84
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6-97 2.67e-08

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 56.64  E-value: 2.67e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNG 85
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569    86 SGQATSTAELLV 97
Cdd:cd05893      81 QGRISCTGRLMV 92
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
31760-31971 2.74e-08

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 60.66  E-value: 2.74e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIAEDLGRGEFGIVHRCVETSSKktFMAKFVKVKGTDQVLVKkEISILNIARHRNIL-----YLHESfesmeeLVM 31834
Cdd:cd05083       5 LQKLTLGEIIGEGEFGAVLQGEYMGQK--VAVKNIKCDVTAQAFLE-ETAVMTKLQHKNLVrllgvILHNG------LYI 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINTSA-FELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQAR-QLKP 31912
Cdd:cd05083      76 VMELMSKGNLVNFLRSRGrALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNIL--VSEDGVAKISDFGLAKvGSMG 153
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31913 GDNFRLlftAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05083     154 VDNSRL---PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPYPKMSVKEVKEAV 210
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
6929-6996 2.74e-08

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 56.46  E-value: 2.74e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6929 GDSVSLQCQVAGTPEITVSWFKGDTKLrstPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTA 6996
Cdd:cd05876      10 GQSLVLECIAEGLPTPTVKWLRPSGPL---PPDRVKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSA 74
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
2037-2128 2.75e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.44  E-value: 2.75e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2037 APKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYwPEDNVCELVIRDVTAEDSASIMVKAINI 2116
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIH-QEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  2117 AGETSSHAFLLV 2128
Cdd:cd20972      80 VGSDTTSAEIFV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7107-7197 2.77e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 56.66  E-value: 2.77e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRP---GGNYTITCVGNTPHLRILKVGKGDSGQYTCQATN 7183
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  7184 DVGKDMCSAQLSVK 7197
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4948-5036 2.79e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 56.60  E-value: 2.79e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4948 APLFTKPlRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSV 5027
Cdd:cd05747       4 ATILTKP-RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ....*....
gi 1958765569  5028 GSKDSRGAL 5036
Cdd:cd05747      83 GKQEAQFTL 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
24824-24913 2.83e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 56.35  E-value: 2.83e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVN--VEETATSTILhIKESSKDDFGKYSVTATNN 24901
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmlVRENGRHSLI-IEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569 24902 AGTATENLSVIV 24913
Cdd:cd05744      80 AGENSFNAELVV 91
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
31761-31970 2.85e-08

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 61.53  E-value: 2.85e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCvetssKKTFMAKFVKVKGTDQ------VLVK---------------KEISILNIARHRNI 31819
Cdd:cd05097       5 QQLRLKEKLGEGQFGEVHLC-----EAEGLAEFLGEGAPEFdgqpvlVAVKmlradvtktarndflKEIKIMSRLKNPNI 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31820 LYLHESFESMEELVMIFEFISGLDIFE-----RINTSAFELNEREVVSYVR------QVCEALEFLHSQNIGHFDIRPEN 31888
Cdd:cd05097      80 IRLLGVCVSDDPLCMITEYMENGDLNQflsqrEIESTFTHANNIPSVSIANllymavQIASGMKYLASLNFVHRDLATRN 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31889 IIYQtrKNSIIKIIEFGQARQLKPGDNFRLLFTA--P-EYYAPEVHQHDVVSSATDMWSLGTLVYVL--LSGINPFLAET 31963
Cdd:cd05097     160 CLVG--NHYTIKIADFGMSRNLYSGDYYRIQGRAvlPiRWMAWESILLGKFTTASDVWAFGVTLWEMftLCKEQPYSLLS 237

                    ....*..
gi 1958765569 31964 NQQMIEN 31970
Cdd:cd05097     238 DEQVIEN 244
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6547-6622 2.88e-08

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 56.42  E-value: 2.88e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  6547 GSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKfSFYNkiSSLKILSVEK-EDAGTYTFQVQNNVGKSS 6622
Cdd:cd20958       8 GNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQR-VFPN--GTLVIENVQRsSDEGEYTCTARNQQGQSA 81
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7107-7196 2.94e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 56.31  E-value: 2.94e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPV--SIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNtphLRILKVGKGDSGQYTCQATND 7184
Cdd:cd04969       1 PDFELNPVkkKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGS---LKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569  7185 VGKDMCSAQLSV 7196
Cdd:cd04969      78 FGKANSTGSLSV 89
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
6914-7002 2.95e-08

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 56.55  E-value: 2.95e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6914 PPYFVteLEPLEASV--GDSVSLQCQVAGTPEITVSWFKGdtkLRSTP-EYRTY-FTNNV-----ATLVFNKVGINDSGE 6984
Cdd:cd20954       1 PPRWI--VEPVDANVaaGQDVMLHCQADGFPTPTVTWKKA---TGSTPgEYKDLlYDPNVrilpnGTLVFGHVQKENEGH 75
                            90
                    ....*....|....*...
gi 1958765569  6985 YTCVAENSIGTAASKTVF 7002
Cdd:cd20954      76 YLCEAKNGIGSGLSKVIF 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
31440-31531 2.97e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 56.25  E-value: 2.97e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQ-SNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEfkggyHQLIIASVTDDDATVYQVRATN 31518
Cdd:cd20978       1 PKFIQKPEKNVVVKGgQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED-----GTLTIINVQPEDTGYYGCVATN 75
                            90
                    ....*....|...
gi 1958765569 31519 QGGSVSGTASLEV 31531
Cdd:cd20978      76 EIGDIYTETLLHV 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7294-7377 2.98e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 56.35  E-value: 2.98e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDT-SLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRhSLIIEPVTKRDAGIYTCIARNRA 80

                    ....*
gi 1958765569  7373 GSDTC 7377
Cdd:cd05744      81 GENSF 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
6540-6629 2.98e-08

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 56.32  E-value: 2.98e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6540 AVIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKhKFSFYNKIS---SLKILSVEKEDAGTYTFQVQN 6616
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTD-RISLYQDNCgriCLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569  6617 NVGKSSCTAVVDV 6629
Cdd:cd05892      80 EAGVVSCNARLDV 92
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
31761-32017 2.99e-08

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 61.18  E-value: 2.99e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVK-VKGTDQVlVKKEISILN-IARHRNI-----LYLHESFESMEELV 31833
Cdd:cd06638      18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDpIHDIDEE-IEAEYNILKaLSDHPNVvkfygMYYKKDVKNGDQLW 96
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISG---LDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQL 31910
Cdd:cd06638      97 LVLELCNGgsvTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGG--VKLVDFGVSAQL 174
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KpgdNFRL---------LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGiNPFLAETN--QQMIENIMNAEYTFD 31979
Cdd:cd06638     175 T---STRLrrntsvgtpFWMAPEVIACEQQLDSTYDARCDVWSLGITAIELGDG-DPPLADLHpmRALFKIPRNPPPTLH 250
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1958765569 31980 EEAFQeiSLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd06638     251 QPELW--SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
4572-4663 3.01e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 56.49  E-value: 3.01e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4572 PPSFVKkVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTvRMSFANSEAILDITDVKVDDSGTYSCEATND 4651
Cdd:cd20976       1 APSFSS-VPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  4652 AGSDSCSTEVVI 4663
Cdd:cd20976      79 AGQVSCSAWVTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7490-7570 3.07e-08

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 56.06  E-value: 3.07e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7490 MTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGKSSCTVSVH 7569
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569  7570 V 7570
Cdd:cd05748      82 V 82
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8327-8429 3.08e-08

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 56.89  E-value: 3.08e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8327 PPQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIvRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKND 8406
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQI-QEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENK 79
                            90       100
                    ....*....|....*....|...
gi 1958765569  8407 AGVQECYATLsvlepaTIVEKPE 8429
Cdd:cd05762      80 LGSRQAQVNL------TVVDKPD 96
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
33083-33162 3.10e-08

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 56.48  E-value: 3.10e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33083 TVHEGESARFSCDTDGEPVPTVTWLRGGQVVStSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQFTLTV 33162
Cdd:cd05730      14 TANLGQSVTLACDADGFPEPTMTWTKDGEPIE-SGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
4386-4476 3.13e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 56.49  E-value: 3.13e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4386 PPTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDcRITDADNKHSLELSNLTVQDRGVYSCKASNKF 4465
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  4466 GADICQAELTI 4476
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
9003-9078 3.15e-08

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 56.19  E-value: 3.15e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  9003 GESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLNI 9078
Cdd:cd20949      14 GQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQERTV 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
22660-22750 3.17e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 56.59  E-value: 3.17e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22660 PAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTT--RVNAESTENNSLLTIKEACREDVGHYTVKLTNS 22737
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 22738 AGEATETLNVIVL 22750
Cdd:cd20974      81 SGQATSTAELLVL 93
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
1052-1127 3.18e-08

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 56.07  E-value: 3.18e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1052 GGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKqtgecrLVISMTFADDAGEYTIVIRNKHGETSASASL 1127
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD------LRITKLSLSDSGMYQCVAENKHGTIYASAEL 83
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
33079-33162 3.19e-08

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 56.45  E-value: 3.19e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33079 PRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARH--QVTTAKYkSTFEISSVQASDEGNYSVVVENTDGKQEA 33156
Cdd:cd05737       8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCnlKVEAGRT-VYFTINGVSSEDSGKYGLVVKNKYGSETS 86

                    ....*.
gi 1958765569 33157 QFTLTV 33162
Cdd:cd05737      87 DVTVSV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8140-8218 3.19e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.03  E-value: 3.19e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8140 PPRFIKKLdQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:pfam13927     1 KPVITVSP-SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
19703-19790 3.24e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 3.24e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19703 DPPGKPEVVDVTKNSASLIWARPKhDGGSKIIGYFVEACKL-PGDKWVRCNTTPHQIpleEYTATGLEENAQYQFRAIAK 19781
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnSGEPWNEITVPGTTT---SVTLTGLKPGTEYEVRVQAV 76

                    ....*....
gi 1958765569 19782 TAVNISQPS 19790
Cdd:pfam00041    77 NGGGEGPPS 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5510-5600 3.32e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 56.49  E-value: 3.32e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5510 PPSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISAsDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKA 5589
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQY-AADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  5590 GHSQCSGHLTV 5600
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
31045-31125 3.33e-08

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 56.04  E-value: 3.33e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31045 PGVRkEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGrthTLTVMT-EEQEDEGVYTCVATNEV 31123
Cdd:cd20958       2 PFIR-PMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNG---TLVIENvQRSSDEGEYTCTARNQQ 77

                    ..
gi 1958765569 31124 GE 31125
Cdd:cd20958      78 GQ 79
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
8433-8511 3.40e-08

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 56.37  E-value: 3.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8433 VTTGDTCTLEC-MVSGTPELSTKWFKDGKELT--GDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCTVSI 8509
Cdd:cd05750      11 VQEGSKLVLKCeATSENPSPRYRWFKDGKELNrkRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNV 90

                    ..
gi 1958765569  8510 QV 8511
Cdd:cd05750      91 TV 92
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
31052-31134 3.44e-08

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 56.39  E-value: 3.44e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31052 ADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVmteEQEDEGVYTCVATNEVGEVETSSK 31131
Cdd:cd20957       9 PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSV---KREDKGMYQCFVRNDGDSAQATAE 85

                    ...
gi 1958765569 31132 LLL 31134
Cdd:cd20957      86 LKL 88
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
31769-31968 3.45e-08

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 60.80  E-value: 3.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILyLHESFESMEELVMIFEFISGLDIFERI 31848
Cdd:cd14150       8 IGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGSSLYRHL 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31849 NTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQA---------RQL-KPGDNfrL 31918
Cdd:cd14150      87 HVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLH--EGLTVKIGDFGLAtvktrwsgsQQVeQPSGS--I 162
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 LFTAPEYYapEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMI 31968
Cdd:cd14150     163 LWMAPEVI--RMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQI 210
fn3 pfam00041
Fibronectin type III domain;
26100-26183 3.47e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 3.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26100 GPPGTPKVVHATKSTMVVSWQVPvNDGGSQVIGYHLEYKERSSILWSKANKVLIADTQMKVSGLDEGLLYEYRVYAENIA 26179
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....
gi 1958765569 26180 GIGK 26183
Cdd:pfam00041    80 GEGP 83
fn3 pfam00041
Fibronectin type III domain;
24629-24712 3.47e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 3.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24629 GPPQNLAVKEVRKDSVLLVWEPPIiDGGAKVKNYVI---DKRESTRKAYANVSSkcSKTSFKVENLTEGAIYYFRVMAEN 24705
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVeyrPKNSGEPWNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77

                    ....*..
gi 1958765569 24706 EFGVGVP 24712
Cdd:pfam00041    78 GGGEGPP 84
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7582-7666 3.58e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 56.36  E-value: 3.58e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7582 KLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVcTLTLSSLEPSDTGAYTCVAAN-VAGQDES 7660
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGT-TLTIRNIRRSDMGIYLCIASNgVPGSVEK 86

                    ....*.
gi 1958765569  7661 SALLTV 7666
Cdd:cd20970      87 RITLQV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
19416-19500 3.59e-08

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 56.46  E-value: 3.59e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19416 MPEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIhKADSS--SVLIIKDVTRKDSGYYSLTAENSSGTDT 19493
Cdd:cd05891       7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSV-KLEQGkyASLTIKGVTSEDSGKYSINVKNKYGGET 85

                    ....*..
gi 1958765569 19494 QKIKVTV 19500
Cdd:cd05891      86 VDVTVSV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
8988-9078 3.69e-08

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 56.48  E-value: 3.69e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8988 PPFFDIPLAPVDAV--VGESADLECHVTGTQPIKVTWAKDNREIRSGGNyQISYLENSAHLTIVKVDKGDSGQYTCYAIN 9065
Cdd:cd05730       1 PPTIRARQSEVNATanLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAEN 79
                            90
                    ....*....|...
gi 1958765569  9066 EVGKDSCTAQLNI 9078
Cdd:cd05730      80 KAGEQEAEIHLKV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8994-9078 3.83e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 56.04  E-value: 3.83e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8994 PLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENS-AHLTIVKVDKGDSGQYTCYAINEVGKDSC 9072
Cdd:cd20973       3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGlCSLIISDVCGDDSGKYTCKAVNSLGEATC 82

                    ....*.
gi 1958765569  9073 TAQLNI 9078
Cdd:cd20973      83 SAELTV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
27791-27875 3.85e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 56.21  E-value: 3.85e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27791 TSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEK--NLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQpKSS 27868
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQ-ATS 86

                    ....*..
gi 1958765569 27869 TVSVKVL 27875
Cdd:cd20974      87 TAELLVL 93
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
902-979 4.00e-08

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 56.07  E-value: 4.00e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   902 LVSGLKNV-TVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSG-IARLMIREAFAEDSGRFTCSAVNEAG 979
Cdd:cd05891       3 VIGGLPDVvTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGkYASLTIKGVTSEDSGKYSINVKNKYG 82
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
1422-1506 4.00e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 56.21  E-value: 4.00e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1422 KPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKE-DGTQSLIIVPAlpSDSGEWTVVAQNRAGKST 1500
Cdd:cd05747       9 KPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEyKSTFEISKVQM--SDEGNYTVVVENSEGKQE 86

                    ....*.
gi 1958765569  1501 ISVTLT 1506
Cdd:cd05747      87 AQFTLT 92
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
31806-32022 4.04e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 61.28  E-value: 4.04e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31806 KEISILNIARHRNILYL------HESFESMEELVMIFEFISGlDIFERINtsaFELnEREVVSY-VRQVCEALEFLHSQN 31878
Cdd:cd07850      48 RELVLMKLVNHKNIIGLlnvftpQKSLEEFQDVYLVMELMDA-NLCQVIQ---MDL-DHERMSYlLYQMLCGIKHLHSAG 122
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31879 IGHFDIRPENIIYQTRknSIIKIIEFGQARqlKPGDNFRLL-FTAPEYY-APEV-----HQHDVvssatDMWSLG----- 31946
Cdd:cd07850     123 IIHRDLKPSNIVVKSD--CTLKILDFGLAR--TAGTSFMMTpYVVTRYYrAPEVilgmgYKENV-----DIWSVGcimge 193
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31947 -----------------TLVYVLLSGINPFLAETNQQMIENIM-----NAEYTFDE---------EAFQEISL---EAMD 31992
Cdd:cd07850     194 mirgtvlfpgtdhidqwNKIIEQLGTPSDEFMSRLQPTVRNYVenrpkYAGYSFEElfpdvlfppDSEEHNKLkasQARD 273
                           250       260       270
                    ....*....|....*....|....*....|
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWLKQRMD 32022
Cdd:cd07850     274 LLSKMLVIDPEKRISVDDALQHPYINVWYD 303
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
914-992 4.06e-08

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 56.12  E-value: 4.06e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569   914 GESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAVQVS 992
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVEDS 93
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
31767-31975 4.07e-08

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 60.51  E-value: 4.07e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK-----EISILNIARHRNILYLHESFESMEeLVMIFEFISG 31841
Cdd:cd05056      12 RCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVRekflqEAYIMRQFDHPHIVKLIGVITENP-VWIVMELAPL 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd05056      91 GELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDC--VKLGDFGLSRYMEDESYYKASKG 168
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31922 A-P-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIMNAE 31975
Cdd:cd05056     169 KlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNNDVIGRIENGE 225
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
20896-20981 4.08e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 56.00  E-value: 4.08e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20896 IKDGLTVKAGDSIVLSaISILGKPLPKSSWSKAGKDIR-PSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKE 20974
Cdd:cd05894       1 AENTIVVVAGNKLRLD-VPISGEPAPTVTWSRGDKAFTaTEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDH 79

                    ....*..
gi 1958765569 20975 EHVKVSV 20981
Cdd:cd05894      80 ASLFVKV 86
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
31054-31132 4.10e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 56.05  E-value: 4.10e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31054 VTTKLGEAAQLSCQIV-GRPLPDIKWYRFGKELVQSRKYKMSSDG-RTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSK 31131
Cdd:pfam00047     6 VTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRtTQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTS 85

                    .
gi 1958765569 31132 L 31132
Cdd:pfam00047    86 L 86
fn3 pfam00041
Fibronectin type III domain;
18518-18596 4.14e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 4.14e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18518 QNLKVSNVTKENCTISWEnPLDNGGSEITNFIVEYRKPNQKGW--SIVASDVTKRLIKANLLANNEYYFRVCAENKVGVG 18595
Cdd:pfam00041     4 SNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPwnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    .
gi 1958765569 18596 P 18596
Cdd:pfam00041    83 P 83
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
899-979 4.16e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 56.21  E-value: 4.16e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    .
gi 1958765569   979 G 979
Cdd:cd05747      83 G 83
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
33416-33505 4.18e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.05  E-value: 4.18e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAG 33495
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81
                            90
                    ....*....|
gi 1958765569 33496 SVSSSCKLTI 33505
Cdd:cd20972      82 SDTTSAEIFV 91
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
17745-17818 4.20e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 56.00  E-value: 4.20e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 17745 GDTLRLSAIIKGVPFPKVTWKKEDR---EAPTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd05894      10 GNKLRLDVPISGEPAPTVTWSRGDKaftATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5045-5131 4.21e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 55.86  E-value: 4.21e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5045 VTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGscyiTKEASESSLELYAVKTTDSGTYTCKVSNVAGSVE 5124
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGR----YEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  5125 CSANLFV 5131
Cdd:cd05725      77 ASATLTV 83
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8234-8315 4.26e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 4.26e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8234 PPVFRKKpFPVETLK-GADVHLECELQGTPPFQVSWYKDKRELRSGKKYKI----MSENLLTS-IHILNVDTADIGEYQC 8307
Cdd:cd20956       1 APVLLET-FSEQTLQpGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgdyvTSDGDVVSyVNISSVRVEDGGEYTC 79

                    ....*...
gi 1958765569  8308 KATNDVGS 8315
Cdd:cd20956      80 TATNDVGS 87
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
1261-1337 4.27e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 55.93  E-value: 4.27e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  1261 GMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERyqMDFLQDGraSLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYV 1337
Cdd:cd04969      17 GGDVIIECKPKASPKPTISWSKGTELLTNSSR--ICILPDG--SLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
7211-7288 4.27e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 56.05  E-value: 4.27e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7211 VAKQGESIQLECKIS-GSPEIKVVWFRNDSELHESWKYNMSFVN-SVALLTINEASVEDTGDYICEAHNGVGHASCSTAL 7288
Cdd:pfam00047     7 TVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRtTQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
24824-24913 4.31e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 55.93  E-value: 4.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPF--NTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATstiLHIKESSKDDFGKYSVTATNN 24901
Cdd:cd04969       1 PDFELNPvkKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGS---LKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569 24902 AGTATENLSVIV 24913
Cdd:cd04969      78 FGKANSTGSLSV 89
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
31054-31127 4.33e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 56.21  E-value: 4.33e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31054 VTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVE 31127
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQE 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6165-6255 4.39e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.05  E-value: 4.39e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6165 PPSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTNDV 6244
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  6245 GSDSCTTMLLV 6255
Cdd:cd20972      81 GSDTTSAEIFV 91
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
31764-31971 4.40e-08

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 60.15  E-value: 4.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31764 MIAEDLGRGEFGIVHRCvetsskktfmakfvKVKGTDQVLVK-------------KEISILNIARHRNILYLHESFESME 31830
Cdd:cd05059       7 TFLKELGSGQFGVVHLG--------------KWRGKIDVAIKmikegsmseddfiEEAKVMMKLSHPKLVQLYGVCTKQR 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 ELVMIFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQL 31910
Cdd:cd05059      73 PIFIVTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCL--VGEQNVVKVSDFGLARYV 150
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31911 -------KPGDNFRLlftapEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05059     151 lddeytsSVGTKFPV-----KWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHI 214
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
3199-3288 4.41e-08

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 55.93  E-value: 4.41e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGF-KCKFLHDGQEYTLLLIE-AFPEDAAVYTCEAKND 3276
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTdRISLYQDNCGRICLLIQnANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  3277 YGVATTSASLSV 3288
Cdd:cd05892      81 AGVVSCNARLDV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
32319-32383 4.41e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 55.65  E-value: 4.41e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 32319 EGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGlDYYALHIRDTLPEDTGYYRVTATN 32383
Cdd:pfam13927    15 EGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSG-SNSTLTISNVTRSDAGTYTCVASN 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
31059-31135 4.47e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.89  E-value: 4.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRFGKEL---VQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSKLLLQ 31135
Cdd:cd20951      15 KSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVVE 94
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7308-7382 4.48e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 56.04  E-value: 4.48e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7308 GSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFK-VTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCACTVK 7382
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQiDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
33086-33162 4.50e-08

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 55.33  E-value: 4.50e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33086 EGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAkykSTFEISSVQASDEGNYSVVVENTDGKQEAQFTLTV 33162
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS---GTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7771-7852 4.50e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 55.59  E-value: 4.50e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7771 DTSVETGSPIVLEATYSGTPPIAVSWLKNEY-PLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEAGQDICEAL 7849
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569   7850 VSV 7852
Cdd:smart00410    83 LTV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5978-6066 4.57e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 55.86  E-value: 4.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5978 QIIEKAKSVDVTEkdPVTLECVVAGTPELKVKWLKDGKQIVpSRYFSMSFENNvaSFRIQSVMKQDSGQYTFKVENDFGS 6057
Cdd:cd20978       5 QKPEKNVVVKGGQ--DVTLPCQVTGVPQPKITWLHNGKPLQ-GPMERATVEDG--TLTIINVQPEDTGYYGCVATNEIGD 79

                    ....*....
gi 1958765569  6058 SSCDAYLRV 6066
Cdd:cd20978      80 IYTETLLHV 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6073-6162 4.57e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.96  E-value: 4.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHEN-TVSLEVSNLELEDTANYTCKVSNVA 6151
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  6152 GDNACSGILTV 6162
Cdd:cd05744      81 GENSFNAELVV 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
33075-33162 4.60e-08

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 55.97  E-value: 4.60e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33075 ILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGqvVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQ 33154
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDG--VPLLGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569 33155 EAQFTLTV 33162
Cdd:cd20952      80 TWSAVLDV 87
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
31791-31959 4.65e-08

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 59.82  E-value: 4.65e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31791 AKFVKVKGTDQVLVKK-------EISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERINtSAFELNEREVVSY 31863
Cdd:cd14059       8 AVFLGKFRGEEVAVKKvrdeketDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLR-AGREITPSLLVDW 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31864 VRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLkpGDN-FRLLFTAP-EYYAPEVHQHDVVSSATD 31941
Cdd:cd14059      87 SKQIASGMNYLHLHKIIHRDLKSPNVLVTY--NDVLKISDFGTSKEL--SEKsTKMSFAGTvAWMAPEVIRNEPCSEKVD 162
                           170
                    ....*....|....*...
gi 1958765569 31942 MWSLGTLVYVLLSGINPF 31959
Cdd:cd14059     163 IWSFGVVLWELLTGEIPY 180
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5134-5225 4.65e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.05  E-value: 4.65e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5134 PATFTEKLEpSQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNE 5213
Cdd:cd20972       1 PPQFIQKLR-SQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  5214 AGSDHCTSIVIV 5225
Cdd:cd20972      80 VGSDTTSAEIFV 91
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
31759-32026 4.69e-08

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 60.84  E-value: 4.69e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK--------KEISILNIARHRNILYLHESFE-SM 31829
Cdd:cd14040       4 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKenyhkhacREYRIHKELDHPRIVKLYDYFSlDT 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQN--IGHFDIRPENIIY-QTRKNSIIKIIEFGQ 31906
Cdd:cd14040      84 DTFCTVLEYCEGNDLDFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTACGEIKITDFGL 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARQLKPG----DNFRLLFTAPE---YYAPEV----HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMI--ENIMN 31973
Cdd:cd14040     163 SKIMDDDsygvDGMDLTSQGAGtywYLPPECfvvgKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqENTIL 242
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31974 AEYTFDEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWLKQRMDRVST 32026
Cdd:cd14040     243 KATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRRSNS 295
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
14898-14975 4.72e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 55.65  E-value: 4.72e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 14898 KPTIDLETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLEN 14975
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3019-3103 4.74e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.89  E-value: 4.74e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3019 EFRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRI---KIQKEKYVHRLLIPSARMSDAGKYTVVA--- 3091
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYKNGVPIDPSSIPgkyKIESEYGVHVLHIRRVTVEDSAVYSAVAkni 81
                            90
                    ....*....|...
gi 1958765569  3092 -GGNMSTANLFVE 3103
Cdd:cd20951      82 hGEASSSASVVVE 94
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
4587-4665 4.75e-08

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 56.12  E-value: 4.75e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4587 PGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVIKE 4665
Cdd:cd05736      14 PGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
18431-18510 4.79e-08

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 55.58  E-value: 4.79e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18431 TVRVGQTIRILARVKGRPEPDITWSKEGK-VLVKDKRvdlIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVN 18509
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKDGVpLLGKDER---ITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLD 86

                    .
gi 1958765569 18510 V 18510
Cdd:cd20952      87 V 87
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
18427-18510 4.80e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 55.93  E-value: 4.80e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18427 RDVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRvdlIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd04969       9 KKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSR---ICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTG 85

                    ....
gi 1958765569 18507 IVNV 18510
Cdd:cd04969      86 SLSV 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7856-7945 4.89e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.96  E-value: 4.89e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNN-VASLVINKVDHSDVGEYTCKAENSV 7934
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  7935 GAVASSAVLVI 7945
Cdd:cd05744      81 GENSFNAELVV 91
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
31769-31972 5.02e-08

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 59.99  E-value: 5.02e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVhrcvetsskktFMAKFvkvKGTDQVLVK-------------KEISILNIARHRNILYLHESFESMEELVMI 31835
Cdd:cd05034       3 LGAGQFGEV-----------WMGVW---NGTTKVAVKtlkpgtmspeaflQEAQIMKKLRHDKLVQLYAVCSDEEPIYIV 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPGD 31914
Cdd:cd05034      69 TELMSKGSLLDYLRTGEGRaLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNIL--VGENNVCKVADFGLARLIEDDE 146
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31915 nfrllFTAPE-------YYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENIM 31972
Cdd:cd05034     147 -----YTAREgakfpikWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQVE 207
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
13154-13242 5.03e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.89  E-value: 5.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13154 IVVPLKDTKVKEQQEAVFNCEVNTE-GAKAKWFRNDEAI---FDSSKYIILQKDLVYTLRIRDARLDDQANFSVSLTNHR 13229
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|...
gi 1958765569 13230 GEnVKSAANLIVE 13242
Cdd:cd20951      83 GE-ASSSASVVVE 94
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
9003-9080 5.08e-08

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 55.73  E-value: 5.08e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9003 GESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLNIKE 9080
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
26706-26787 5.11e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 55.82  E-value: 5.11e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26706 KTLTVKAGSSFTMTVPFRGRPIPNVSWSKP----DTDLRTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMT 26781
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDgqviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*.
gi 1958765569 26782 FVVKVL 26787
Cdd:cd20974      88 AELLVL 93
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
31066-31134 5.15e-08

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 55.67  E-value: 5.15e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31066 CQIVGRPLPDIKWYRFGKELVQSRKYKMSSDgrtHTLTVMTEEQEDEGVYTCVATNEVGEVETSSKLLL 31134
Cdd:cd05723      19 CEVTGKPTPTVKWVKNGDVVIPSDYFKIVKE---HNLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
31805-31971 5.18e-08

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 60.41  E-value: 5.18e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31805 KKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERI----------------NTSAFELNEREVVSYVRQVC 31868
Cdd:cd05090      55 QQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLimrsphsdvgcssdedGTVKSSLDHGDFLHIAIQIA 134
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31869 EALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRL---LFTAPEYYAPEVHQHDVVSSATDMWSL 31945
Cdd:cd05090     135 AGMEYLSSHFFVHKDLAARNILVGEQLH--VKISDLGLSREIYSSDYYRVqnkSLLPIRWMPPEAIMYGKFSSDSDIWSF 212
                           170       180
                    ....*....|....*....|....*..
gi 1958765569 31946 GTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05090     213 GVVLWEIFSfGLQPYYGFSNQEVIEMV 239
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6839-6902 5.19e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 55.03  E-value: 5.19e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  6839 IILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAGR 6902
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33440-33505 5.23e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 5.23e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 33440 TGEPQPTVTWTKDGKAIAQSSKYKLSndkeEFI---------LEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd20956      26 SGNPLPQITWTLDGFPIPESPRFRVG----DYVtsdgdvvsyVNISSVRVEDGGEYTCTATNDVGSVSHSARINV 96
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
19128-19207 5.41e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 55.62  E-value: 5.41e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVRKGQVDL---VDTMAFlVIPNSTRDDSGKYSLTLVNPAGEKAVFVN 19204
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVesyKDLSSF-VIEGAEREDEGVYTITVTNPVGEDHASLF 83

                    ...
gi 1958765569 19205 VKV 19207
Cdd:cd05894      84 VKV 86
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
31768-31970 5.64e-08

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 59.98  E-value: 5.64e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31768 DLGRGEFGIVHRCVETSSK--KTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESME-ELVMIFEFISGLDI 31844
Cdd:cd05116       2 ELGSGNFGTVKKGYYQMKKvvKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEaESWMLVMEMAELGP 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31845 FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiiKIIEFGQARQLKPGDNFRLLFTA-- 31922
Cdd:cd05116      82 LNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYA--KISDFGLSKALRADENYYKAQTHgk 159
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31923 -P-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQ---QMIEN 31970
Cdd:cd05116     160 wPvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNevtQMIEK 213
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
13067-13148 5.70e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 55.48  E-value: 5.70e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13067 ISKPQNLEILEGEKAEFVCTISKESF-EVQWKRDDQTLESGdKYDIIADgkkRVLVVKDATLQDMGTYVV----MVGAAR 13141
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVpTVRWRKEDGELPKG-RYEILDD---HSLKIRKVTAGDMGSYTCvaenMVGKIE 76

                    ....*..
gi 1958765569 13142 AAAHLTV 13148
Cdd:cd05725      77 ASATLTV 83
fn3 pfam00041
Fibronectin type III domain;
22068-22152 5.71e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 5.71e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22068 GPPEGpLAVSDVTSEKCVLSWLPPlDDGGAKIDHYIVQKRETSRLAWTNVATEVQVTK-LKVTKLLKGNEYIFRVMAVNK 22146
Cdd:pfam00041     1 SAPSN-LTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 22147 YGVGEP 22152
Cdd:pfam00041    79 GGEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9307-9374 5.73e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 55.03  E-value: 5.73e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9307 ATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGEIES 9374
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNG-KPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
31762-31949 5.76e-08

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 60.13  E-value: 5.76e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSK-KTFMAKFVKV---KGTDQVLVKKEISILN---IARHRNILYLHESFESMEELVM 31834
Cdd:cd14052       1 RFANVELIGSGEFSQVYKVSERVPTgKVYAVKKLKPnyaGAKDRLRRLEEVSILReltLDGHDNIVQLIDSWEYHGHLYI 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFIS--GLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLkP 31912
Cdd:cd14052      81 QTELCEngSLDVFLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT--LKIGDFGMATVW-P 157
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958765569 31913 GDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLV 31949
Cdd:cd14052     158 LIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLIL 194
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6076-6162 5.78e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 55.66  E-value: 5.78e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6076 TKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHEN-TVSLEVSNLELEDTANYTCKVSNVAGDN 6154
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  6155 ACSGILTV 6162
Cdd:cd20973      81 TCSAELTV 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5511-5600 5.82e-08

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 55.65  E-value: 5.82e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGsHPI-SIQWFKDDQEISASDKYKfSFHDNTafLEISQLEG-TDSGTYTCSATNK 5588
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAG-YPIsSITWEKDGRRLPLNHRQR-VFPNGT--LVIENVQRsSDEGEYTCTARNQ 76
                            90
                    ....*....|...
gi 1958765569  5589 AGHS-QCSGHLTV 5600
Cdd:cd20958      77 QGQSaSRSVFVKV 89
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9085-9176 5.82e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.89  E-value: 5.82e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKL-SETIEEteGNSFKLEGRVAGSQPITIAWYKNNVEIHPTS---NCEITFKNNALLLQVKKASMADAGLYTCKA 9160
Cdd:cd20951       1 PEFIIRLqSHTVWE--KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVA 78
                            90
                    ....*....|....*.
gi 1958765569  9161 TNDAGSALCTSSIVIR 9176
Cdd:cd20951      79 KNIHGEASSSASVVVE 94
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
19417-19500 5.91e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 55.62  E-value: 5.91e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19417 PEQITIKAGKKLRVEAHVYGKPNPICKWKKGeDDVVTSSHLAIH---KADSSSvLIIKDVTRKDSGYYSLTAENSSGTDT 19493
Cdd:cd05894       2 ENTIVVVAGNKLRLDVPISGEPAPTVTWSRG-DKAFTATEGRVRvesYKDLSS-FVIEGAEREDEGVYTITVTNPVGEDH 79

                    ....*..
gi 1958765569 19494 QKIKVTV 19500
Cdd:cd05894      80 ASLFVKV 86
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
103-193 5.94e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 55.64  E-value: 5.94e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   103 PPNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQ----EGDLYSLL-IAEAYPEDSGTYSVN 177
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDyvtsDGDVVSYVnISSVRVEDGGEYTCT 80
                            90
                    ....*....|....*.
gi 1958765569   178 ATNSVGRATSTADLLV 193
Cdd:cd20956      81 ATNDVGSVSHSARINV 96
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4588-4663 5.97e-08

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 55.29  E-value: 5.97e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVI 4663
Cdd:cd05748       7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
6551-6629 6.00e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 55.54  E-value: 6.00e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6551 VTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKhkfSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVVDV 6629
Cdd:cd04969      14 AAKGGDVIIECKPKASPKPTISWSKGTELLTNSSR---ICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
25227-25310 6.03e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 55.62  E-value: 6.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25227 DVIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPI 25306
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 25307 TVKV 25310
Cdd:cd05894      83 FVKV 86
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5791-5878 6.07e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.58  E-value: 6.07e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5791 PIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTM----SEKMSVFYLHITKcapSDVGEYQCIIA 5866
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMlvreNGRHSLIIEPVTK---RDAGIYTCIAR 77
                            90
                    ....*....|..
gi 1958765569  5867 NEGGSCACTARV 5878
Cdd:cd05744      78 NRAGENSFNAEL 89
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
1679-1754 6.24e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 55.66  E-value: 6.24e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  1679 PAHFECRLTpiGDPTMVVEWLHDGKPLEAANRLRLI-NEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:cd20973      14 AARFDCKVE--GYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
5982-6066 6.30e-08

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 55.49  E-value: 6.30e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5982 KAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVP-SRYFSMSFE-NNVASFRIQSVMKQDSGQYTFKVENDFGSSS 6059
Cdd:cd05893       6 KLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPkSDHYTIQRDlDGTCSLHTTASTLDDDGNYTIMAANPQGRIS 85

                    ....*..
gi 1958765569  6060 CDAYLRV 6066
Cdd:cd05893      86 CTGRLMV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4760-4849 6.31e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.58  E-value: 6.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4760 PTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSF-SSGVAVLTISDVQIGLGGKYTCLAENEA 4838
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVrENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  4839 GSQTSVGELIV 4849
Cdd:cd05744      81 GENSFNAELVV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3025-3102 6.33e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 55.20  E-value: 6.33e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3025 KDIKVLEKKRAMFECEVS-EPDITVQWMKDGQE-LQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVAGGNM----STA 3098
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSgsasSGT 81

                     ....
gi 1958765569   3099 NLFV 3102
Cdd:smart00410    82 TLTV 85
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
33078-33162 6.51e-08

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 55.70  E-value: 6.51e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33078 KPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSAR----HQVTTakyKSTFEISSVQASDEGNYSVVVENTDGK 33153
Cdd:cd05763       5 TPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARerrmHVMPE---DDVFFIVDVKIEDTGVYSCTAQNSAGS 81

                    ....*....
gi 1958765569 33154 QEAQFTLTV 33162
Cdd:cd05763      82 ISANATLTV 90
I-set pfam07679
Immunoglobulin I-set domain;
17045-17124 6.57e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 55.34  E-value: 6.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17045 RIVVHAGGVIRIIAYVSGKPPPTVTWNMNERALPQEATIETTAI--SSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIV 17122
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEggTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                    ..
gi 1958765569 17123 DV 17124
Cdd:pfam07679    89 TV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
15624-15705 6.59e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 55.20  E-value: 6.59e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15624 GGIQIMAGKTLRIPAVVTGRPVPTKVWTIEEGEL--DKERVVIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAAA 15701
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  15702 RVEV 15705
Cdd:smart00410    82 TLTV 85
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
7585-7666 6.60e-08

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 55.20  E-value: 6.60e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7585 DTTATLGASVVLECRVSGSAPISVGWFLDGNEIisSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQDESSALL 7664
Cdd:cd20952       8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPL--LGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVL 85

                    ..
gi 1958765569  7665 TV 7666
Cdd:cd20952      86 DV 87
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7480-7570 6.64e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 55.33  E-value: 6.64e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7480 PARIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSrHHITFVRNLASLKIPSAEMNDKGLYSFEVENSV 7559
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAA-DRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  7560 GKSSCTVSVHV 7570
Cdd:cd20976      80 GQVSCSAWVTV 90
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
5704-5787 6.64e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 55.09  E-value: 6.64e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5704 SPVLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRygisfvdglatFQISNARVENSGTYVCEARNDAG-TASCS 5782
Cdd:pfam13895     6 PSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN-----------FFTLSVSAEDSGTYTCVARNGRGgKVSNP 74

                    ....*
gi 1958765569  5783 IELKV 5787
Cdd:pfam13895    75 VELTV 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
33891-33984 6.71e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 55.33  E-value: 6.71e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIqsQEQQGRFHIENTddLTTLIIMDVQKQDGGLYTLSLG 33970
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL--QYAADRSTCEAG--VGELHIQDVLPEDHGTYTCLAK 76
                            90
                    ....*....|....
gi 1958765569 33971 NEFGSDSATVNINI 33984
Cdd:cd20976      77 NAAGQVSCSAWVTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3305-3394 6.74e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.50  E-value: 6.74e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3305 PAIVTPLQDAVTSEGRPARFQCQVSGT-DLKVSWYCRDKKIKPSRFFRMTQFEDTY---QLEIAEAFPEDEGTYAFVANN 3380
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIDPSSIPGKYKIESEYgvhVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  3381 AVGQVSSTATLRLE 3394
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5980-6066 7.16e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.58  E-value: 7.16e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5980 IEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVP-SRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSS 6058
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGEN 83

                    ....*...
gi 1958765569  6059 SCDAYLRV 6066
Cdd:cd05744      84 SFNAELVV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5346-5401 7.17e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 54.64  E-value: 7.17e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5346 KGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAG 5401
Cdd:cd00096       8 SGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5884-5963 7.21e-08

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 55.27  E-value: 7.21e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNvHISFEDsvATLQVRSVDNGH-SGRYTCQAKNES 5962
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR-QRVFPN--GTLVIENVQRSSdEGEYTCTARNQQ 77

                    .
gi 1958765569  5963 G 5963
Cdd:cd20958      78 G 78
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
33417-33505 7.21e-08

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 55.20  E-value: 7.21e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33417 VIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIA-QSSKYKLSNDKEefiLEILKTETSDGGLYSCTVANSAG 33495
Cdd:cd20952       1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLgKDERITTLENGS---LQIKGAEKSDTGEYTCVALNLSG 77
                            90
                    ....*....|
gi 1958765569 33496 SVSSSCKLTI 33505
Cdd:cd20952      78 EATWSAVLDV 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6352-6435 7.22e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 55.28  E-value: 7.22e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6352 PPVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEV 6431
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....
gi 1958765569  6432 GSDT 6435
Cdd:cd20972      81 GSDT 84
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
31769-32018 7.22e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 60.85  E-value: 7.22e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKF-----VKVKGTDQVLVKKEI--SILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd05633      13 IGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGETLALNERImlSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiiKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd05633      93 GDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV--RISDLGLACDFSKKKPHASVGT 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 ApEYYAPEVHQHDVV-SSATDMWSLGTLVYVLLSGINPFLAETNQQMIEnIMNAEYTFDEEAFQEISLEAMDFIDRLLVK 32000
Cdd:cd05633     170 H-GYMAPEVLQKGTAyDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-IDRMTLTVNVELPDSFSPELKSLLEGLLQR 247
                           250       260
                    ....*....|....*....|...
gi 1958765569 32001 ERKSRM-----TASEALKHPWLK 32018
Cdd:cd05633     248 DVSKRLgchgrGAQEVKEHSFFK 270
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
33435-33505 7.32e-08

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 55.28  E-value: 7.32e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 33435 FVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEefiLEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd05723      17 FECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
19825-19893 7.46e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 54.64  E-value: 7.46e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 19825 VCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATI 19893
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8141-8218 7.50e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.50  E-value: 7.50e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8141 PRFIKKLdQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESS---KFRMSFEDSVAILEMHNLSVEDSGDYTCEAR 8217
Cdd:cd20951       1 PEFIIRL-QSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAK 79

                    .
gi 1958765569  8218 N 8218
Cdd:cd20951      80 N 80
fn3 pfam00041
Fibronectin type III domain;
29659-29737 7.66e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 7.66e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29659 LTVSRVTEEKCTLAWSLPqEDGGAEITHYIVERRET---SRLNWVIVEAEclTLSYVVTRLIKNNEYTFRVRAVNKYGLG 29735
Cdd:pfam00041     6 LTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnsgEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    ..
gi 1958765569 29736 VP 29737
Cdd:pfam00041    83 PP 84
I-set pfam07679
Immunoglobulin I-set domain;
21296-21369 7.68e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 55.34  E-value: 7.68e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 21296 RTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLK--HRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKS 21369
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAE 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
121-188 7.76e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 54.64  E-value: 7.76e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   121 ARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATST 188
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
21575-21657 7.81e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 55.16  E-value: 7.81e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21575 PELDLRGIYQKLVIARAGDnIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINecvRSDSGAYPLTAKN 21654
Cdd:cd04969       1 PDFELNPVKKKILAAKGGD-VIIECKPKASPKPTISWSKGTELLTNSSRICILPDGSLKIKNVT---KSDEGKYTCFAVN 76

                    ...
gi 1958765569 21655 TVG 21657
Cdd:cd04969      77 FFG 79
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
31767-32023 7.86e-08

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 59.86  E-value: 7.86e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL--VKKEISILNIARHRNILYLHESFESMEELVMIFEFISG--L 31842
Cdd:cd06622       7 DELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFnqIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAgsL 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31843 DIFERINTSAFELNEREVVSYVRQVCEALEFLHSQ-NIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKPGDNfRLLFT 31921
Cdd:cd06622      87 DKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNG--NGQVKLCDFGVSGNLVASLA-KTNIG 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APEYYAPE------VHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEAMDFID 31995
Cdd:cd06622     164 CQSYMAPEriksggPNQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLSAIVDGDPPTLPSGYSDDAQDFVA 243
                           250       260       270
                    ....*....|....*....|....*....|
gi 1958765569 31996 RLLVKERKSRMTASEALKHPWLK--QRMDR 32023
Cdd:cd06622     244 KCLNKIPNRRPTYAQLLEHPWLVkyKNADV 273
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
25217-25310 7.89e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 55.21  E-value: 7.89e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25217 PNASLDPKYRDVIiVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKStlQKTTLTVKDCIRTDGGQYTLKLS 25296
Cdd:cd20970       1 PVISTPQPSFTVT-AREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRE--NGTTLTIRNIRRSDMGIYLCIAS 77
                            90
                    ....*....|....*
gi 1958765569 25297 N-VGGTKTIPITVKV 25310
Cdd:cd20970      78 NgVPGSVEKRITLQV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
9586-9653 7.92e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.88  E-value: 7.92e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9586 HLQDVTLKEGQTCTMTCQ-FSVPNVKSEWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTCK 9653
Cdd:pfam13927     7 SPSSVTVREGETVTLTCEaTGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8050-8127 7.95e-08

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 55.41  E-value: 7.95e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8050 FDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAG 8127
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS 79
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
7121-7198 8.04e-08

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 55.35  E-value: 8.04e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7121 GESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSVKE 7198
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7210-7290 8.05e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 55.27  E-value: 8.05e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7210 KVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSF-VNSVALLTINEASVEDTGDYICEAHNGVGHASCSTAL 7288
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569  7289 KV 7290
Cdd:cd20973      87 TV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
20888-20968 8.08e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.88  E-value: 8.08e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20888 PTIVLDPTikdGLTVKAGDSIVLSaISILGKPLPKSSWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITAT 20967
Cdd:pfam13927     2 PVITVSPS---SVTVREGETVTLT-CEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 20968 N 20968
Cdd:pfam13927    78 N 78
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8-97 8.27e-08

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 55.20  E-value: 8.27e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     8 FTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDgqviststlpGVQISFSDGRAR------LMIPAVTKANSGRYSLR 81
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKD----------GVPLLGKDERITtlengsLQIKGAEKSDTGEYTCV 71
                            90
                    ....*....|....*.
gi 1958765569    82 ATNGSGQATSTAELLV 97
Cdd:cd20952      72 ALNLSGEATWSAVLDV 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7859-7945 8.29e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 55.27  E-value: 8.29e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7859 IEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKM-QFKNNVASLVINKVDHSDVGEYTCKAENSVGAV 7937
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  7938 ASSAVLVI 7945
Cdd:cd20973      81 TCSAELTV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
28080-28152 8.32e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.88  E-value: 8.32e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 28080 IPGAQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDN 28152
Cdd:pfam13927     6 VSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
6917-7003 8.35e-08

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 55.03  E-value: 8.35e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6917 FVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTa 6996
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI- 80

                    ....*..
gi 1958765569  6997 ASKTVFR 7003
Cdd:cd20949      81 ASDMQER 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
30257-30340 8.41e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 8.41e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30257 QKTIHVPAGRPIELVIPITGRPPPTASWFF-AGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSET 30335
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  30336 IKVVI 30340
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12715-12792 8.41e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 8.41e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12715 KDVTVTAGETATFDCELSYEDIP-VEWYL-KGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAG----EVQLTAKDFKTQA 12788
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPeVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGtytcAATNSSGSASSGT 81

                     ....
gi 1958765569  12789 NLFV 12792
Cdd:smart00410    82 TLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
3577-3654 8.49e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.88  E-value: 8.49e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIIHNpDGSGTFIVNDPQRGDSGLYICKAEN 3654
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLS-GSNSTLTISNVTRSDAGTYTCVASN 78
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
21981-22063 8.57e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 54.85  E-value: 8.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21981 DTITLKAGEAFKLEADVSGRPPPTMEWAKDGKEL-EGTGKLEI-KIADFSTHLInKDSSRTDSGAYILTATNPGGFAKHI 22058
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFtATEGRVRVeSYKDLSSFVI-EGAEREDEGVYTITVTNPVGEDHAS 81

                    ....*
gi 1958765569 22059 FNVKV 22063
Cdd:cd05894      82 LFVKV 86
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
14899-14988 8.57e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 55.44  E-value: 8.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14899 PTIDLETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASD--RLTMKNDHISAHLEVPKSVHADAGVYTITLENK 14976
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569 14977 LGSATASINVKV 14988
Cdd:cd20974      81 SGQATSTAELLV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28877-28957 8.57e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 8.57e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  28877 QTHIVRAGASIRLFIAYQGRPTPTAVWSKPDSNLSI---RADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITF 28953
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  28954 TVKV 28957
Cdd:smart00410    82 TLTV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
6259-6349 8.62e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 55.09  E-value: 8.62e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEASKIVKAGDSARLECKITGSPEIRVVWYRNEHELTAsDKYQMTFIDSVAVmqMNSLGTEDSGDFICEAQNPA 6338
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG-PMERATVEDGTLT--IINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  6339 GSTSCSTKVIV 6349
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6926-7004 8.76e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 54.71  E-value: 8.76e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6926 ASVGDSVSLQCQVAGTPEITVSWFKGDTKLrstPEYRTYFTNNvATLVFNKVGINDSGEYTCVAENSIGTAASKTVFRI 7004
Cdd:cd05725       9 VLVDDSAEFQCEVGGDPVPTVRWRKEDGEL---PKGRYEILDD-HSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
29965-30033 8.82e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.88  E-value: 8.82e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 29965 KKTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTES--YSLLIVDKVNRYDAGKYTIEAEN 30033
Cdd:pfam13927     8 PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSgsNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5976-6066 8.90e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 54.95  E-value: 8.90e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5976 PAQIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQI-VPSRYFSMsfENNVASFRIQSVMKQDSGQYTFKVEND 6054
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTC--EAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  6055 FGSSSCDAYLRV 6066
Cdd:cd20976      79 AGQVSCSAWVTV 90
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
5891-5969 8.96e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 55.21  E-value: 8.96e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5891 ENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSvATLQVRSVDNGHSGRYTCQAKNESG--VERCY 5968
Cdd:cd20970      10 FTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENG-TTLTIRNIRRSDMGIYLCIASNGVPgsVEKRI 88

                    .
gi 1958765569  5969 A 5969
Cdd:cd20970      89 T 89
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
6073-6153 8.96e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 55.09  E-value: 8.96e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTK-MDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVcHENTvsLEVSNLELEDTANYTCKVSNVA 6151
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATV-EDGT--LTIINVQPEDTGYYGCVATNEI 77

                    ..
gi 1958765569  6152 GD 6153
Cdd:cd20978      78 GD 79
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
9292-9380 9.03e-08

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 54.81  E-value: 9.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRILIHQKGdesKLEIRDTTKTDSGLYRCVAFNKHGE 9371
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENG---SLQIKGAEKSDTGEYTCVALNLSGE 78

                    ....*....
gi 1958765569  9372 IESNVNLQV 9380
Cdd:cd20952      79 ATWSAVLDV 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
30656-30736 9.08e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 55.05  E-value: 9.08e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30656 EGVFVRQGGVIRLTIPIKGKPFPICKWTKEGQDVS----KRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVY 30731
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIStstlPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*
gi 1958765569 30732 IKVKV 30736
Cdd:cd20974      88 AELLV 92
fn3 pfam00041
Fibronectin type III domain;
20593-20672 9.13e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 9.13e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20593 GPIKFDEVTAEAMTLKWGPPkDDGGSEITNYVLEKRDSVNNK-WVTCASAVQKTTFRVTRLHEGIEYTFRVSAENKYGVG 20671
Cdd:pfam00041     4 SNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                    .
gi 1958765569 20672 E 20672
Cdd:pfam00041    83 P 83
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
9003-9086 9.27e-08

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 55.35  E-value: 9.27e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9003 GESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLNIKERL 9082
Cdd:cd05762      16 GESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVDKP 95

                    ....
gi 1958765569  9083 TPPS 9086
Cdd:cd05762      96 DPPA 99
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2936-3013 9.55e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 9.55e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2936 KDINAEEKDTITFEVTVN-YEGISYKWLKNGVE-IKSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVA----GKATSTA 3009
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSGT 81

                     ....
gi 1958765569   3010 TLYV 3013
Cdd:smart00410    82 TLTV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
1417-1507 9.62e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 54.95  E-value: 9.62e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVikEDGTQSLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:cd20976       2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTC--EAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8530-8607 9.75e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 54.71  E-value: 9.75e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8530 LSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQttLTDNTcaLTVNMLEDADAGDYTCIATNVAGSDECSAPLTV 8607
Cdd:cd05725      10 LVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEI--LDDHS--LKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7952-8040 9.76e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.12  E-value: 9.76e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLL---KDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASN 8028
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|..
gi 1958765569  8029 PLGTASSSAKLI 8040
Cdd:cd20951      81 IHGEASSSASVV 92
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
32201-32293 1.00e-07

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 55.17  E-value: 1.00e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPgdDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRP--DQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVN 78
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:cd20975      79 EYGARQCEARLEV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12359-12433 1.01e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.82  E-value: 1.01e-07
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  12359 SDVKVFEKDEAKFECEVSREPK-TFRWLK-GTQEIAGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAEDKRTSGK 12433
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPpEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
31806-32017 1.02e-07

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 59.70  E-value: 1.02e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31806 KEISILNIARHRNILYLHESFESMEELVMIFEFISGlDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIR 31885
Cdd:cd07844      47 REASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLDT-DLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLK 125
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31886 PENIIYQTRKNsiIKIIEFGQARQ----------------LKPGDnfrLLFTAPEYyapevhqhdvvSSATDMWSLGTLV 31949
Cdd:cd07844     126 PQNLLISERGE--LKLADFGLARAksvpsktysnevvtlwYRPPD---VLLGSTEY-----------STSLDMWGVGCIF 189
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31950 YVLLSGINPFLAETN-QQMIENI--------------MNAEYTFDEEAFQ--------------EISLEAMDFIDRLLVK 32000
Cdd:cd07844     190 YEMATGRPLFPGSTDvEDQLHKIfrvlgtpteetwpgVSSNPEFKPYSFPfypprplinhaprlDRIPHGEELALKFLQY 269
                           250
                    ....*....|....*..
gi 1958765569 32001 ERKSRMTASEALKHPWL 32017
Cdd:cd07844     270 EPKKRISAAEAMKHPYF 286
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8989-9078 1.03e-07

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 55.16  E-value: 1.03e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLT--IVKVDKGDSGQYTCYAINE 9066
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICllIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  9067 VGKDSCTAQLNI 9078
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
32200-32293 1.03e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 54.95  E-value: 1.03e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32200 PPEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDdkkyTFESDKGLYQLTINSVTTDDDAEYAVVAR 32279
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD----RSTCEAGVGELHIQDVLPEDHGTYTCLAK 76
                            90
                    ....*....|....
gi 1958765569 32280 NKHGEDSCKAKLTV 32293
Cdd:cd20976      77 NAAGQVSCSAWVTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
19420-19687 1.04e-07

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 61.50  E-value: 1.04e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19420 ITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSshlaihkadsssVLIIKDVTRKDSGYYSLTA-----ENSSGTDTQ 19494
Cdd:COG4733     455 VQSVAGRTLTVSTAYSETPEAGAVWAFGPDELETQ------------LFRVVSIEENEDGTYTITAvqhapEKYAAIDAG 522
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19495 KIkvtvmDAPGPPQPPFDIS-----EIDADACS-----LSWhipleDGGSNITNYIVEkcdVSR--GDWVTAlASVTKTS 19562
Cdd:COG4733     523 AF-----DDVPPQWPPVNVTtseslSVVAQGTAvttltVSW-----DAPAGAVAYEVE---WRRddGNWVSV-PRTSGTS 588
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19563 CRVGKLIPGQeYIFRVRAENRFGI-SEPLTSPKMLAKFPFDVPSEPKNARVTKVNKDCIFVaWDRPDsdgGSPITGYLIE 19641
Cdd:COG4733     589 FEVPGIYAGD-YEVRVRAINALGVsSAWAASSETTVTGKTAPPPAPTGLTATGGLGGITLS-WSFPV---DADTLRTEIR 663
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569 19642 RKERNSLLWVKANDTIVRSTEYPCAGLVEGLEYSFRIYALNKAGSS 19687
Cdd:COG4733     664 YSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNV 709
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
910-991 1.05e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 54.32  E-value: 1.05e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   910 TVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITfqsgiarlmirEAFAEDSGRFTCSAVNEAGTVsTSCYLAV 989
Cdd:pfam13895    10 VVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTL-----------SVSAEDSGTYTCVARNGRGGK-VSNPVEL 77

                    ..
gi 1958765569   990 QV 991
Cdd:pfam13895    78 TV 79
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8239-8323 1.08e-07

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 54.71  E-value: 1.08e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8239 KKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKkYKIMSENlltSIHILNVDTADIGEYQCKATNDVGSDTC 8318
Cdd:cd05725       2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGR-YEILDDH---SLKIRKVTAGDMGSYTCVAENMVGKIEA 77

                    ....*
gi 1958765569  8319 VGSVT 8323
Cdd:cd05725      78 SATLT 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5229-5316 1.08e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 54.90  E-value: 1.08e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEVG 5308
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81

                    ....*...
gi 1958765569  5309 SSTCSARV 5316
Cdd:cd20972      82 SDTTSAEI 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3219-3283 1.08e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 54.26  E-value: 1.08e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  3219 CAViAGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTS 3283
Cdd:cd00096       5 CSA-SGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
5144-5228 1.09e-07

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 54.96  E-value: 1.09e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5144 SQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTSIV 5223
Cdd:cd05736       9 FQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSL 88

                    ....*
gi 1958765569  5224 IVKES 5228
Cdd:cd05736      89 FVEDS 93
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
31440-31531 1.09e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 55.10  E-value: 1.09e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEFKGGYHQLIIASVTDDDATVYQVRATNQ 31519
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569 31520 GGSVSGTASLEV 31531
Cdd:cd05893      81 QGRISCTGRLMV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
22685-22744 1.09e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 54.26  E-value: 1.09e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22685 GRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATET 22744
Cdd:cd00096       9 GNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
12530-12601 1.09e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.49  E-value: 1.09e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12530 PYFTGKLQDYTGVEKDEVVLQCEISKADAP-VKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC 12601
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPtITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTC 74
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15048-15233 1.10e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 61.17  E-value: 1.10e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15048 LSWTVKDLIPNGEYFFRVKAVNKIGGGEYielKNPVIAQDPKQPPDPPVDVEVHNPTAKAMTITWKPPLYDGgskIMGYI 15127
Cdd:COG3401     192 LVDGGGDIEPGTTYYYRVAATDTGGESAP---SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYR 265
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15128 IEKLAKGEDRWKRCNEhlVPVLTYTAKGLEEGKEYQFRVRAENAAgiGEPSRATPPTKAVDPIDAPKVILrtslevkrgd 15207
Cdd:COG3401     266 VYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAA--GNESAPSNVVSVTTDLTPPAAPS---------- 331
                           170       180
                    ....*....|....*....|....*.
gi 1958765569 15208 eiALDATISGSPYPTITWIKDENVIV 15233
Cdd:COG3401     332 --GLTATAVGSSSITLSWTASSDADV 355
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12808-12881 1.10e-07

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 54.56  E-value: 1.10e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 12808 VEEEATAVLECEVSRENAKVKWFKNGTEILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAKDFKTSCNLNV 12881
Cdd:cd20967       9 VSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
4953-5033 1.11e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 54.51  E-value: 1.11e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4953 KPLRNVDSVVGGACRLDCKIAGSLPM-RVSWFKDGKEIAASDRYQIAFV-EGTASLEISRVDMNDAGNFTCRATNSVGSK 5030
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSASTGSPGpDVTWSKEGGTLIESLKVKHDNGrTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                    ...
gi 1958765569  5031 DSR 5033
Cdd:pfam00047    81 TLS 83
I-set pfam07679
Immunoglobulin I-set domain;
13512-13598 1.12e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.96  E-value: 1.12e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13512 PKIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTK---TVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHG 13588
Cdd:pfam07679     1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSdrfKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                            90
                    ....*....|
gi 1958765569 13589 KAEGFINLQV 13598
Cdd:pfam07679    81 EAEASAELTV 90
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8799-8886 1.13e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 54.64  E-value: 1.13e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8799 FVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGEV 8878
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIA 81

                    ....*...
gi 1958765569  8879 SSSTFLTV 8886
Cdd:cd20949      82 SDMQERTV 89
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
5699-5787 1.13e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 54.93  E-value: 1.13e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5699 FIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDG-NEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDAG 5777
Cdd:cd05763       2 FTKTPHDITI-RAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAG 80
                            90
                    ....*....|
gi 1958765569  5778 TASCSIELKV 5787
Cdd:cd05763      81 SISANATLTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12992-13047 1.14e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 54.26  E-value: 1.14e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 12992 IKLVCEVS-KPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCR 13047
Cdd:cd00096       1 VTLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCV 57
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
8893-8982 1.15e-07

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 54.77  E-value: 1.15e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQ--LRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVqtSFLDNiATLNIFKTDRSLAGQYSCTVTNP 8970
Cdd:cd04969       1 PDFELNpvKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRI--CILPD-GSLKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569  8971 IGSASSSAKLIL 8982
Cdd:cd04969      78 FGKANSTGSLSV 89
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
4296-4381 1.17e-07

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 55.00  E-value: 1.17e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4296 RRIEPLEVALGHLAKFTCEIQGA-PNVRFQWFKAGREIYESDK---CSIRSSNYISSLEILRTQVVDCGEYTCKASNEYG 4371
Cdd:cd05895       4 KEMKSQEVAAGSKLVLRCETSSEyPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSSKLG 83
                            90
                    ....*....|
gi 1958765569  4372 SVSCTATLTV 4381
Cdd:cd05895      84 NDSASANVTI 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5884-5974 1.17e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 54.73  E-value: 1.17e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQ-----------ILEENDNVHisfedsvaTLQVRSVDNGHSG 5952
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVpidpssipgkyKIESEYGVH--------VLHIRRVTVEDSA 72
                            90       100
                    ....*....|....*....|..
gi 1958765569  5953 RYTCQAKNESGVERCYAFLLVQ 5974
Cdd:cd20951      73 VYSAVAKNIHGEASSSASVVVE 94
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
32203-32293 1.19e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 54.64  E-value: 1.19e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32203 FTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPG-DDDKKYTFESDKglyqLTINSVTTDDDAEYAVVARNK 32281
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASvADMSKYRILADG----LLINKVTQDDTGEYTCRAYQV 77
                            90
                    ....*....|..
gi 1958765569 32282 HGEDSCKAKLTV 32293
Cdd:cd20949      78 NSIASDMQERTV 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
24135-24214 1.19e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.49  E-value: 1.19e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24135 PRISMDPKfrdTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASN 24214
Cdd:pfam13927     2 PVITVSPS---SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8327-8405 1.19e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.49  E-value: 1.19e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8327 PPQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDkGEIVRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKN 8405
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKN-GEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
25625-25707 1.20e-07

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 54.90  E-value: 1.20e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25625 LRKVVTLRASATLRLFVTIKGRPEPEVKWEKAEG--ILTERAQIEV-TSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTA 25701
Cdd:cd05737       7 LPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQalAFLDHCNLKVeAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETS 86

                    ....*.
gi 1958765569 25702 FVNVRV 25707
Cdd:cd05737      87 DVTVSV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8532-8606 1.21e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 54.67  E-value: 1.21e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  8532 GSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAGSDECSAPLT 8606
Cdd:cd05747      18 GESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTLT 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8047-8137 1.21e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 54.90  E-value: 1.21e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8047 PPFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVA 8126
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8127 GKDSCSAQLGV 8137
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
32306-32396 1.22e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.67  E-value: 1.22e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLG--PHIEIvheglDYYALHIRDTLPE----DTGYYRV 32379
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTStlPGVQI-----SFSDGRAKLSIPAvtkaNSGRYSL 75
                            90
                    ....*....|....*..
gi 1958765569 32380 TATNTAGSTSCQAHLQV 32396
Cdd:cd20974      76 TATNGSGQATSTAELLV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2849-2927 1.22e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 1.22e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2849 RNIEVPETKAASFECEVSHFNVPSM-WLKNGVE-IEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVCGND--QVSATL 2924
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVtWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSsgSASSGT 81

                     ...
gi 1958765569   2925 TVT 2927
Cdd:smart00410    82 TLT 84
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
6916-6998 1.22e-07

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 54.77  E-value: 1.22e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6916 YFVTELEPleASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPeyRTYFTNNvATLVFNKVGINDSGEYTCVAENSIGT 6995
Cdd:cd04969       6 NPVKKKIL--AAKGGDVIIECKPKASPKPTISWSKGTELLTNSS--RICILPD-GSLKIKNVTKSDEGKYTCFAVNFFGK 80

                    ...
gi 1958765569  6996 AAS 6998
Cdd:cd04969      81 ANS 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
33898-33984 1.24e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 54.81  E-value: 1.24e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENtdDLTTLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:cd05744       7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVREN--GRHSLIIEPVTKRDAGIYTCIARNRAGENS 84

                    ....*..
gi 1958765569 33978 ATVNINI 33984
Cdd:cd05744      85 FNAELVV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
33076-33162 1.24e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 54.81  E-value: 1.24e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33076 LTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKS-TFEISSVQASDEGNYSVVVENTDGKQ 33154
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRhSLIIEPVTKRDAGIYTCIARNRAGEN 83

                    ....*...
gi 1958765569 33155 EAQFTLTV 33162
Cdd:cd05744      84 SFNAELVV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6183-6251 1.24e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.87  E-value: 1.24e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6183 VEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTNDV-GSDSCTT 6251
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6829-6910 1.24e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 1.24e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   6829 SDHSVEPGKSIILEGTYTGTLPISVTWKKDG-VVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAGRDSCDA 6907
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569   6908 LVS 6910
Cdd:smart00410    82 TLT 84
fn3 pfam00041
Fibronectin type III domain;
27479-27563 1.25e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 1.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27479 GPPGGPiEFKTVTAEKITLLWRPPaDDGGAKITHYIVEKRET---SRVVWSMVAENLEECIITttKIIKGNEYIFRVRAV 27555
Cdd:pfam00041     1 SAPSNL-TVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKnsgEPWNEITVPGTTTSVTLT--GLKPGTEYEVRVQAV 76

                    ....*...
gi 1958765569 27556 NKYGIGEP 27563
Cdd:pfam00041    77 NGGGEGPP 84
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
3486-3550 1.25e-07

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 54.77  E-value: 1.25e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  3486 GCPKPKIQWFFNGMLLTPSADYKFVFDGnnhSLIILFTRFQDEGEYTCMASNEYGRAVCSAHLKV 3550
Cdd:cd04969      28 ASPKPTISWSKGTELLTNSSRICILPDG---SLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4480-4569 1.26e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 54.90  E-value: 1.26e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAG 4559
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81
                            90
                    ....*....|
gi 1958765569  4560 SSSSSATVAV 4569
Cdd:cd20972      82 SDTTSAEIFV 91
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
7118-7196 1.27e-07

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 54.56  E-value: 1.27e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7118 VIAGESADFECHVTGAQPmRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCqatnDVGKDMCSAQLSV 7196
Cdd:cd20967       9 VSKGHKIRLTVELADPDA-EVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC----VAGGEKCSFELFV 82
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
29560-29650 1.28e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.67  E-value: 1.28e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29560 LDARLQGdlVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCE--KVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNA 29637
Cdd:cd20974       3 FTQPLQS--VVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 29638 SGTKSVSVMVKVL 29650
Cdd:cd20974      81 SGQATSTAELLVL 93
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
31769-31984 1.28e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 58.81  E-value: 1.28e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRcveTSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLD-IFER 31847
Cdd:cd14068       2 LGDGGFGSVYR---AVYRGEDVAVKIFNKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRMLVMELAPKGSLDaLLQQ 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31848 INTSafeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNS---IIKIIEFGQArQLKPGDNFRLLFTAPE 31924
Cdd:cd14068      79 DNAS---LTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNcaiIAKIADYGIA-QYCCRMGIKTSEGTPG 154
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31925 YYAPEVHQHDVV-SSATDMWSLGTLVYVLLSGinpflaetNQQMIENiMNAEYTFDEEAFQ 31984
Cdd:cd14068     155 FRAPEVARGNVIyNQQADVYSFGLLLYDILTC--------GERIVEG-LKFPNEFDELAIQ 206
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
11-95 1.29e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 54.46  E-value: 1.29e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    11 PLQSVVVleGSAATFEAHISGSPVPEVSWFRDGQVISTSTLpgVQISFSDgraRLMIPAVTKANSGRYSLRATNGSGQAT 90
Cdd:cd20957       9 PVQTVDF--GRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSR--VQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQ 81

                    ....*
gi 1958765569    91 STAEL 95
Cdd:cd20957      82 ATAEL 86
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
4953-5038 1.29e-07

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 54.82  E-value: 1.29e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4953 KPLRNVDSVVGGACRLDCKIAGSLP-MRVSWFKDGKEIAA--SDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGS 5029
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEATSENPsPRYRWFKDGKELNRkrPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGK 83

                    ....*....
gi 1958765569  5030 KDSRGALIV 5038
Cdd:cd05750      84 DTVTGNVTV 92
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
31762-32017 1.31e-07

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 59.21  E-value: 1.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVL---VKKEISILNIAR---HRNILYLHESFESME----- 31830
Cdd:cd07863       1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLplsTVREVALLKRLEafdHPNIVRLMDVCATSRtdret 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 ELVMIFEFISGlDI---FERINTSAFELNEreVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQA 31907
Cdd:cd07863      81 KVTLVFEHVDQ-DLrtyLDKVPPPGLPAET--IKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQ--VKLADFGLA 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31908 RQLKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMN-----------AEY 31976
Cdd:cd07863     156 RIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDliglppeddwpRDV 235
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31977 TFDEEAFQ------------EISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07863     236 TLPRGAFSprgprpvqsvvpEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
7482-7571 1.31e-07

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 54.87  E-value: 1.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7482 RIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGREL-----SSGSRHHITFVRNLASLKIPSAEMN--DKGLYSFE 7554
Cdd:cd07693       2 RIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLetdkdDPRSHRIVLPSGSLFFLRVVHGRKGrsDEGVYVCV 81
                            90
                    ....*....|....*...
gi 1958765569  7555 VENSVGKS-SCTVSVHVS 7571
Cdd:cd07693      82 AHNSLGEAvSRNASLEVA 99
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
8532-8607 1.32e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 54.82  E-value: 1.32e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8532 GSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTcALTVNMLEDADAGDYTCIATN-VAGSDECSAPLTV 8607
Cdd:cd20970      17 GENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGT-TLTIRNIRRSDMGIYLCIASNgVPGSVEKRITLQV 92
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
31769-31959 1.34e-07

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 59.42  E-value: 1.34e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVK-------GTDQVLVKKEISILN-IARHRNILYLHESFESMEELVMIFEFIS 31840
Cdd:cd05055      43 LGAGAFGKVVEATAYGLSKSDAVMKVAVKmlkptahSSEREALMSELKIMShLGNHENIVNLLGACTIGGPILVITEYCC 122
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31841 GLDI--FERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKnsIIKIIEFGQARQLKPGDNFRL 31918
Cdd:cd05055     123 YGDLlnFLRRKRESF-LTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGK--IVKICDFGLARDIMNDSNYVV 199
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 31919 ---LFTAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPF 31959
Cdd:cd05055     200 kgnARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPY 244
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5321-5398 1.34e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.11  E-value: 1.34e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5321 PPSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKN 5398
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
3039-3102 1.36e-07

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 54.17  E-value: 1.36e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  3039 CEVSEPDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVAGGNMSTANLFV 3102
Cdd:cd20967      19 VELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
5150-5225 1.36e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 54.50  E-value: 1.36e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5150 GDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVES-TAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTSIVIV 5225
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
31718-32056 1.39e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 60.48  E-value: 1.39e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31718 SEPSEPTVTKEDKTRAMNYDE---EVDETREVTMTKASHSKtkELYEKYMIAEDLGRGEFGIVHRC-------------- 31780
Cdd:PHA03210    104 SAGDGPSGAEDSDASHLDFDEappDAAGPVPLAQAKLKHDD--EFLAHFRVIDDLPAGAFGKIFICalrasteeaearrg 181
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31781 -----VETSSKKTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMI---FEFisglDIFERINTSA 31852
Cdd:PHA03210    182 vnstnQGKPKCERLIAKRVKAGSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMItqkYDF----DLYSFMYDEA 257
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31853 FELNEREVVSYVR----QVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKiiEFGQArqlKPGDNFRLLFtapEY--- 31925
Cdd:PHA03210    258 FDWKDRPLLKQTRaimkQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLG--DFGTA---MPFEKEREAF---DYgwv 329
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31926 -----YAPEVHQHDVVSSATDMWSLGTLVYVLLSG----INPFLAETNQQMIEnIMNAEYTFDEEaFQEISLEAMDFID- 31995
Cdd:PHA03210    330 gtvatNSPEILAGDGYCEITDIWSCGLILLDMLSHdfcpIGDGGGKPGKQLLK-IIDSLSVCDEE-FPDPPCKLFDYIDs 407
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31996 ----------------------------RLLVKERKSRMTASEALKHPWLKQRMDRVSTkVIRTLRHRRYYHTLIKKDLN 32047
Cdd:PHA03210    408 aeidhaghsvpplirnlglpadfeyplvKMLTFDWHLRPGAAELLALPLFSAEEEEEIL-FIHGLKSGAAHFKPIKPACR 486

                    ....*....
gi 1958765569 32048 MVVSAARIS 32056
Cdd:PHA03210    487 IESDTAALP 495
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8796-8886 1.43e-07

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 54.50  E-value: 1.43e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8796 PPyFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLrPTTTCKMHFKNnvATLVFTQVDSN-DSGEYICRAENS 8874
Cdd:cd20958       1 PP-FIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRL-PLNHRQRVFPN--GTLVIENVQRSsDEGEYTCTARNQ 76
                            90
                    ....*....|...
gi 1958765569  8875 VGE-VSSSTFLTV 8886
Cdd:cd20958      77 QGQsASRSVFVKV 89
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
32306-32396 1.44e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 54.72  E-value: 1.44e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLD-YYALHIRDTLPEDTGYYRVTATNT 32384
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDgTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569 32385 AGSTSCQAHLQV 32396
Cdd:cd05893      81 QGRISCTGRLMV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
33437-33505 1.47e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 54.13  E-value: 1.47e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 33437 IKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd05748      14 IPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
I-set pfam07679
Immunoglobulin I-set domain;
15626-15705 1.48e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.57  E-value: 1.48e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15626 IQIMAGKTLRIPAVVTGRPVPTKVWTIEEGEL-DKERVVIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAAARVE 15704
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 15705 V 15705
Cdd:pfam07679    90 V 90
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7199-7290 1.49e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 54.56  E-value: 1.49e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7199 PPKFIKKLdTSKVAKQGESIQLECKISGSPEIKVVWFRNDSELheSWKYNMSFVNS-VALLTINEASVEDTGDYICEAHN 7277
Cdd:cd20976       1 APSFSSVP-KDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL--QYAADRSTCEAgVGELHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|...
gi 1958765569  7278 GVGHASCSTALKV 7290
Cdd:cd20976      78 AAGQVSCSAWVTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2038-2128 1.50e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 54.42  E-value: 1.50e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIA 2117
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  2118 GETSSHAFLLV 2128
Cdd:cd05744      81 GENSFNAELVV 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
30262-30347 1.51e-07

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 54.57  E-value: 1.51e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30262 VPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKVVIL 30341
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*.
gi 1958765569 30342 DKPGPP 30347
Cdd:cd05762      93 DKPDPP 98
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
18712-18792 1.51e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.11  E-value: 1.51e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18712 KPVLDLKLSGVlTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTSaeSSKFSLTKAKRSDGGKYVVTAT 18791
Cdd:pfam13927     1 KPVITVSPSSV-TVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGS--NSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 18792 N 18792
Cdd:pfam13927    78 N 78
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8893-8977 1.51e-07

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 54.50  E-value: 1.51e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSePI-SVSWYKDGKPLKDSPNvQTSFLDniATLNIFKTDRSL-AGQYSCTVTNP 8970
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGY-PIsSITWEKDGRRLPLNHR-QRVFPN--GTLVIENVQRSSdEGEYTCTARNQ 76

                    ....*...
gi 1958765569  8971 IG-SASSS 8977
Cdd:cd20958      77 QGqSASRS 84
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
6548-6629 1.53e-07

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 54.44  E-value: 1.53e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6548 SMTVTVGETCSLECK-VAGTPELSVEWYKDGKLLTSSQKHKFSFYN--KISSLKILSVEKEDAGTYTFQVQNNVGKSSCT 6624
Cdd:cd05750       8 SQTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNkkKNSELQINKAKLEDSGEYTCVVENILGKDTVT 87

                    ....*
gi 1958765569  6625 AVVDV 6629
Cdd:cd05750      88 GNVTV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
5986-6066 1.53e-07

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 54.52  E-value: 1.53e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5986 VDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFEN-NVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYL 6064
Cdd:cd05737      11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTV 90

                    ..
gi 1958765569  6065 RV 6066
Cdd:cd05737      91 SV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
30257-30340 1.54e-07

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 54.46  E-value: 1.54e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30257 QKTIHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESE-RVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSET 30335
Cdd:cd05894       2 ENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS 81

                    ....*
gi 1958765569 30336 IKVVI 30340
Cdd:cd05894      82 LFVKV 86
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8053-8137 1.54e-07

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 54.32  E-value: 1.54e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8053 KPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIrPGGNYKMtLVENTatLTVLKVAKGDAGQYTCYASNVAGKDSCS 8132
Cdd:cd05725       3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL-PKGRYEI-LDDHS--LKIRKVTAGDMGSYTCVAENMVGKIEAS 78

                    ....*
gi 1958765569  8133 AQLGV 8137
Cdd:cd05725      79 ATLTV 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
7300-7376 1.59e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 54.12  E-value: 1.59e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7300 PPPVGALKGSDVILQCEIS-GTPPFEVVWVKDRKQ-VRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDT 7376
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTlIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7487-7565 1.63e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 54.46  E-value: 1.63e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7487 PEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVrnlASLKIPSAEMNDKGLYSFEVENSVGKSSCT 7565
Cdd:cd20957       8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSE---DVLVIPSVKREDKGMYQCFVRNDGDSAQAT 83
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
33074-33162 1.64e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 54.26  E-value: 1.64e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33074 RILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGK 33153
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                    ....*....
gi 1958765569 33154 QEAQFTLTV 33162
Cdd:cd20949      81 ASDMQERTV 89
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7011-7098 1.64e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 54.33  E-value: 1.64e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDG--VLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNP 7088
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGkqISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|
gi 1958765569  7089 LGTASSTARL 7098
Cdd:cd05893      81 QGRISCTGRL 90
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
5697-5779 1.64e-07

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 54.48  E-value: 1.64e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDGNEI----TDLRRYGISFVDG-LATFQISNARVENS--GTYV 5769
Cdd:cd07693       1 PRIVEHPSDLIV-SKGDPATLNCKAEGRPTPTIQWLKNGQPLetdkDDPRSHRIVLPSGsLFFLRVVHGRKGRSdeGVYV 79
                            90
                    ....*....|
gi 1958765569  5770 CEARNDAGTA 5779
Cdd:cd07693      80 CVAHNSLGEA 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
15614-15705 1.65e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.28  E-value: 1.65e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15614 PTVELDVSvkgGIQIMAGKTLRIPAVVTGRPVPTKVWTIEEGELDKER---VVIENVGTKSELIIKNALRKDHGRYVITA 15690
Cdd:cd20974       1 PVFTQPLQ---SVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpgVQISFSDGRAKLSIPAVTKANSGRYSLTA 77
                            90
                    ....*....|....*
gi 1958765569 15691 TNSCGSKFAAARVEV 15705
Cdd:cd20974      78 TNGSGQATSTAELLV 92
I-set pfam07679
Immunoglobulin I-set domain;
9498-9578 1.66e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.19  E-value: 1.66e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9498 IENQTVLKDNDAIFEIDIkINYPEIKLSWYKGTEKLEPSNKYEITINGDRHTLRVRNCQLKDQGNYRLVC----GPHIAS 9573
Cdd:pfam07679     7 PKDVEVQEGESARFTCTV-TGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGEAEAS 85

                    ....*
gi 1958765569  9574 AKLTV 9578
Cdd:pfam07679    86 AELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5432-5497 1.68e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.49  E-value: 1.68e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5432 ATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSS 5497
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
20899-20982 1.70e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.28  E-value: 1.70e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20899 GLTVKAGDSIVLSAiSILGKPLPKSSWSKAGKDIRPSDI--AQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEH 20976
Cdd:cd20974       9 SVVVLEGSTATFEA-HVSGKPVPEVSWFRDGQVISTSTLpgVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*.
gi 1958765569 20977 VKVSVL 20982
Cdd:cd20974      88 AELLVL 93
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
33890-33978 1.70e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 54.28  E-value: 1.70e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33890 IPPKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEqqgRFHIENTDDLTTLIIMDVQKQDGGLYTLSL 33969
Cdd:cd05747       2 LPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQ---RHQITSTEYKSTFEISKVQMSDEGNYTVVV 78

                    ....*....
gi 1958765569 33970 GNEFGSDSA 33978
Cdd:cd05747      79 ENSEGKQEA 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
32323-32389 1.70e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.49  E-value: 1.70e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32323 VCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDYYaLHIRDTLPEDTGYYRVTATNTAGSTS 32389
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGT-LTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
22670-22743 1.70e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 54.26  E-value: 1.70e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATE 22743
Cdd:cd20949      10 TVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASD 83
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
908-989 1.71e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 54.55  E-value: 1.71e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   908 NVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSiDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYL 987
Cdd:cd05730      12 NATANLGQSVTLACDADGFPEPTMTWTKDGEPIESG-EEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHL 90

                    ..
gi 1958765569   988 AV 989
Cdd:cd05730      91 KV 92
fn3 pfam00041
Fibronectin type III domain;
17139-17213 1.74e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 1.74e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 17139 NLTNDSCKLTWfSPEDDGGSPITNYVIQKREADR-RAWTPVTYTVTRQNATVQGLIQGKSYFFRIAAENSIGMGPF 17213
Cdd:pfam00041    10 DVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
2228-2312 1.74e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.19  E-value: 1.74e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2228 EFVKELQDIEVPESYSGELECIIS--PEnIEGKWYHNDVELKSNGKYSITSRRGRQNLTVKDVTKEDQGEYCFVV--DGK 2303
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtPD-PEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnSAG 80

                    ....*....
gi 1958765569  2304 KTTCKLKMK 2312
Cdd:pfam07679    81 EAEASAELT 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2045-2128 1.75e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 1.75e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2045 QSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVK-IERSDRIYWYWpEDNVCELVIRDVTAEDSASIMVKAINIAGETSSH 2123
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSR-SGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569   2124 AFLLV 2128
Cdd:smart00410    81 TTLTV 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
17469-17708 1.76e-07

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 60.73  E-value: 1.76e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17469 DIWMPVTSASAKTTCKVPKLLEGKDYIFRI----HAENLYGISDplvsdsmkarDRFRVPDAPEQPVVTEVTKDS----- 17539
Cdd:COG4733     477 AVWAFGPDELETQLFRVVSIEENEDGTYTItavqHAPEKYAAID----------AGAFDDVPPQWPPVNVTTSESlsvva 546
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17540 -------ALVTWNKPNDGgkpiTNYILEKRETmSKRWVRVtkePIHPYTKYRVPDLLEGcQYEFRVSAENEIGIGDP--S 17610
Cdd:COG4733     547 qgtavttLTVSWDAPAGA----VAYEVEWRRD-DGNWVSV---PRTSGTSFEVPGIYAG-DYEVRVRAINALGVSSAwaA 617
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17611 PPSKPVFARdpIAKPSPPINPEAIDTTcNSVDLTWQPPRhdgGSKILGYIVEYQKVGDeeWRRANHTPESCPETKYKVTG 17690
Cdd:COG4733     618 SSETTVTGK--TAPPPAPTGLTATGGL-GGITLSWSFPV---DADTLRTEIRYSTTGD--WASATVAQALYPGNTYTLAG 689
                           250
                    ....*....|....*...
gi 1958765569 17691 LRDGQTYKFRVLAVNEAG 17708
Cdd:COG4733     690 LKAGQTYYYRARAVDRSG 707
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
1812-1879 1.76e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 54.12  E-value: 1.76e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1812 VLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYD--GIHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd20973       9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDedGLCSLIISDVCGDDSGKYTCKAVNSLG 78
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6550-6625 1.78e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 54.07  E-value: 1.78e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6550 TVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKissLKILSVEKEDAGTYTFQVQNNVGKSSCTA 6625
Cdd:cd20957      12 TVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDV---LVIPSVKREDKGMYQCFVRNDGDSAQATA 84
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6928-7002 1.78e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 53.75  E-value: 1.78e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6928 VGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTaASKTVF 7002
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGE-KSATIN 79
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8423-8511 1.79e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 54.32  E-value: 1.79e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8423 TIVEKPESIKVTT-GDTCTLECMVSGTPELSTKWFKDGKELTGDSkyKISFFNKvSGLKIISVAPGDSGVYSFEVQNPVG 8501
Cdd:cd20978       2 KFIQKPEKNVVVKgGQDVTLPCQVTGVPQPKITWLHNGKPLQGPM--ERATVED-GTLTIINVQPEDTGYYGCVATNEIG 78
                            90
                    ....*....|
gi 1958765569  8502 KDSCTVSIQV 8511
Cdd:cd20978      79 DIYTETLLHV 88
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
31765-31975 1.80e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 58.83  E-value: 1.80e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHRcveTSSKKTFMAKFVKVKGTDQ---VLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14152       4 LGELIGQGRWGKVHR---GRWHGEVAIRLLEIDGNNQdhlKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLKPG---DNFRL 31918
Cdd:cd14152      81 RTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVQEGrreNELKL 160
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31919 LFTAPEYYAPEV-------HQHDVV--SSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAE 31975
Cdd:cd14152     161 PHDWLCYLAPEIvremtpgKDEDCLpfSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGE 226
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
29169-29249 1.80e-07

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 54.08  E-value: 1.80e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29169 ITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLKETD-RMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITV 29247
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 29248 VV 29249
Cdd:cd05894      85 KV 86
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8048-8137 1.81e-07

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 54.34  E-value: 1.81e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVEN-TATLTVLKVAKGDAGQYTCYASNVA 8126
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENgVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  8127 GKDSCSAQLGV 8137
Cdd:cd20990      81 GQNSFNLELVV 91
fn3 pfam00041
Fibronectin type III domain;
21870-21956 1.81e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 1.81e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21870 DPPGKPVPLNITRHTVALKWAKPEYTGGfKITSYVVEKRDL-PNGRWLKANFSNIlENEFTVSGLTEDAAYEFRVIAKNA 21948
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKnSGEPWNEITVPGT-TTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*...
gi 1958765569 21949 AGaISPPS 21956
Cdd:pfam00041    79 GG-EGPPS 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7577-7666 1.83e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.28  E-value: 1.83e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEI--ISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANV 7654
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIstSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  7655 AGQDESSALLTV 7666
Cdd:cd20974      81 SGQATSTAELLV 92
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
31768-32019 1.83e-07

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 58.88  E-value: 1.83e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31768 DLGRGEFGIVH--RCVETSS-----KKTFMAKFVKVKGTDqvlVKKEISILNIARHRNILYLHESF--ESMEELVMIFEF 31838
Cdd:cd06634      22 EIGHGSFGAVYfaRDVRNNEvvaikKMSYSGKQSNEKWQD---IIKEVKFLQKLRHPNTIEYRGCYlrEHTAWLVMEYCL 98
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 ISGLDIFErinTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLKPGDNFrl 31918
Cdd:cd06634      99 GSASDLLE---VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLT--EPGLVKLGDFGSASIMAPANSF-- 171
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31919 lFTAPEYYAPEV------HQHDvvsSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFQEISLEamD 31992
Cdd:cd06634     172 -VGTPYWMAPEVilamdeGQYD---GKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQSGHWSEYFR--N 245
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 31993 FIDRLLVKERKSRMTASEALKHPWLKQ 32019
Cdd:cd06634     246 FVDSCLQKIPQDRPTSDVLLKHRFLLR 272
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
31759-32017 1.83e-07

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 58.92  E-value: 1.83e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31759 LYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKV--------KGTDQVLVKKEISILNIARHRNILYLHESFE-SM 31829
Cdd:cd14041       4 LNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLnknwrdekKENYHKHACREYRIHKELDHPRIVKLYDYFSlDT 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGLDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQN--IGHFDIRPENIIY-QTRKNSIIKIIEFGQ 31906
Cdd:cd14041      84 DSFCTVLEYCEGNDLDFYLKQHKL-MSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvNGTACGEIKITDFGL 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARqLKPGDNFRLL----FTAPE-----YYAPEV----HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMI--EN- 31970
Cdd:cd14041     163 SK-IMDDDSYNSVdgmeLTSQGagtywYLPPECfvvgKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDIlqENt 241
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 1958765569 31971 IMNA-EYTFDEEAFqeISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd14041     242 ILKAtEVQFPPKPV--VTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5236-5317 1.84e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 1.84e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   5236 KSIEVLKEYDVMLLAEVAGTPPFEITWFKDN-TTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEVGSSTCSA 5314
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ...
gi 1958765569   5315 RVT 5317
Cdd:smart00410    82 TLT 84
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
31047-31132 1.88e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 54.17  E-value: 1.88e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31047 VRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQ-SRKYKMSSDGRThtLTVMTEEQEDEGVYTCVATNEVGE 31125
Cdd:cd05730       6 ARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESgEEKYSFNEDGSE--MTILDVDKLDEAEYTCIAENKAGE 83

                    ....*..
gi 1958765569 31126 VETSSKL 31132
Cdd:cd05730      84 QEAEIHL 90
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5135-5216 1.89e-07

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 54.49  E-value: 1.89e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5135 ATFTEklepsQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMS-FVESTAV----LRLTDVAIEDSGEYMCE 5209
Cdd:cd20956       6 ETFSE-----QTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGdYVTSDGDvvsyVNISSVRVEDGGEYTCT 80

                    ....*..
gi 1958765569  5210 AQNEAGS 5216
Cdd:cd20956      81 ATNDVGS 87
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
9292-9380 1.90e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 53.94  E-value: 1.90e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKT-TATFIAKVGGDPIPNVKWT-KGKWRQLNQGgRILIHQKGdeskLEIRDTTKTDSGLYRCVAFNKH 9369
Cdd:cd20978       3 FIQKPEKNVVVKGGqDVTLPCQVTGVPQPKITWLhNGKPLQGPME-RATVEDGT----LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  9370 GEIESNVNLQV 9380
Cdd:cd20978      78 GDIYTETLLHV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28084-28147 1.91e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 1.91e-07
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  28084 QISVRIGHNVHLELPYKGKPKPSISWLKDGL-PLKESEYVRFSKTENKITLSIKNVKKENGGKYT 28147
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYT 67
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4870-4939 1.95e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.49  E-value: 1.95e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4870 ATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETT 4939
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6543-6622 1.95e-07

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 54.34  E-value: 1.95e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6543 VEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFY-NKISSLKILSVEKEDAGTYTFQVQNNVGKS 6621
Cdd:cd20990       4 LQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVReNGVHSLIIEPVTSRDAGIYTCIATNRAGQN 83

                    .
gi 1958765569  6622 S 6622
Cdd:cd20990      84 S 84
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
17329-17427 1.96e-07

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 54.57  E-value: 1.96e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17329 PPTLdLDFRDKLTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENS 17408
Cdd:cd05762       1 PPQI-IQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENK 79
                            90
                    ....*....|....*....
gi 1958765569 17409 TGSRKGFCQVNVVDRPGPP 17427
Cdd:cd05762      80 LGSRQAQVNLTVVDKPDPP 98
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
25621-25708 2.02e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.28  E-value: 2.02e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25621 LDADLRKVVTLRASaTLRLFVTIKGRPEPEVKWEKAEGILT----ERAQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNS 25696
Cdd:cd20974       3 FTQPLQSVVVLEGS-TATFEAHVSGKPVPEVSWFRDGQVIStstlPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|..
gi 1958765569 25697 GSKTAFVNVRVL 25708
Cdd:cd20974      82 GQATSTAELLVL 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1515-1594 2.03e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.72  E-value: 2.03e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1515 KPAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGTKGEaaLKIDSTISQDSAWYTATAIN 1594
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNST--LTISNVTRSDAGTYTCVASN 78
PRK10819 PRK10819
transport protein TonB; Provisional
10146-10254 2.03e-07

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 58.16  E-value: 2.03e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10146 KVEPPAVKVPEAPKKPVPE--EKKPVPIPKKEPAAPPKVpeapkKPAPEektavPVAKKKEAPPPKVTEVQKKVVTEEKI 10223
Cdd:PRK10819     65 QPPPEPVVEPEPEPEPIPEppKEAPVVIPKPEPKPKPKP-----KPKPK-----PVKKVEEQPKREVKPVEPRPASPFEN 134
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1958765569 10224 TIIPQREESPPPAVPEIPKKKVPEEKRPVPR 10254
Cdd:PRK10819    135 TAPARPTSSTATAAASKPVTSVSSGPRALSR 165
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5065-5127 2.04e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.49  E-value: 2.04e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5065 FQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSN-VAGSVECSA 5127
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
31769-32018 2.05e-07

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 58.91  E-value: 2.05e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKF-----VKVKGTDQVLVKKEI--SILNIARHRNILYLHESFESMEELVMIFEFISG 31841
Cdd:cd14223       8 IGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGETLALNERImlSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31842 LDIFERINTSAFeLNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKPGDNFRLLFT 31921
Cdd:cd14223      88 GDLHYHLSQHGV-FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH--VRISDLGLACDFSKKKPHASVGT 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31922 APeYYAPEVHQHDVV-SSATDMWSLGTLVYVLLSGINPFLAETNQQMIEnIMNAEYTFDEEAFQEISLEAMDFIDRLLVK 32000
Cdd:cd14223     165 HG-YMAPEVLQKGVAyDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-IDRMTLTMAVELPDSFSPELRSLLEGLLQR 242
                           250       260
                    ....*....|....*....|...
gi 1958765569 32001 ERKSRM-----TASEALKHPWLK 32018
Cdd:cd14223     243 DVNRRLgcmgrGAQEVKEEPFFR 265
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
33416-33506 2.06e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.28  E-value: 2.06e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSS--KYKLSNDKEEFILEILKTETSDGGLYSCTVANS 33493
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 33494 AGSVSSSCKLTIK 33506
Cdd:cd20974      81 SGQATSTAELLVL 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
11648-11714 2.10e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.49  E-value: 2.10e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 11648 AIFECLVSPSTAIT-TWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTST 11714
Cdd:cd00096       1 VTLTCSASGNPPPTiTWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4674-4747 2.13e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.66  E-value: 2.13e-07
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569   4674 EPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQ-IRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEVGK 4747
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
32886-32962 2.13e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.72  E-value: 2.13e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32886 PRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTN 32962
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
19416-19500 2.16e-07

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 54.13  E-value: 2.16e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19416 MPEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLI-IKDVTRKDSGYYSLTAENSSGTDTQ 19494
Cdd:cd05737       7 LPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFtINGVSSEDSGKYGLVVKNKYGSETS 86

                    ....*.
gi 1958765569 19495 KIKVTV 19500
Cdd:cd05737      87 DVTVSV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
33891-33984 2.18e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 53.94  E-value: 2.18e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIqsQEQQGRFHIENtddlTTLIIMDVQKQDGGLYTLSLG 33970
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL--QGPMERATVED----GTLTIINVQPEDTGYYGCVAT 74
                            90
                    ....*....|....
gi 1958765569 33971 NEFGSDSATVNINI 33984
Cdd:cd20978      75 NEIGDIYTETLLHV 88
I-set pfam07679
Immunoglobulin I-set domain;
33612-33689 2.18e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.80  E-value: 2.18e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33612 MNITSGQRVTLKANIAGATD--VKWVLNGTELSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCIGKTSQGVVKCQFDLT 33689
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
31769-31968 2.19e-07

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 58.17  E-value: 2.19e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCvetSSKKTFMAKFVKVKG---TDQVLVKKEISILNIARHRNILyLHESFESMEELVMIFEFISGLDIF 31845
Cdd:cd14062       1 IGSGSFGTVYKG---RWHGDVAVKKLNVTDptpSQLQAFKNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEGSSLY 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31846 ERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQArQLKPGDNFRLLFTAPE- 31924
Cdd:cd14062      77 KHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLH--EDLTVKIGDFGLA-TVKTRWSGSQQFEQPTg 153
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31925 ---YYAPEVHQHDVV---SSATDMWSLGTLVYVLLSGINPFLAETNQQMI 31968
Cdd:cd14062     154 silWMAPEVIRMQDEnpySFQSDVYAFGIVLYELLTGQLPYSHINNRDQI 203
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
23456-23543 2.21e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.28  E-value: 2.21e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23456 LDLELRKVInIRAGGSLRLFVPIKGRPTPEVKWGKvDGEIRDAAI-----IDVTSSFTSLVLDNVNRYDSGKYTLTLENS 23530
Cdd:cd20974       3 FTQPLQSVV-VLEGSTATFEAHVSGKPVPEVSWFR-DGQVISTSTlpgvqISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 23531 SGTKSAFVTVRVL 23543
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4956-5038 2.21e-07

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 53.94  E-value: 2.21e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4956 RNVDSVVGGACRLDCKIAGSLPM-RVSWFKDGKEIAASD-RYQIafVEGtASLEISRVDMNDAGNFTCRATNSVGSKDSR 5033
Cdd:cd05724       5 SDTQVAVGEMAVLECSPPRGHPEpTVSWRKDGQPLNLDNeRVRI--VDD-GNLLIAEARKSDEGTYKCVATNMVGERESR 81

                    ....*.
gi 1958765569  5034 GA-LIV 5038
Cdd:cd05724      82 AArLSV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
31047-31132 2.24e-07

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 54.04  E-value: 2.24e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31047 VRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGK-ELVQSRKYKMSSDGrthTLTVMTEEQEDEGVYTCVATNEVGE 31125
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVpLLGKDERITTLENG---SLQIKGAEKSDTGEYTCVALNLSGE 78

                    ....*..
gi 1958765569 31126 VETSSKL 31132
Cdd:cd20952      79 ATWSAVL 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6446-6537 2.27e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.90  E-value: 2.27e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEV-VRESENVRISFVNNVATLQFAKAEPANAGKYICQVKND 6524
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIsTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  6525 GGVRENMASLTVL 6537
Cdd:cd20974      81 SGQATSTAELLVL 93
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
28189-28377 2.30e-07

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 60.34  E-value: 2.30e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28189 SWDIPEDDGGgeitcYSIEKREASqTNWkmvcSSVARTT---FKVSNLVkDSEYQFRVRAENRYGVSEPLVSNVIVAkHQ 28265
Cdd:COG4733     557 SWDAPAGAVA-----YEVEWRRDD-GNW----VSVPRTSgtsFEVPGIY-AGDYEVRVRAINALGVSSAWAASSETT-VT 624
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28266 FRIpGPPGKPVIYNVTS--DGMSLTWDAPVydgGSEVTGFHVEKKERNSILWQRVNTSPISGREYRATGLIEGLDYQFRV 28343
Cdd:COG4733     625 GKT-APPPAPTGLTATGglGGITLSWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRA 700
                           170       180       190
                    ....*....|....*....|....*....|....
gi 1958765569 28344 YAENSAGLSSPsdpsKFTLAVSPVDPPGTPDYID 28377
Cdd:COG4733     701 RAVDRSGNVSA----WWVSGQASADAAGILDAIT 730
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
7867-7935 2.35e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 54.17  E-value: 2.35e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7867 AAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAyKMQFKNNVASLVINKVDHSDVGEYTCKAENSVG 7935
Cdd:cd05730      15 ANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAG 82
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4393-4476 2.38e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 53.69  E-value: 2.38e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4393 PKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADnkhSLELSNLTVQDRGVYSCKASNKfgADICQ- 4471
Cdd:cd20957       8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRND--GDSAQa 82

                    ....*.
gi 1958765569  4472 -AELTI 4476
Cdd:cd20957      83 tAELKL 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
28093-28154 2.39e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.10  E-value: 2.39e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 28093 VHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDNAV 28154
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSA 62
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6446-6536 2.39e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 53.96  E-value: 2.39e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESENVRISFVN--NVATLQFAKAEPANAGKYICQVKN 6523
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESeyGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569  6524 DGGVRENMASLTV 6536
Cdd:cd20951      81 IHGEASSSASVVV 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
33698-33787 2.40e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 53.94  E-value: 2.40e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNI-NEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRnmyTLEIRNASVSDSGKYTVKAKNFR 33776
Cdd:cd20978       1 PKFIQKPEKNVVvKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDG---TLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569 33777 GQCSATASLTV 33787
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
24146-24219 2.41e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 53.90  E-value: 2.41e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 24146 TIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSK 24219
Cdd:cd05747      12 SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQ 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
25629-25707 2.41e-07

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 53.69  E-value: 2.41e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25629 VTLRASATLRLFVTIKGRPEPEVKWEKAEGILTE---RAQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVNV 25705
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTAtegRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 25706 RV 25707
Cdd:cd05894      85 KV 86
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
4572-4664 2.43e-07

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 53.87  E-value: 2.43e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4572 PPSFVKKVDPSYLMLpGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSfansEAILDITDVKVDDSGTYSCEATND 4651
Cdd:cd05851       1 PADINVKFKDTYALK-GQNVTLECFALGNPVPVIRWRKILEPMPATAEISMS----GAVLKIFNIQPEDEGTYECEAENI 75
                            90
                    ....*....|...
gi 1958765569  4652 AGSDSCSTEVVIK 4664
Cdd:cd05851      76 KGKDKHQARVYVQ 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6640-6725 2.47e-07

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 53.55  E-value: 2.47e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6640 RRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGaKYQTtFSDNvcTLQLNSLDSSDMGSYTCVAANVAGSDEC 6719
Cdd:cd05725       2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEI-LDDH--SLKIRKVTAGDMGSYTCVAENMVGKIEA 77

                    ....*.
gi 1958765569  6720 RALLTV 6725
Cdd:cd05725      78 SATLTV 83
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4301-4380 2.48e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 53.90  E-value: 2.48e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4301 LEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLT 4380
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTLT 92
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4949-5033 2.51e-07

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 53.73  E-value: 2.51e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRyQIAFVEGTasLEISRVDMN-DAGNFTCRATNSV 5027
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR-QRVFPNGT--LVIENVQRSsDEGEYTCTARNQQ 77

                    ....*.
gi 1958765569  5028 GSKDSR 5033
Cdd:cd20958      78 GQSASR 83
fn3 pfam00041
Fibronectin type III domain;
16940-17018 2.52e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 2.52e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16940 KVTDWTKSSVDLEWSPPlKDGGSKITGYIVEYKEEGKEEWEKGKDkeVRGTK--LVVTGLKEGAFYKFRVRAVNIAGVGE 17017
Cdd:pfam00041     7 TVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEIT--VPGTTtsVTLTGLKPGTEYEVRVQAVNGGGEGP 83

                    .
gi 1958765569 17018 P 17018
Cdd:pfam00041    84 P 84
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
31769-31986 2.52e-07

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 57.91  E-value: 2.52e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKTFMAKFVKVKgTDQVLVKKEISILNIARHRNIL-YLHESFESmEELVMIFEFISGLDIFER 31847
Cdd:cd14156       1 IGSGFFSKVYKVTHGATGKVMVVKIYKND-VDQHKIVREISLLQKLSHPNIVrYLGICVKD-EKLHPILEYVSGGCLEEL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31848 INTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPEN-IIYQTRKNSIIKIIEFGQARQL------KPGDNFRLLF 31920
Cdd:cd14156      79 LAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNcLIRVTPRGREAVVTDFGLAREVgempanDPERKLSLVG 158
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31921 TApEYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGI--NP-FLAETNqqmienimnaEYTFDEEAFQEI 31986
Cdd:cd14156     159 SA-FWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIpaDPeVLPRTG----------DFGLDVQAFKEM 216
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
23750-23829 2.57e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 53.74  E-value: 2.57e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23750 SYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIEI 23829
Cdd:cd20972      10 SQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEI 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6915-7000 2.57e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 53.65  E-value: 2.57e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNN-VATLVFNKVGINDSGEYTCVAENSI 6993
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80

                    ....*..
gi 1958765569  6994 GTAASKT 7000
Cdd:cd05744      81 GENSFNA 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5511-5601 2.58e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.90  E-value: 2.58e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASD--KYKFSFHDNTAFLEISQLEGTDSGTYTCSATNK 5588
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  5589 AGHSQCSGHLTVK 5601
Cdd:cd20974      81 SGQATSTAELLVL 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
3304-3380 2.59e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.34  E-value: 2.59e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  3304 PPAIVTPLQDAVTSEGRPARFQCQVSGTDL-KVSWYCRDKKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANN 3380
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPpTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
23748-23832 2.63e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.90  E-value: 2.63e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23748 FSSYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTT--RINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTA 23825
Cdd:cd20974       7 LQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86

                    ....*..
gi 1958765569 23826 AIEIITL 23832
Cdd:cd20974      87 TAELLVL 93
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
5699-5787 2.64e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 53.87  E-value: 2.64e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5699 FIKKPSpVLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEIT----DLRRYGIsFVDGLAtfqISNARVENSGTYVCEARN 5774
Cdd:cd20949       2 FTENAY-VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISasvaDMSKYRI-LADGLL---INKVTQDDTGEYTCRAYQ 76
                            90
                    ....*....|...
gi 1958765569  5775 DAGTASCSIELKV 5787
Cdd:cd20949      77 VNSIASDMQERTV 89
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
33894-33984 2.65e-07

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 53.76  E-value: 2.65e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33894 IEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQ------QGRFhientddlTTLIIMDVQKQDGGLYTL 33967
Cdd:cd05891       4 IGGLPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHysvkleQGKY--------ASLTIKGVTSEDSGKYSI 75
                            90
                    ....*....|....*..
gi 1958765569 33968 SLGNEFGSDSATVNINI 33984
Cdd:cd05891      76 NVKNKYGGETVDVTVSV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
24846-24907 2.69e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.10  E-value: 2.69e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 24846 PVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATE 24907
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
12175-12245 2.69e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.34  E-value: 2.69e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12175 PYFTVKLHDKTGVEKDEIILKCEVSKDVP--VKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC 12245
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPptITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTC 74
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7856-7946 2.71e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.90  E-value: 2.71e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEH--TKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENS 7933
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  7934 VGAVASSAVLVIK 7946
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
17330-17420 2.71e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.90  E-value: 2.71e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17330 PTLDLDFRDKLtVRVGEAFALTGRYSGKPKPKVDWFKDE--ADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVEN 17407
Cdd:cd20974       1 PVFTQPLQSVV-VLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|...
gi 1958765569 17408 STGSRKGFCQVNV 17420
Cdd:cd20974      80 GSGQATSTAELLV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8518-8607 2.73e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.90  E-value: 2.73e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGR--KYQTTLTDNTCALTVNMLEDADAGDYTCIATNV 8595
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  8596 AGSDECSAPLTV 8607
Cdd:cd20974      81 SGQATSTAELLV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12185-12258 2.74e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.66  E-value: 2.74e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12185 TGVEKDEIILKCEVSKDVP--VKWFKDG-EEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC----DCGTDTTKANVT 12257
Cdd:smart00410     5 TVKEGESVTLSCEASGSPPpeVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCaatnSSGSASSGTTLT 84

                     .
gi 1958765569  12258 V 12258
Cdd:smart00410    85 V 85
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8050-8139 2.79e-07

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 53.81  E-value: 2.79e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8050 FDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKD--------NREIRPGGNYkmtLVENTATLTVLKVAKGDAGQYTCY 8121
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEgsqnllfpYQPPQPSSRF---SVSPTGDLTITNVQRSDVGYYICQ 78
                            90
                    ....*....|....*...
gi 1958765569  8122 ASNVAGKDSCSAQLGVQE 8139
Cdd:cd05726      79 ALNVAGSILAKAQLEVTD 96
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
19818-19897 2.83e-07

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 53.65  E-value: 2.83e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19818 TVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKqTEGVKMAMKRNlCTLELFSVNRKDSGDYTITAENSSGSKSATIKLKV 19897
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKDGVPLL-GKDERITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
104-193 2.83e-07

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 53.57  E-value: 2.83e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQ-SSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSV 182
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRpDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569   183 GRATSTADLLV 193
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
5980-6066 2.84e-07

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 53.62  E-value: 2.84e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5980 IEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGK--QIVPSRyFSMSFEN-NVASFRIQSVMKQDSGQYTFKVENDFG 6056
Cdd:cd05892       4 IQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEmlQYNTDR-ISLYQDNcGRICLLIQNANKKDAGWYTVSAVNEAG 82
                            90
                    ....*....|
gi 1958765569  6057 SSSCDAYLRV 6066
Cdd:cd05892      83 VVSCNARLDV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
4759-4849 2.87e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 53.79  E-value: 2.87e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4759 PPTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKiKMSFSSGVAVLTISDVQIGLGGKYTCLAENEA 4838
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  4839 GSQTSVGELIV 4849
Cdd:cd20976      80 GQVSCSAWVTV 90
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
31756-32017 2.89e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 58.90  E-value: 2.89e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31756 TKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK---EISILNIARHRNILYL------HESF 31826
Cdd:cd07875      19 TFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRayrELVLMKCVNHKNIIGLlnvftpQKSL 98
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31827 ESMEELVMIFEFISGlDIFERINtsaFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQ 31906
Cdd:cd07875      99 EEFQDVYIVMELMDA-NLCQVIQ---MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIV--VKSDCTLKILDFGL 172
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARqlKPGDNFRLL-FTAPEYY-APEVHQHDVVSSATDMWSLGTLVYVLLSGINPF------------------------- 31959
Cdd:cd07875     173 AR--TAGTSFMMTpYVVTRYYrAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFpgtdhidqwnkvieqlgtpcpefmk 250
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31960 -LAETNQQMIENIMN-AEYTF-----------DEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07875     251 kLQPTVRTYVENRPKyAGYSFeklfpdvlfpaDSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYI 321
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
8052-8141 2.90e-07

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 54.09  E-value: 2.90e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8052 LKPVSVDLALGESGSFKCHVT--GTAPIKITWAKDNREI---RPGGNY-KMTLVENTATLTVLKVAKGDAGQYTCYASNV 8125
Cdd:cd04970       7 LAPSNADITVGENATLQCHAShdPTLDLTFTWSFNGVPIdleKIEGHYrRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTV 86
                            90
                    ....*....|....*.
gi 1958765569  8126 AGKDSCSAQLGVQEPP 8141
Cdd:cd04970      87 VDSDSASATLVVRGPP 102
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
4588-4663 2.91e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 53.17  E-value: 2.91e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESntvRMSFANSeailditdVKVDDSGTYSCEATNDAGS-DSCSTEVVI 4663
Cdd:pfam13895    14 GEPVTLTCSAPGNPPPSYTWYKDGSAISSS---PNFFTLS--------VSAEDSGTYTCVARNGRGGkVSNPVELTV 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6352-6436 2.93e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 53.79  E-value: 2.93e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6352 PPVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFhASIHILNVDSTDIGEYHCKAQNEV 6431
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGV-GELHIQDVLPEDHGTYTCLAKNAA 79

                    ....*
gi 1958765569  6432 GSDTC 6436
Cdd:cd20976      80 GQVSC 84
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
31057-31135 2.94e-07

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 53.80  E-value: 2.94e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31057 KLGEAAQLSCQIVGRPLPDIKWYRFGKELV--QSRKYKMSSDGRThtLTVMTEEQEDEGVYTCVATNEVGEVETSSKLLL 31134
Cdd:cd05736      13 EPGVEASLRCHAEGIPLPRVQWLKNGMDINpkLSKQLTLIANGSE--LHISNVRYEDTGAYTCIAKNEGGVDEDISSLFV 90

                    .
gi 1958765569 31135 Q 31135
Cdd:cd05736      91 E 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
19433-19496 2.96e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.10  E-value: 2.96e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 19433 HVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKI 19496
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
12982-13048 2.98e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 53.35  E-value: 2.98e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 12982 ANLEVSEGDTIKLVCEVS--KPGAEVTWYKGDEeVIETGRFEILTDGRKRI--LIIQNAQLEDAGSYNCRL 13048
Cdd:pfam00047     4 PTVTVLEGDSATLTCSAStgSPGPDVTWSKEGG-TLIESLKVKHDNGRTTQssLLISNVTKEDAGTYTCVV 73
I-set pfam07679
Immunoglobulin I-set domain;
13931-13996 2.98e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.42  E-value: 2.98e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 13931 TGYPRPKATWTFGDQVLEAGDRVKIKTISAYAELIISPSERPDKGIYTLTLENPVKSISGEIDVNV 13996
Cdd:pfam07679    25 TGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
15907-15997 3.01e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.90  E-value: 3.01e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15907 PTIKLRLAvrgdTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKPTdalnITKEEVSRSEAKTELSIPKAVREDKGT 15986
Cdd:cd20974       1 PVFTQPLQ----SVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTST----LPGVQISFSDGRAKLSIPAVTKANSGR 72
                            90
                    ....*....|.
gi 1958765569 15987 YTITASNRLGS 15997
Cdd:cd20974      73 YSLTATNGSGQ 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33245-33317 3.02e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.28  E-value: 3.02e-07
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  33245 AKLTCAVESSAlcAKEVAWYKDG-KKLKENGHFQFHYSaDGTYELKIHNLSESDCGEYVCEVSGEGGTSKTSFQ 33317
Cdd:smart00410    12 VTLSCEASGSP--PPEVTWYKQGgKLLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
31767-31959 3.02e-07

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 57.75  E-value: 3.02e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVHrcvetssKKTFMAKFVKVK-------GTDQVLvkKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05039      12 ELIGKGEFGDVM-------LGDYRGQKVAVKclkddstAAQAFL--AEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYM 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 SGLDIFERINTSAFELNER-EVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQAR---QLKPGDN 31915
Cdd:cd05039      83 AKGSLVDYLRSRGRAVITRkDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVS--EDNVAKVSDFGLAKeasSNQDGGK 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 31916 FRLLFTAPEYYapevhQHDVVSSATDMWSLGTLVYVLLS-GINPF 31959
Cdd:cd05039     161 LPIKWTAPEAL-----REKKFSTKSDVWSFGILLWEIYSfGRVPY 200
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8610-8700 3.07e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 53.41  E-value: 3.07e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8610 PPSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSEL-VPGARCNVSLQdsVAELELFDVDTSQSGDYTCIVSNE 8688
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTCEAG--VGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  8689 AGRASCTTQLFV 8700
Cdd:cd20976      79 AGQVSCSAWVTV 90
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
5990-6064 3.14e-07

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 53.35  E-value: 3.14e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5990 EKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVasfRIQSVMKQDSGQYTFKVENDFGSSSCDAYL 6064
Cdd:cd05723      11 ESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNL---QVLGLVKSDEGFYQCIAENDVGNAQASAQL 82
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
31768-32018 3.16e-07

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 58.22  E-value: 3.16e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31768 DLGRGEFGIVHRCVETSSKKTFMAKFVK--VKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISG--LD 31843
Cdd:cd06615       8 ELGAGNGGVVTKVLHRPSGLIMARKLIHleIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGgsLD 87
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERintSAFELNEREVVSYVRQVCEALEFLHSQ-NIGHFDIRPENIIYQTRKNsiIKIIEFGQARQLKpgDNFRLLFTA 31922
Cdd:cd06615      88 QVLK---KAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGE--IKLCDFGVSGQLI--DSMANSFVG 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31923 PE-YYAPEVHQ--HDVVSSatDMWSLGTLVYVLLSGINPFLAEtNQQMIENIMNAEYTFDEEAFQEI------------- 31986
Cdd:cd06615     161 TRsYMSPERLQgtHYTVQS--DIWSLGLSLVEMAIGRYPIPPP-DAKELEAMFGRPVSEGEAKESHRpvsghppdsprpm 237
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31987 ----------------------SLEAMDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd06615     238 aifelldyivnepppklpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8993-9078 3.17e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 53.17  E-value: 3.17e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8993 IPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISylensahltivKVDKGDSGQYTCYAINE-VGKDS 9071
Cdd:pfam13895     4 LTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTL-----------SVSAEDSGTYTCVARNGrGGKVS 72

                    ....*..
gi 1958765569  9072 CTAQLNI 9078
Cdd:pfam13895    73 NPVELTV 79
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
12175-12258 3.24e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 53.36  E-value: 3.24e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12175 PYFTVKLHDKTGVEKDEIILKCEVSKDVP--VKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC----DCG 12248
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTpvVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSClatnSVG 81
                            90
                    ....*....|
gi 1958765569 12249 TDTTKANVTV 12258
Cdd:cd20972      82 SDTTSAEIFV 91
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
33074-33152 3.25e-07

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 53.71  E-value: 3.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33074 RILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVST---SARHQVTTAKYKSTFEISSVQA----SDEGNYSVV 33146
Cdd:cd07693       2 RIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETdkdDPRSHRIVLPSGSLFFLRVVHGrkgrSDEGVYVCV 81

                    ....*.
gi 1958765569 33147 VENTDG 33152
Cdd:cd07693      82 AHNSLG 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
18417-18497 3.27e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.95  E-value: 3.27e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18417 PPEVELDvtcRDVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAK 18496
Cdd:pfam13927     1 KPVITVS---PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 18497 N 18497
Cdd:pfam13927    78 N 78
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4291-4381 3.27e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 53.36  E-value: 3.27e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4291 APVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEY 4370
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  4371 GSVSCTATLTV 4381
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8799-8886 3.35e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 53.39  E-value: 3.35e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8799 FVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYK-GDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGE 8877
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKdGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81

                    ....*....
gi 1958765569  8878 VSSSTFLTV 8886
Cdd:cd05763      82 ISANATLTV 90
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
12717-12792 3.36e-07

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 53.01  E-value: 3.36e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12717 VTVTAGETATFDCELSYEDIPVEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAKDFKTQANLFV 12792
Cdd:cd20967       7 VQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6746-6814 3.40e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 52.72  E-value: 3.40e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6746 ITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNNA-GQASCTT 6814
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1680-1754 3.41e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 53.65  E-value: 3.41e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1680 AHFECRLTpiGDPTMVVEWLHDGKPL-EAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:cd05744      18 CRFDCKVS--GLPTPDLFWQLNGKPVrPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
33087-33162 3.58e-07

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 53.37  E-value: 3.58e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33087 GESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKykstFEISSVQASDEGNYSVVVENTDGKQEAQFTLTV 33162
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
31865-32017 3.62e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 58.02  E-value: 3.62e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31865 RQVCEALEFLHSQNIGHFDIRPENIIYqTRKNSIIKIIEFGQArqLKPGDNFRLLFTAPEYYAPEVHQHDVV-------- 31936
Cdd:cd14020     117 RDVLEALAFLHHEGYVHADLKPRNILW-SAEDECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAELQNCLaqaglqse 193
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31937 ---SSATDMWSLGTLVYVLLSGINpfLAET--NQQMIENIMN-AEYTFDEEAFQEISLEAM---DFIDRLLVKERKSRMT 32007
Cdd:cd14020     194 tecTSAVDLWSLGIVLLEMFSGMK--LKHTvrSQEWKDNSSAiIDHIFASNAVVNPAIPAYhlrDLIKSMLHNDPGKRAT 271
                           170
                    ....*....|
gi 1958765569 32008 ASEALKHPWL 32017
Cdd:cd14020     272 AEAALCSPFF 281
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
32200-32293 3.65e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 53.36  E-value: 3.65e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32200 PPEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDdkkYTFESDKGLYQLTINSVTTDDDAEYAVVAR 32279
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPD---IQIHQEGDLHSLIIAEAFEEDTGRYSCLAT 77
                            90
                    ....*....|....
gi 1958765569 32280 NKHGEDSCKAKLTV 32293
Cdd:cd20972      78 NSVGSDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
23150-23234 3.65e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 3.65e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23150 GPPEGPVAiSGVTAEKCMLAWKPPLqDGGSDIINYIVERRET---SRLVWTLVDANvqTLSCKVTKLLEGNEYIFRIMAV 23226
Cdd:pfam00041     1 SAPSNLTV-TDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnsgEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAV 76

                    ....*...
gi 1958765569 23227 NKYGVGEP 23234
Cdd:pfam00041    77 NGGGEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5621-5690 3.68e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 52.72  E-value: 3.68e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5621 VQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSNDVGTTSSKAT 5690
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
3199-3288 3.69e-07

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 53.71  E-value: 3.69e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLST-----GFKCKFLHDGQEYTLLLIEA--FPEDAAVYTC 3271
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETdkddpRSHRIVLPSGSLFFLRVVHGrkGRSDEGVYVC 80
                            90
                    ....*....|....*...
gi 1958765569  3272 EAKNDYGVATT-SASLSV 3288
Cdd:cd07693      81 VAHNSLGEAVSrNASLEV 98
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5702-5774 3.69e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 53.35  E-value: 3.69e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5702 KPSPVLVLRNGQSTTFECQV-TGTPEIRVSWYLDGNEITDLRRYGISFVD-GLATFQISNARVENSGTYVCEARN 5774
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRtTQSSLLISNVTKEDAGTYTCVVNN 75
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
900-989 3.70e-07

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 53.32  E-value: 3.70e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSI--------DFQITfqsGIARLMIREAFAEDSGRFT 971
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQVPGKENLImrpnhvrgNVVVT---NIGQLVIYNAQPQDAGLYT 77
                            90
                    ....*....|....*...
gi 1958765569   972 CSAVNEAGTVSTSCYLAV 989
Cdd:cd05765      78 CTARNSGGLLRANFPLSV 95
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4953-5038 3.72e-07

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 53.17  E-value: 3.72e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4953 KPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASdRYQIAfveGTASLEISRVDMNDAGNFTCRATNSVGSKDS 5032
Cdd:cd05725       2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEIL---DDHSLKIRKVTAGDMGSYTCVAENMVGKIEA 77

                    ....*.
gi 1958765569  5033 RGALIV 5038
Cdd:cd05725      78 SATLTV 83
fn3 pfam00041
Fibronectin type III domain;
27183-27268 3.73e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 3.73e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27183 GPPSTPWVSNVTRESITVGWHEPvSNGGSAVIGYHLEMKDRNSiLWQKANKMIIRTTH-FKVTTISAGLIYEFRVYAENA 27261
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNS-GEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1958765569 27262 AGIGKPS 27268
Cdd:pfam00041    79 GGEGPPS 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
3199-3288 3.73e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 53.16  E-value: 3.73e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQS-GKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHDGqeyTLLLIEAFPEDAAVYTCEAKNDY 3277
Cdd:cd20978       1 PKFIQKPEKNVVVKgGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDG---TLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  3278 GVATTSASLSV 3288
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7495-7565 3.76e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 53.56  E-value: 3.76e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  7495 GNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHiTFVRNL---ASLKIPSAEMNDKGLYSFEVENSVGKSSCT 7565
Cdd:cd05893      15 GMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHY-TIQRDLdgtCSLHTTASTLDDDGNYTIMAANPQGRISCT 87
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6833-6904 3.78e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 52.98  E-value: 3.78e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  6833 VEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAGRDS 6904
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
22670-22749 3.78e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 53.58  E-value: 3.78e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTT---RVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLN 22746
Cdd:cd20951      11 TVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSAS 90

                    ...
gi 1958765569 22747 VIV 22749
Cdd:cd20951      91 VVV 93
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
24829-24913 3.79e-07

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 53.34  E-value: 3.79e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24829 PFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSkdDFGKYSVTATNNAG-TATE 24907
Cdd:cd20958       6 PMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNGTLVIENVQRSS--DEGEYTCTARNQQGqSASR 83

                    ....*.
gi 1958765569 24908 NLSVIV 24913
Cdd:cd20958      84 SVFVKV 89
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5883-5973 3.81e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 53.41  E-value: 3.81e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5883 PPSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEEnDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNES 5962
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQY-AADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  5963 GVERCYAFLLV 5973
Cdd:cd20976      80 GQVSCSAWVTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23064-23145 3.86e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.28  E-value: 3.86e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23064 TVVVQAGESFKIDADIYGKPIPTTQWVKGDQE-LSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVN 23142
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  23143 VKV 23145
Cdd:smart00410    83 LTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7952-8039 3.87e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 53.27  E-value: 3.87e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSN----LQMSFVHhvaTLQILQTDQSHVGQYNCSAS 8027
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAhkmlVRENGRH---SLIIEPVTKRDAGIYTCIAR 77
                            90
                    ....*....|..
gi 1958765569  8028 NPLGTASSSAKL 8039
Cdd:cd05744      78 NRAGENSFNAEL 89
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8805-8884 3.88e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 52.97  E-value: 3.88e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8805 PLKVTVGDSASLQCQL-AGTPEIGVSWYKGDTKLRPTTTCKMHFKNN-VATLVFTQVDSNDSGEYICRAENSVGEVSSST 8882
Cdd:pfam00047     5 TVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84

                    ..
gi 1958765569  8883 FL 8884
Cdd:pfam00047    85 SL 86
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8048-8137 3.96e-07

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 53.23  E-value: 3.96e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVL--KVAKGDAGQYTCYASNV 8125
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLLiqNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  8126 AGKDSCSAQLGV 8137
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8047-8137 4.15e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 53.16  E-value: 4.15e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8047 PPFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRpgGNYKMTLVENtATLTVLKVAKGDAGQYTCYASNVA 8126
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ--GPMERATVED-GTLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  8127 GKDSCSAQLGV 8137
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5884-5963 4.19e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 53.16  E-value: 4.19e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSS-ATFQSTVAGSPPISITWLKDDQILEENdNVHISFEDSvaTLQVRSVDNGHSGRYTCQAKNES 5962
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQdVTLPCQVTGVPQPKITWLHNGKPLQGP-MERATVEDG--TLTIINVQPEDTGYYGCVATNEI 77

                    .
gi 1958765569  5963 G 5963
Cdd:cd20978      78 G 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8424-8511 4.25e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 53.19  E-value: 4.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8424 IVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTG---DSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|.
gi 1958765569  8501 GKDSCTVSIQV 8511
Cdd:cd20951      83 GEASSSASVVV 93
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
1040-1127 4.26e-07

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 52.88  E-value: 4.26e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1040 FISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPL-TTGYRYKVSYNKQtgecrLVISMTFADDAGEYTIVIRNKH 1118
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLlGKDERITTLENGS-----LQIKGAEKSDTGEYTCVALNLS 76

                    ....*....
gi 1958765569  1119 GETSASASL 1127
Cdd:cd20952      77 GEATWSAVL 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
16328-16420 4.29e-07

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 52.92  E-value: 4.29e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16328 AQDCLICKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKAMKDGIHdipedaqLETAENSSVIVIPECTRAHSGKYSITAKN 16407
Cdd:cd05894       1 AENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVR-------VESYKDLSSFVIEGAEREDEGVYTITVTN 73
                            90
                    ....*....|...
gi 1958765569 16408 KAGQKTANCRVKV 16420
Cdd:cd05894      74 PVGEDHASLFVKV 86
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
31440-31531 4.31e-07

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 53.18  E-value: 4.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGL-KYRVQEfkGGYHQLIIASVTDDDATVYQVRATN 31518
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAhKMLVRE--NGVHSLIIEPVTSRDAGIYTCIATN 78
                            90
                    ....*....|...
gi 1958765569 31519 QGGSVSGTASLEV 31531
Cdd:cd20990      79 RAGQNSFNLELVV 91
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8518-8607 4.35e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 53.18  E-value: 4.35e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLT--DNTCALTVNMLEDADAGDYTCIATNV 8595
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRdlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  8596 AGSDECSAPLTV 8607
Cdd:cd05893      81 QGRISCTGRLMV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
11644-11703 4.38e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.57  E-value: 4.38e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11644 VGSSAIFECLVS-PSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCV 11703
Cdd:pfam13927    15 EGETVTLTCEATgSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
7870-7947 4.39e-07

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 53.42  E-value: 4.39e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7870 GEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSAVLVIKE 7947
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4666-4747 4.43e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 52.97  E-value: 4.43e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4666 PPSFIKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEV 4745
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ..
gi 1958765569  4746 GK 4747
Cdd:cd20972      81 GS 82
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33079-33149 4.44e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 52.92  E-value: 4.44e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 33079 PRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTakyKSTFEISSVQASDEGNYSVVVEN 33149
Cdd:cd20957       8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILS---EDVLVIPSVKREDKGMYQCFVRN 75
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
4565-4661 4.48e-07

First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 53.36  E-value: 4.48e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4565 ATVAVREPPSFVKKVDPSYLMLPGESARLHCKLKGSpVIQVTWFKNNKELSESNTVRMSFANseaiLDITDVKVDDSGTY 4644
Cdd:cd04973       1 PTLPPEAPPTYQISEVESYSAHPGDLLQLRCRLRDD-VQSINWTKDGVQLGENNRTRITGEE----VQIKDAVPRDSGLY 75
                            90
                    ....*....|....*....
gi 1958765569  4645 SCEATNDAGSDS--CSTEV 4661
Cdd:cd04973      76 ACVTSSPSGSDTtyFSVNV 94
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
19818-19900 4.48e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 53.40  E-value: 4.48e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19818 TVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGvKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLKV 19897
Cdd:cd05730      14 TANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92

                    ...
gi 1958765569 19898 LDK 19900
Cdd:cd05730      93 FAK 95
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
33076-33162 4.50e-07

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 52.97  E-value: 4.50e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33076 LTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTakyKSTFEISSVQASDEGNYSVVVENTDGKQE 33155
Cdd:cd05723       1 LKKPSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVK---EHNLQVLGLVKSDEGFYQCIAENDVGNAQ 77

                    ....*..
gi 1958765569 33156 AQFTLTV 33162
Cdd:cd05723      78 ASAQLII 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23462-23542 4.51e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.89  E-value: 4.51e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  23462 KVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEI---RDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFV 23538
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  23539 TVRV 23542
Cdd:smart00410    82 TLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1818-1884 4.51e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 52.33  E-value: 4.51e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1818 ARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVR-YDGIHYLDIVDCKSYDTGEVKVTAENPEGVTEHK 1884
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRsELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3600-3660 4.51e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 52.33  E-value: 4.51e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  3600 VHGEPAPTVLWFKEDMPLYTNVcYTIIHNPDGSGTFIVNDPQRGDSGLYICKAENLWGTST 3660
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLPPSS-RDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7294-7381 4.55e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 53.19  E-value: 4.55e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSK---KFKVTSKNFDTSLHIFNLEAPDIGEYHCKATN 7370
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|.
gi 1958765569  7371 EVGSDTCACTV 7381
Cdd:cd20951      81 IHGEASSSASV 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
8707-8793 4.56e-07

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 53.28  E-value: 4.56e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8707 VKRLNDYSIEKGKPLILE-GTFSGTPPISVTWKKNG--VNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASG 8783
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLKcEATSENPSPRYRWFKDGkeLNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILG 82
                            90
                    ....*....|
gi 1958765569  8784 KDSCSAQILI 8793
Cdd:cd05750      83 KDTVTGNVTV 92
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
7011-7096 4.62e-07

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 53.24  E-value: 4.62e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQ--TDLSHSGQYSCSASNP 7088
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQLIIasVTDDDATVYQVRATNQ 81

                    ....*...
gi 1958765569  7089 LGTASSTA 7096
Cdd:cd20971      82 GGSVSGTA 89
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
24277-24524 4.63e-07

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 59.57  E-value: 4.63e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24277 AWTVVASEVVTNSLKVTKLLEGNEYIFRIMAV----NKYGVGE--PLESAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVC 24350
Cdd:COG4733     478 VWAFGPDELETQLFRVVSIEENEDGTYTITAVqhapEKYAAIDagAFDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVS 557
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24351 WNRPDSDggseiIGYIVEKRDRSGiRWIkcNKRRITDLRLRVTGLTeDHEYEFRVSAENAAGVGEPSPATVYYKAcdpVF 24430
Cdd:COG4733     558 WDAPAGA-----VAYEVEWRRDDG-NWV--SVPRTSGTSFEVPGIY-AGDYEVRVRAINALGVSSAWAASSETTV---TG 625
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24431 KPGPPTNVHIVDTTKN--SITLAWGKPIydgGSDILGYvvEICKADEEEWQIVT-PQTGLRVTRFEISKLIEHQEYKIRV 24507
Cdd:COG4733     626 KTAPPPAPTGLTATGGlgGITLSWSFPV---DADTLRT--EIRYSTTGDWASATvAQALYPGNTYTLAGLKAGQTYYYRA 700
                           250
                    ....*....|....*..
gi 1958765569 24508 CALNKVGLGEAASVPGT 24524
Cdd:COG4733     701 RAVDRSGNVSAWWVSGQ 717
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12804-12881 4.64e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.89  E-value: 4.64e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12804 EDQTVEEEATAVLECEVS-RENAKVKWFKNGTE-ILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAK----DFKTSC 12877
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATnssgSASSGT 81

                     ....
gi 1958765569  12878 NLNV 12881
Cdd:smart00410    82 TLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
32886-32975 4.71e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.88  E-value: 4.71e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32886 PRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIH-YTNTSGVLTLEILDCQTEDSGTYRAVCTNYK 32964
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569 32965 GEASDYATLDV 32975
Cdd:cd05744      81 GENSFNAELVV 91
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
31760-31959 4.75e-07

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 57.35  E-value: 4.75e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31760 YEKYMIAEDLGRGEFGIVHRcvetsskKTFMAKFVKVKGTDQ----------VLVKKEISILNIARHRNILYLHESFESM 31829
Cdd:cd14147       2 FQELRLEEVIGIGGFGKVYR-------GSWRGELVAVKAARQdpdedisvtaESVRQEARLFAMLAHPNIIALKAVCLEE 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31830 EELVMIFEFISGLDIFERIntSAFELNEREVVSYVRQVCEALEFLHSQNIG---HFDIRPENIIY------QTRKNSIIK 31900
Cdd:cd14147      75 PNLCLVMEYAAGGPLSRAL--AGRRVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLlqpienDDMEHKTLK 152
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31901 IIEFGQARQLKPGDNfrlLFTAPEY--YAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPF 31959
Cdd:cd14147     153 ITDFGLAREWHKTTQ---MSAAGTYawMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
4875-4942 4.78e-07

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 52.90  E-value: 4.78e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4875 TVSGTPELKPKWYKDGRPLVASKKYRISFKNN--IAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTV 4942
Cdd:cd05750      23 ATSENPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
28089-28154 4.79e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 52.94  E-value: 4.79e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 28089 IGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKteNKITLSIKNVKKENGGKYTVILDNAV 28154
Cdd:cd05856      18 VGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKK--KKWTLSLKNLKPEDSGKYTCHVSNRA 81
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
22659-22736 4.79e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.57  E-value: 4.79e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 22659 PPAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTN 22736
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
31765-32018 4.87e-07

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 57.69  E-value: 4.87e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVHRcveTSSKKTFMAKFVK----VKGTDQVlVKKEISIL-NIARHRNILYLHESFESMEELV-----M 31834
Cdd:cd06639      26 IIETIGKGTYGKVYK---VTNKKDGSLAAVKildpISDVDEE-IEAEYNILrSLPNHPNVVKFYGMFYKADQYVggqlwL 101
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31835 IFEFISGLDIFERINtSAFELNER---EVVSYV-RQVCEALEFLHSQNIGHFDIRPENIIYQTRKNsiIKIIEFGQARQL 31910
Cdd:cd06639     102 VLELCNGGSVTELVK-GLLKCGQRldeAMISYIlYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVSAQL 178
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31911 KPGDNFR-LLFTAPEYYAPEV----HQHDVVSSA-TDMWSLGTLVYVLLSGiNPFLAETN--QQMIENIMNAEYTF--DE 31980
Cdd:cd06639     179 TSARLRRnTSVGTPFWMAPEViaceQQYDYSYDArCDVWSLGITAIELADG-DPPLFDMHpvKALFKIPRNPPPTLlnPE 257
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1958765569 31981 EAFQEISleamDFIDRLLVKERKSRMTASEALKHPWLK 32018
Cdd:cd06639     258 KWCRGFS----HFISQCLIKDFEKRPSVTHLLEHPFIK 291
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6445-6536 4.93e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 52.97  E-value: 4.93e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6445 PPKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEvVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKND 6524
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKE-LQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  6525 GGVRENMASLTV 6536
Cdd:cd20972      80 VGSDTTSAEIFV 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
9677-9744 4.98e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.57  E-value: 4.98e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9677 QNIVVSEHQSATFECEVS-FDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIAR 9744
Cdd:pfam13927     9 SSVTVREGETVTLTCEATgSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
9297-9380 5.11e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.13  E-value: 5.11e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9297 QSIRVVEKTTATFIAKVGGDPIPNVKWTK-GKWRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGEIESN 9375
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRdGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*
gi 1958765569  9376 VNLQV 9380
Cdd:cd20974      88 AELLV 92
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
7111-7200 5.14e-07

Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 409440  Cd Length: 102  Bit Score: 53.51  E-value: 5.14e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7111 IKPVSIDVIAGESADFECHVTGAQPMRVT--WSKDNKEI---RPGGNYTITCVGNT-PHLRILKVGKGDSGQYTCQATND 7184
Cdd:cd05854       7 LAPSSADINQGENLTLQCHASHDPTMDLTftWSLDDFPIdldKPNGHYRRMEVKETiGDLVIVNAQLSHAGTYTCTAQTV 86
                            90
                    ....*....|....*.
gi 1958765569  7185 VGKDMCSAQLSVKEPP 7200
Cdd:cd05854      87 VDSASASATLVVRGPP 102
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
6445-6538 5.15e-07

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 53.42  E-value: 5.15e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6445 PPKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEvVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKND 6524
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQ-IQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENK 79
                            90
                    ....*....|....
gi 1958765569  6525 GGVRENMASLTVLE 6538
Cdd:cd05762      80 LGSRQAQVNLTVVD 93
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5416-5505 5.16e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.13  E-value: 5.16e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5416 TITEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQ--ELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDV 5493
Cdd:cd20974       2 VFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|..
gi 1958765569  5494 GRSSCKASINVL 5505
Cdd:cd20974      82 GQATSTAELLVL 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6353-6436 5.24e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.88  E-value: 5.24e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6353 PVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYK-IASKNFHASIHILNVDSTDIGEYHCKAQNEV 6431
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                    ....*
gi 1958765569  6432 GSDTC 6436
Cdd:cd05744      81 GENSF 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
25629-26046 5.25e-07

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 59.19  E-value: 5.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25629 VTLRASATLRLFVTIKGRPEPEVKWekaegilteraQIEVTSSYTMLV-IDNVTRFDSGRYNLTLENNSGSKTAFVNVRV 25707
Cdd:COG4733     455 VQSVAGRTLTVSTAYSETPEAGAVW-----------AFGPDELETQLFrVVSIEENEDGTYTITAVQHAPEKYAAIDAGA 523
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25708 LDSPS---APVNLTVREV--------KKDSVTLSWEPPlidggAKVTNYIVE-KRETTRKAYATITnncTKTTFKIENLQ 25775
Cdd:COG4733     524 FDDVPpqwPPVNVTTSESlsvvaqgtAVTTLTVSWDAP-----AGAVAYEVEwRRDDGNWVSVPRT---SGTSFEVPGIY 595
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25776 EGcSYYFRVLASNEYGIGLPAETTEPVKVSEPPLPPGRVTLVDVTRNT--ATIKWEKPEsdgGSKITGYVVEMQTKGSEK 25853
Cdd:COG4733     596 AG-DYEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTGLTATGGLggITLSWSFPV---DADTLRTEIRYSTTGDWA 671
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25854 WSTCTQ--VKTLEATISGLTAGEEYVFRVAAVNEKGR-SDPRQLGVPVVAKDIEIKPSVELPFNTFNVKANDQLKIDIPF 25930
Cdd:COG4733     672 SATVAQalYPGNTYTLAGLKAGQTYYYRARAVDRSGNvSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATV 751
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25931 KGRPQATVAW---KKDGQVLR-----------ETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIV 25996
Cdd:COG4733     752 AEVVAATVTDvtaQIDTAVLFagvataaaigaEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAAS 831
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25997 LDRPGPPGPIRIDEVSCDNVSISWTPPEYDGGCQISNYIVEKRETTSTTW 26046
Cdd:COG4733     832 TTRVAAAVVLAGVVVYGDAIIESGNTGDIVATGDIASAAAGAVATTVSGT 881
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13519-13598 5.27e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.89  E-value: 5.27e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13519 QDLVVDAGQPLTMVVPYDAYPKAEAEWFKEN-EPLSTK---TVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKAEGFI 13594
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESgrfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  13595 NLQV 13598
Cdd:smart00410    82 TLTV 85
THB pfam18362
Tri-helix bundle domain; This domain can be found in the myosin-binding motif (m-domain) ...
9414-9444 5.31e-07

Tri-helix bundle domain; This domain can be found in the myosin-binding motif (m-domain) region present in myosin-binding protein C (MyBP-C). MyBP-C is a sarcomeric assembly protein necessary for the regulation of sarcomere structure and function. The MyBP-C family of proteins consists mainly of modules with immunoglobulin (Ig) or fibronectin folds. This domain exhibits a three-helix bundle fold and there is a known actin-binding motif, LK(R/K)XK positioned in the third helix (alpha3), similar to that found in villin and related proteins.


Pssm-ID: 465725  Cd Length: 34  Bit Score: 51.20  E-value: 5.31e-07
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1958765569  9414 DIMELLKNVDPKEYEKYARMYGITDFRGLLQ 9444
Cdd:pfam18362     1 DVWEILSNAPPKDYEKIAFQYGITDLRGMLK 31
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
33075-33162 5.38e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 52.40  E-value: 5.38e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33075 ILTKPRSiTVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARhqvttakykstFEISSVQASDEGNYSVVVENTDG-K 33153
Cdd:pfam13895     3 VLTPSPT-VVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN-----------FFTLSVSAEDSGTYTCVARNGRGgK 70

                    ....*....
gi 1958765569 33154 QEAQFTLTV 33162
Cdd:pfam13895    71 VSNPVELTV 79
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7107-7197 5.41e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.13  E-value: 5.41e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIR----PGgnYTITCVGNTPHLRILKVGKGDSGQYTCQAT 7182
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIStstlPG--VQISFSDGRAKLSIPAVTKANSGRYSLTAT 78
                            90
                    ....*....|....*
gi 1958765569  7183 NDVGKDMCSAQLSVK 7197
Cdd:cd20974      79 NGSGQATSTAELLVL 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6635-6725 5.44e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 52.97  E-value: 5.44e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6635 PPSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVA 6714
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  6715 GSDECRALLTV 6725
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
1260-1337 5.44e-07

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 52.25  E-value: 5.44e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1260 EGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMdfLQDGraSLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYV 1337
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLV--LSSG--TLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33424-33505 5.46e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 52.92  E-value: 5.46e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33424 DTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKeefILEILKTETSDGGLYSCTVANSAGSVSSSCKL 33503
Cdd:cd20957      10 VQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQATAEL 86

                    ..
gi 1958765569 33504 TI 33505
Cdd:cd20957      87 KL 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5511-5600 5.50e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.88  E-value: 5.50e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAF-LEISQLEGTDSGTYTCSATNKA 5589
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  5590 GHSQCSGHLTV 5600
Cdd:cd05744      81 GENSFNAELVV 91
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4292-4381 5.55e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 52.79  E-value: 5.55e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIY-ESDKCSI-RSSNYISSLEILRTQVVDCGEYTCKASNE 4369
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIqRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  4370 YGSVSCTATLTV 4381
Cdd:cd05893      81 QGRISCTGRLMV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
15906-15993 5.60e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.57  E-value: 5.60e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15906 PPTIKlrlaVRGDTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKPTDALNITKEEVSRseakteLSIPKAVREDKG 15985
Cdd:pfam13927     1 KPVIT----VSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNST------LTISNVTRSDAG 70

                    ....*...
gi 1958765569 15986 TYTITASN 15993
Cdd:pfam13927    71 TYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
25906-25983 5.77e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.57  E-value: 5.77e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 25906 KPSVELPFNTFNVKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSN 25983
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
24824-24903 5.80e-07

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 52.86  E-value: 5.80e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTI-LHIKESSKDDFGKYSVTATNNA 24902
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCrLRILAAERGDAGFYTCKAVNEY 80

                    .
gi 1958765569 24903 G 24903
Cdd:cd20975      81 G 81
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
18033-18099 5.88e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.18  E-value: 5.88e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 18033 VVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSN 18099
Cdd:pfam13927    12 TVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
31855-31959 5.93e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 57.71  E-value: 5.93e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31855 LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQL-------KPGDNfRLLFtapEYYA 31927
Cdd:cd14207     177 LTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLS--ENNVVKICDFGLARDIyknpdyvRKGDA-RLPL---KWMA 250
                            90       100       110
                    ....*....|....*....|....*....|...
gi 1958765569 31928 PEVHQHDVVSSATDMWSLGTLVYVLLS-GINPF 31959
Cdd:cd14207     251 PESIFDKIYSTKSDVWSYGVLLWEIFSlGASPY 283
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
27397-27474 5.94e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 52.97  E-value: 5.94e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 27397 RAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRVQI 27474
Cdd:cd20972      14 AEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
18040-18107 6.00e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 51.95  E-value: 6.00e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 18040 VRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVA 18107
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3035-3091 6.00e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 51.95  E-value: 6.00e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  3035 AMFECEVS-EPDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVA 3091
Cdd:cd00096       1 VTLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVA 58
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
6918-7001 6.11e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 52.40  E-value: 6.11e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6918 VTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEyrtYFTNNVAtlvfnkvgINDSGEYTCVAENSIGTAA 6997
Cdd:pfam13895     3 VLTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN---FFTLSVS--------AEDSGTYTCVARNGRGGKV 71

                    ....
gi 1958765569  6998 SKTV 7001
Cdd:pfam13895    72 SNPV 75
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1258-1337 6.12e-07

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 52.80  E-value: 6.12e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1258 ILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYV 1337
Cdd:cd20990      12 VQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVV 91
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8163-8218 6.15e-07

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 52.18  E-value: 6.15e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8163 CKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAIlemHNLSVEDSGDYTCEARN 8218
Cdd:cd05746       5 CSAQGDPEPTITWNKDGVQVTESGKFHISPEGYLAI---RDVGVADQGRYECVARN 57
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
8051-8130 6.16e-07

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 53.12  E-value: 6.16e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8051 DLKPVSVDLALGESGSFKCHVTGTAPIK-ITWAKDNREIRPGGNYKMTLVEN---TATLTVLKVAKGDAGQYTCYASNVA 8126
Cdd:cd05865       4 DIVPSQGEISVGESKFFLCQVAGEAKDKdISWFSPNGEKLTPNQQRISVVRNddySSTLTIYNANIDDAGIYKCVVSNED 83

                    ....
gi 1958765569  8127 GKDS 8130
Cdd:cd05865      84 EGES 87
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
15922-16006 6.31e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 52.78  E-value: 6.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15922 VKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKPTDALNITkeevsrseaKTELSIPKAVREDKGTYTITASNRLGSVFRN 16001
Cdd:cd20978      13 VKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVE---------DGTLTIINVQPEDTGYYGCVATNEIGDIYTE 83

                    ....*
gi 1958765569 16002 VHVEV 16006
Cdd:cd20978      84 TLLHV 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
6-97 6.31e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 52.78  E-value: 6.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQS-VVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTstlPGVQISFSDGraRLMIPAVTKANSGRYSLRATN 84
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG---PMERATVEDG--TLTIINVQPEDTGYYGCVATN 75
                            90
                    ....*....|...
gi 1958765569    85 GSGQATSTAELLV 97
Cdd:cd20978      76 EIGDIYTETLLHV 88
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
4581-4650 6.32e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 52.58  E-value: 6.32e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  4581 PSYLMLPGESARLHCKLK-GSPVIQVTWFKNNKELSESNTVRMSFANSEAI-LDITDVKVDDSGTYSCEATN 4650
Cdd:pfam00047     4 PTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSsLLISNVTKEDAGTYTCVVNN 75
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8237-8311 6.42e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 52.72  E-value: 6.42e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8237 FRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSG----KKYKIMSENLLtsihILNVDTADIGEYQCKATN 8311
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASvadmSKYRILADGLL----INKVTQDDTGEYTCRAYQ 76
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
31756-32017 6.46e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 57.79  E-value: 6.46e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31756 TKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKK---EISILNIARHRNILYL------HESF 31826
Cdd:cd07874      12 TFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRayrELVLMKCVNHKNIISLlnvftpQKSL 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31827 ESMEELVMIFEFISGlDIFERINtsaFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQ 31906
Cdd:cd07874      92 EEFQDVYLVMELMDA-NLCQVIQ---MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIV--VKSDCTLKILDFGL 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31907 ARqlKPGDNFRLL-FTAPEYY-APEVHQHDVVSSATDMWSLGTLV------YVLLSGIN----------------PFLAE 31962
Cdd:cd07874     166 AR--TAGTSFMMTpYVVTRYYrAPEVILGMGYKENVDIWSVGCIMgemvrhKILFPGRDyidqwnkvieqlgtpcPEFMK 243
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31963 TNQQMIENIMN-----AEYTF-----------DEEAFQEISLEAMDFIDRLLVKERKSRMTASEALKHPWL 32017
Cdd:cd07874     244 KLQPTVRNYVEnrpkyAGLTFpklfpdslfpaDSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQHPYI 314
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
9000-9080 6.48e-07

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409398  Cd Length: 101  Bit Score: 52.88  E-value: 6.48e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9000 AVVGESADLECHVTGTQPIKVTWAKDNREIRSGGN--YQISYLENS----AHLTIVKVDKGDSGQYTCYAINEVGKDSCT 9073
Cdd:cd05735      15 ATKGQKKEMSCTAHGEKPIIVRWEKEDTIINPSEMsrYLVTTKEVGdeviSTLQILPTVREDSGFFSCHAINSYGEDRGI 94

                    ....*..
gi 1958765569  9074 AQLNIKE 9080
Cdd:cd05735      95 IQLTVQE 101
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8327-8418 6.48e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 52.59  E-value: 6.48e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8327 PPQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIvRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKND 8406
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKEL-QNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  8407 AGVQECYATLSV 8418
Cdd:cd20972      80 VGSDTTSAEIFV 91
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
15906-16007 6.49e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 53.01  E-value: 6.49e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15906 PPTIKLRLAVRGDTIKVkaGEPVNIPADVTGLPMPKIEWSKNEKVIEKptdalniTKEEVSRSEAKTELSIPKAVREDKG 15985
Cdd:cd05730       1 PPTIRARQSEVNATANL--GQSVTLACDADGFPEPTMTWTKDGEPIES-------GEEKYSFNEDGSEMTILDVDKLDEA 71
                            90       100
                    ....*....|....*....|..
gi 1958765569 15986 TYTITASNRLGSVFRNVHVEVY 16007
Cdd:cd05730      72 EYTCIAENKAGEQEAEIHLKVF 93
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
8522-8607 6.49e-07

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 52.78  E-value: 6.49e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8522 RKLKETNGLSGSSVVMECKVFGSPPISVLWLHDG----NAISSGRkyQTTLTDNTcaLTVNMLEDADAGDYTCIATNVAG 8597
Cdd:cd20969       7 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRkhlvSAKSNGR--LTVFPDGT--LEVRYAQVQDNGTYLCIAANAGG 82
                            90
                    ....*....|
gi 1958765569  8598 SDECSAPLTV 8607
Cdd:cd20969      83 NDSMPAHLHV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
29966-30046 6.51e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 52.74  E-value: 6.51e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29966 KTVIIRAGASLRLMVSVSGRPSPVITWSKKG--IDLAN--RAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSAT 30041
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*
gi 1958765569 30042 VLVKV 30046
Cdd:cd20974      88 AELLV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32101-32170 6.54e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.51  E-value: 6.54e-07
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  32101 CKIENYDqSTQVTWYF-GVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 32170
Cdd:smart00410    16 CEASGSP-PPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8519-8607 6.68e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 52.72  E-value: 6.68e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8519 SFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAGS 8598
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                    ....*....
gi 1958765569  8599 DECSAPLTV 8607
Cdd:cd20949      81 ASDMQERTV 89
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
1249-1337 6.70e-07

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 52.85  E-value: 6.70e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRG-ERYQMdfLQD--GRASLRIPVVLPEDEGIYTAFASNI 1325
Cdd:cd05892       3 FIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNtDRISL--YQDncGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  1326 KGNAICSGKLYV 1337
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
24824-24913 6.76e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 52.39  E-value: 6.76e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSF-KLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPL-RQTTRVNVEEtatsTILHIKESSKDDFGKYSVTATNN 24901
Cdd:cd20978       1 PKFiQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLqGPMERATVED----GTLTIINVQPEDTGYYGCVATNE 76
                            90
                    ....*....|..
gi 1958765569 24902 AGTATENLSVIV 24913
Cdd:cd20978      77 IGDIYTETLLHV 88
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7491-7570 6.80e-07

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 52.51  E-value: 6.80e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7491 TVTTGNPFTLEC-VVAGTPELSAKWLKDGRELSSGSRHHITFVRNLAS--LKIPSAEMNDKGLYSFEVENSVGKSSCTVS 7567
Cdd:cd05750      10 TVQEGSKLVLKCeATSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNseLQINKAKLEDSGEYTCVVENILGKDTVTGN 89

                    ...
gi 1958765569  7568 VHV 7570
Cdd:cd05750      90 VTV 92
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
33892-33977 6.81e-07

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 52.67  E-value: 6.81e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQ--QGRFHIENTDDLTTLIIMDVQKQDGGLYTLSL 33969
Cdd:cd05869       3 PKITYVENQTAMELEEQITLTCEASGDPIPSITWRTSTRNISSEEKtlDGHIVVRSHARVSSLTLKYIQYTDAGEYLCTA 82

                    ....*...
gi 1958765569 33970 GNEFGSDS 33977
Cdd:cd05869      83 SNTIGQDS 90
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
33425-33505 6.88e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 52.72  E-value: 6.88e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33425 TTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSCKLT 33504
Cdd:cd20949       9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQERT 88

                    .
gi 1958765569 33505 I 33505
Cdd:cd20949      89 V 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
18090-18425 6.93e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 58.48  E-value: 6.93e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18090 TGEYQLTVSNAAGTKTVAVHLTVLDVPGPPTGPINILDVTPEYMTISWQPPKDDGGSPVINYIVEKQDTRKGTWGVVSAG 18169
Cdd:COG3401      14 AASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATG 93
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18170 SSKLklkvphlQKGCEYVFRVKAENKMGVGPPLDSIPTVAKHKFSPPSPPGKPVVTDitenaaTVSWTLPKSDGGSPITG 18249
Cdd:COG3401      94 LTTL-------TGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYAL------GAGLYGVDGANASGTTA 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18250 YYVERREITGKWVRVNKTPIADLKFRVT---------GLYEGNTYEFRVFAENLAGLSNPSPSsdpIKACRPIKPPGPPI 18320
Cdd:COG3401     161 SSVAGAGVVVSPDTSATAAVATTSLTVTsttlvdgggDIEPGTTYYYRVAATDTGGESAPSNE---VSVTTPTTPPSAPT 237
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18321 NPKLKDKTKESADLVWTKPLSDGgspILGYVVECQKPGTTQWDRINKdelIRQCAFRVPGLIEGNEYRFRIRAANIVGEG 18400
Cdd:COG3401     238 GLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGNE 311
                           330       340
                    ....*....|....*....|....*
gi 1958765569 18401 EPRELAESVIAKDILHPPEVELDVT 18425
Cdd:COG3401     312 SAPSNVVSVTTDLTPPAAPSGLTAT 336
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7404-7472 6.94e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 51.95  E-value: 6.94e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7404 VELQAVVEGFQPISVVWLKDkGEVIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKNDAGMRECS 7472
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKN-GKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
4388-4477 7.04e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 52.62  E-value: 7.04e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4388 TFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCR----ITDADnkhSLELSNLTVQDRGVYSCKASN 4463
Cdd:cd05763       1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARERrmhvMPEDD---VFFIVDVKIEDTGVYSCTAQN 77
                            90
                    ....*....|....
gi 1958765569  4464 KFGADICQAELTII 4477
Cdd:cd05763      78 SAGSISANATLTVL 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
8808-8886 7.08e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 52.51  E-value: 7.08e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8808 VTVGDSASLQCQLAGTPEIGVSWYKgDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSV-GEVSSSTFLTV 8886
Cdd:cd20970      14 AREGENATFMCRAEGSPEPEISWTR-NGNLIIEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGVpGSVEKRITLQV 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8997-9076 7.09e-07

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 52.40  E-value: 7.09e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8997 PVD--AVVGESADLECHVTGTQPIKVTWAKDNREIRSGgNYQIsyLENSAhLTIVKVDKGDSGQYTCYAINEVGKDSCTA 9074
Cdd:cd05725       4 PQNqvVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEI--LDDHS-LKIRKVTAGDMGSYTCVAENMVGKIEASA 79

                    ..
gi 1958765569  9075 QL 9076
Cdd:cd05725      80 TL 81
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
3577-3667 7.09e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.50  E-value: 7.09e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIIHNPDGSGTFIVNDPQRGDSGLYICKAENLW 3656
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  3657 GTSTCTAELLV 3667
Cdd:cd05744      81 GENSFNAELVV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5322-5411 7.09e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.50  E-value: 7.09e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5322 PSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTF-ENNVASLYLSGIEVKHDGKYVCQAKNDA 5400
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVrENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  5401 GIQRCSALLSV 5411
Cdd:cd05744      81 GENSFNAELVV 91
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5907-5963 7.14e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 52.21  E-value: 7.14e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5907 VAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESG 5963
Cdd:cd05748      16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG 72
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
9186-9271 7.17e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 52.58  E-value: 7.17e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9186 QHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSF-ASGTAVLELKDTAKADSGDYVCKASNVAGSDT 9264
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569  9265 SKCKVTI 9271
Cdd:cd20973      82 CSAELTV 88
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
24825-24914 7.25e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 52.62  E-value: 7.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24825 SF-KLPFNTySVQAGEDLKIEIPVIGRPRPKISWVKDGE---PLRQTTRVNVeeTATSTILHIKESSKDDFGKYSVTATN 24900
Cdd:cd05763       1 SFtKTPHDI-TIRAGSTARLECAATGHPTPQIAWQKDGGtdfPAARERRMHV--MPEDDVFFIVDVKIEDTGVYSCTAQN 77
                            90
                    ....*....|....
gi 1958765569 24901 NAGTATENLSVIVL 24914
Cdd:cd05763      78 SAGSISANATLTVL 91
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7856-7943 7.32e-07

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 52.46  E-value: 7.32e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVA--SLVINKVDHSDVGEYTCKAENS 7933
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGriCLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|
gi 1958765569  7934 VGAVASSAVL 7943
Cdd:cd05892      81 AGVVSCNARL 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
6550-6622 7.39e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 52.20  E-value: 7.39e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6550 TVTVGETCSLECKV-AGTPELSVEWYKDGKLLTSSQKHKFSFYNK-ISSLKILSVEKEDAGTYTFQVQNNVGKSS 6622
Cdd:pfam00047     7 TVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8518-8608 7.71e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.42  E-value: 7.71e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISS---GRKYQTTLTDNTCALTVNMLEDADAGDYTCIATN 8594
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  8595 VAGSDECSAPLTVR 8608
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7201-7283 7.81e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 52.33  E-value: 7.81e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7201 KFIKKLDTSKVaKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVG 7280
Cdd:cd20949       1 TFTENAYVTTV-KEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS 79

                    ...
gi 1958765569  7281 HAS 7283
Cdd:cd20949      80 IAS 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
12795-12871 7.81e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.18  E-value: 7.81e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 12795 PPVeFTKPLEDQTVEEEATAVLECEVSREN-AKVKWFKNGTEILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAK 12871
Cdd:pfam13927     1 KPV-ITVSPSSVTVREGETVTLTCEATGSPpPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2758-2839 7.90e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.50  E-value: 7.90e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2758 IKKPKDVTALENATVAFEVSVSHDTVP-VKWFHKNVEIKPSDKH-RLVSERKVHKLMLQNISPSDAGEYTAVV----GQL 2831
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPdLFWQLNGKPVRPDSAHkMLVRENGRHSLIIEPVTKRDAGIYTCIArnraGEN 83

                    ....*...
gi 1958765569  2832 ECKAKLFV 2839
Cdd:cd05744      84 SFNAELVV 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
7483-7570 7.96e-07

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 52.11  E-value: 7.96e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7483 IVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELsSGSRHHITFVRNlASLKIPSAEMNDKGLYSFEVENSVGKS 7562
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPL-LGKDERITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569  7563 SCTVSVHV 7570
Cdd:cd20952      80 TWSAVLDV 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9599-9653 8.20e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 51.56  E-value: 8.20e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  9599 TMTCQFS-VPNVKSEWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTCK 9653
Cdd:cd00096       2 TLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCV 57
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
9297-9380 8.22e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 52.19  E-value: 8.22e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9297 QSIR---VVEKTTATFIAKVGGDPIPNVKWTKgKWRQLNQGGRILIHQKGD-ESKLEIRDTTKTDSGLYRCVAFNKHGEI 9372
Cdd:cd20973       2 QTLRdkeVVEGSAARFDCKVEGYPDPEVKWMK-DDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  9373 ESNVNLQV 9380
Cdd:cd20973      81 TCSAELTV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
1265-1324 8.22e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 52.15  E-value: 8.22e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1265 TFHCKMSGYPLPKIAWYKDGKRIRRGERYQMdflqDGRASLRIPVVLPEDEGIYTAFASN 1324
Cdd:cd20957      20 VFNCSVTGNPIHTVLWMKDGKPLGHSSRVQI----LSEDVLVIPSVKREDKGMYQCFVRN 75
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
21587-21667 8.28e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 52.51  E-value: 8.28e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWK-KGDQILKQTQRVNV-ENTATSTILNINecvRSDSGAYPLTAKNTV-GEVGDVI 21663
Cdd:cd20970      12 VTAREGENATFMCRAEGSPEPEISWTrNGNLIIEFNTRYIVrENGTTLTIRNIR---RSDMGIYLCIASNGVpGSVEKRI 88

                    ....
gi 1958765569 21664 TIQV 21667
Cdd:cd20970      89 TLQV 92
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
33892-33982 8.28e-07

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 52.41  E-value: 8.28e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENtdDLTTLIIMDVQKQDGGLYTLSLGN 33971
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVREN--GVHSLIIEPVTSRDAGIYTCIATN 78
                            90
                    ....*....|.
gi 1958765569 33972 EFGSDSATVNI 33982
Cdd:cd20990      79 RAGQNSFNLEL 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4387-4476 8.31e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 52.36  E-value: 8.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDG--TALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNK 4464
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  4465 FGADICQAELTI 4476
Cdd:cd20974      81 SGQATSTAELLV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6824-6909 8.42e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.42  E-value: 8.42e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6824 FVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSE---RCNIVTTEKTCILEILTSTKGDAGHYSCEIENEA 6900
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82

                    ....*....
gi 1958765569  6901 GRDSCDALV 6909
Cdd:cd20951      83 GEASSSASV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
22660-22749 8.45e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.50  E-value: 8.45e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22660 PAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSL-LTIKEACREDVGHYTVKLTNSA 22738
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569 22739 GEATETLNVIV 22749
Cdd:cd05744      81 GENSFNAELVV 91
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
3198-3288 8.48e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 52.25  E-value: 8.48e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3198 PPQVLQELQPVTVQSGKP-ARFCAViAGRPQPKISWYKEEQLLSTGFKcKFLHDGQEYTLLLIEAFPEDAAVYTCEAKND 3276
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDfVAQCSA-RGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  3277 YGVATTSASLSV 3288
Cdd:cd20976      79 AGQVSCSAWVTV 90
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
3484-3550 8.61e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 52.41  E-value: 8.61e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3484 VVGCPKPKIQWFFNGMLLTPSADYKFV---FDGNNhSLIILFTRFQDEGEYTCMASNEYGRAVCSAHLKV 3550
Cdd:cd05893      24 VAGNPKPKIYWFKDGKQISPKSDHYTIqrdLDGTC-SLHTTASTLDDDGNYTIMAANPQGRISCTGRLMV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
20917-20976 8.61e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 51.56  E-value: 8.61e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20917 GKPLPKSSWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEH 20976
Cdd:cd00096       9 GNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8893-8981 8.67e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.42  E-value: 8.67e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPL---KDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTN 8969
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|..
gi 1958765569  8970 PIGSASSSAKLI 8981
Cdd:cd20951      81 IHGEASSSASVV 92
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
913-989 8.71e-07

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 51.86  E-value: 8.71e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   913 EGESVTLECHISGYPSPKVTWYREDYQIesSIDFQ-ITFQSGIARlmIREAFAEDSGRFTCSAVNEAGTVSTSCYLAV 989
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQL--SVDRRhLVLSSGTLR--ISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
I-set pfam07679
Immunoglobulin I-set domain;
2668-2752 8.72e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.26  E-value: 8.72e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2668 KIKKTLRNLTVTETQDAIFSVELT-HPDVKgVQWIKNGVVLDSNDKYEISVKGTLYSLKIKNCAMADESVYGFK----LG 2742
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgTPDPE-VSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVatnsAG 80
                            90
                    ....*....|
gi 1958765569  2743 RLGASARLHV 2752
Cdd:pfam07679    81 EAEASAELTV 90
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
4588-4653 8.78e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 52.51  E-value: 8.78e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTvRMSFANSEAILDITDVKVDDSGTYSCEATNDAG 4653
Cdd:cd20970      17 GENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTTLTIRNIRRSDMGIYLCIASNGVP 81
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4578-4661 8.89e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 52.15  E-value: 8.89e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4578 KVDPSYLMLP-GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSfanSEAILDITDVKVDDSGTYSCEATNDAGSDS 4656
Cdd:cd20957       5 TIDPPVQTVDfGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQIL---SEDVLVIPSVKREDKGMYQCFVRNDGDSAQ 81

                    ....*
gi 1958765569  4657 CSTEV 4661
Cdd:cd20957      82 ATAEL 86
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
8517-8607 9.04e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 52.24  E-value: 9.04e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8517 PPSFTRKLKETNGLS--GSSVVMECKVFGSPPISVLWLHDGNAISSGR-KYqtTLTDNTCALTVNMLEDADAGDYTCIAT 8593
Cdd:cd05730       1 PPTIRARQSEVNATAnlGQSVTLACDADGFPEPTMTWTKDGEPIESGEeKY--SFNEDGSEMTILDVDKLDEAEYTCIAE 78
                            90
                    ....*....|....
gi 1958765569  8594 NVAGSDECSAPLTV 8607
Cdd:cd05730      79 NKAGEQEAEIHLKV 92
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7856-7945 9.04e-07

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 52.41  E-value: 9.04e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNN-VASLVINKVDHSDVGEYTCKAENSV 7934
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENgVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  7935 GAVASSAVLVI 7945
Cdd:cd20990      81 GQNSFNLELVV 91
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
31769-31954 9.05e-07

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 56.14  E-value: 9.05e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIV----HRCVETSskktfmAKFVKVKGTDQVLVKkEISILNIARHRNILYLHESF-ESMEELVMIFEFISGLD 31843
Cdd:cd05082      14 IGKGEFGDVmlgdYRGNKVA------VKCIKNDATAQAFLA-EASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKGS 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAFE-LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKPGDNFRLLftA 31922
Cdd:cd05082      87 LVDYLRSRGRSvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVL--VSEDNVAKVSDFGLTKEASSTQDTGKL--P 162
                           170       180       190
                    ....*....|....*....|....*....|..
gi 1958765569 31923 PEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS 31954
Cdd:cd05082     163 VKWTAPEALREKKFSTKSDVWSFGILLWEIYS 194
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
1530-1607 9.12e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 52.17  E-value: 9.12e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1530 GSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPririEGTKGEAALKIDSTISQDSAWYTATAINKAGRDTTRCKVNI 1607
Cdd:cd05856      19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPEIG----ENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7577-7666 9.12e-07

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 52.18  E-value: 9.12e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSaPI-SVGWFLDGNEIISSPKcQPSFADNvcTLTLSSLEP-SDTGAYTCVAANV 7654
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGY-PIsSITWEKDGRRLPLNHR-QRVFPNG--TLVIENVQRsSDEGEYTCTARNQ 76
                            90
                    ....*....|...
gi 1958765569  7655 AGQ-DESSALLTV 7666
Cdd:cd20958      77 QGQsASRSVFVKV 89
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
907-989 9.25e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 52.24  E-value: 9.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   907 KNVTVVEGESVTLECHISGYPSPKVTWyredyQIESSIDF------QITFQSGIARLMIREAFAEDSGRFTCSAVNEAGT 980
Cdd:cd05763       7 HDITIRAGSTARLECAATGHPTPQIAW-----QKDGGTDFpaarerRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81

                    ....*....
gi 1958765569   981 VSTSCYLAV 989
Cdd:cd05763      82 ISANATLTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9671-9757 9.28e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.42  E-value: 9.28e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9671 QFTKRIQNIVVSEHQSATFECEVS-FDDAIVTWYKGPTELTESQ---KYNFRNDGRCHYMTIHNVTPDDEGVYSVIARlE 9746
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAK-N 80
                            90
                    ....*....|.
gi 1958765569  9747 PRGEARSTAEL 9757
Cdd:cd20951      81 IHGEASSSASV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
18443-18507 9.31e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 51.56  E-value: 9.31e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 18443 RVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
29966-30040 9.35e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 52.36  E-value: 9.35e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 29966 KTVIIRAGASLRLMVSVSGRPSPVITWSKKG--IDLANRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSA 30040
Cdd:cd05747      11 RSLTVSEGESARFSCDVDGEPAPTVTWMREGqiIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEA 87
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
31440-31531 9.36e-07

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 52.09  E-value: 9.36e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYrVQEFKGGYHQLIIASVTDDDATVYQVRATNQ 31519
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRF-AEEAEGGLCRLRILAAERGDAGFYTCKAVNE 79
                            90
                    ....*....|..
gi 1958765569 31520 GGSVSGTASLEV 31531
Cdd:cd20975      80 YGARQCEARLEV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13070-13148 9.48e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 9.48e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13070 PQNLEILEGEKAEFVCTIS-KESFEVQWKRDDQT-LESGDKYDIIADGKKRVLVVKDATLQDMGTYVVMV----GAARAA 13143
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSG 80

                     ....*
gi 1958765569  13144 AHLTV 13148
Cdd:smart00410    81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
19128-19207 9.48e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 9.48e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVRKG--QVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNV 19205
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  19206 KV 19207
Cdd:smart00410    84 TV 85
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
1516-1609 9.74e-07

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 52.09  E-value: 9.74e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYpRIRIEGTKGEAALKIDSTISQDSAWYTATAINK 1595
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQR-RFAEEAEGGLCRLRILAAERGDAGFYTCKAVNE 79
                            90
                    ....*....|....
gi 1958765569  1596 AGrdTTRCKVNIEV 1609
Cdd:cd20975      80 YG--ARQCEARLEV 91
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
900-989 9.74e-07

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 52.09  E-value: 9.74e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIE-SSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRpDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd20975      81 GARQCEARLEV 91
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
31761-31968 9.83e-07

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 56.59  E-value: 9.83e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTfMAKFVKvKGTDQV-LVKKEISILNIARHRNILYLHESFESMEELVMIFEFI 31839
Cdd:cd05072       7 ESIKLVKKLGAGQFGEVWMGYYNNSTKV-AVKTLK-PGTMSVqAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYM 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31840 ---SGLDIFERINTSAFELNEreVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLKpgDNf 31916
Cdd:cd05072      85 akgSLLDFLKSDEGGKVLLPK--LIDFSAQIAEGMAYIERKNYIHRDLRAANVL--VSESLMCKIADFGLARVIE--DN- 157
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31917 rlLFTAPE-------YYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMI 31968
Cdd:cd05072     158 --EYTAREgakfpikWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVM 215
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8916-8981 9.85e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 51.82  E-value: 9.85e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8916 VSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPIGSASSSAKLI 8981
Cdd:cd05748      16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6073-6162 9.87e-07

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 52.41  E-value: 9.87e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCH--ENTVSLEVSNLELEDTANYTCKVSNV 6150
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRdlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  6151 AGDNACSGILTV 6162
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
33705-33787 9.89e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 52.19  E-value: 9.89e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33705 RSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRN-MYTLEIRNASVSDSGKYTVKAKNFRGQCSATA 33783
Cdd:cd20973       5 RDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSA 84

                    ....
gi 1958765569 33784 SLTV 33787
Cdd:cd20973      85 ELTV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4672-4745 9.90e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 52.15  E-value: 9.90e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4672 TLEPAH-IVR-GANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTfvfLEITSFNSADIGDYECVVANEV 4745
Cdd:cd20957       5 TIDPPVqTVDfGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDV---LVIPSVKREDKGMYQCFVRNDG 77
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8054-8137 9.97e-07

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 52.11  E-value: 9.97e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8054 PVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIrPGGNYKMTLVENtATLTVLKVAKGDAGQYTCYASNVAGKDSCSA 8133
Cdd:cd20952       6 PQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPL-LGKDERITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEATWSA 83

                    ....
gi 1958765569  8134 QLGV 8137
Cdd:cd20952      84 VLDV 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
3019-3091 9.97e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 51.80  E-value: 9.97e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  3019 EFRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVA 3091
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATgSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
33699-33788 1.00e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 52.24  E-value: 1.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33699 SFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKN---NLPISISSNISVSRSRNMYTleIRNASVSDSGKYTVKAKNF 33775
Cdd:cd05763       1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDggtDFPAARERRMHVMPEDDVFF--IVDVKIEDTGVYSCTAQNS 78
                            90
                    ....*....|...
gi 1958765569 33776 RGQCSATASLTVL 33788
Cdd:cd05763      79 AGSISANATLTVL 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4303-4381 1.01e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 52.01  E-value: 1.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4303 VALGHLAKFTCEIQG--APNVRfqWFKAGREIYESdKCSIRSSNyisSLEILRTQVVDCGEYTCKASNEYGSVSCTATLT 4380
Cdd:cd05725       9 VLVDDSAEFQCEVGGdpVPTVR--WRKEDGELPKG-RYEILDDH---SLKIRKVTAGDMGSYTCVAENMVGKIEASATLT 82

                    .
gi 1958765569  4381 V 4381
Cdd:cd05725      83 V 83
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5604-5693 1.01e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 52.01  E-value: 1.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5604 PYFVEKPQSQ-DVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELfsaKAADSGTYICQLSNDV 5682
Cdd:cd20978       1 PKFIQKPEKNvVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIINV---QPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  5683 GTTSSKATIFV 5693
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6548-6629 1.02e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 52.01  E-value: 1.02e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6548 SMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSfynkISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVV 6627
Cdd:cd05725       6 NQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILD----DHSLKIRKVTAGDMGSYTCVAENMVGKIEASATL 81

                    ..
gi 1958765569  6628 DV 6629
Cdd:cd05725      82 TV 83
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
20508-20582 1.02e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 52.36  E-value: 1.02e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 20508 ENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSI 20582
Cdd:cd05747      17 EGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTL 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4480-4570 1.02e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.04  E-value: 1.02e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQKL---PAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASN 4556
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  4557 EAGSSSSSATVAVR 4570
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6728-6818 1.03e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 52.20  E-value: 1.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6728 PPSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFEDTVAEL---ELFNIDvsqSGEYTCVVS 6804
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLiiaEAFEED---TGRYSCLAT 77
                            90
                    ....*....|....
gi 1958765569  6805 NNAGQASCTTRLFV 6818
Cdd:cd20972      78 NSVGSDTTSAEIFV 91
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
33606-33688 1.03e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 51.86  E-value: 1.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33606 KALSTQMNITSGQRVTLKANIAGA-TDVKWVLNGTELSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCIGktsqGVVKC 33684
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELADPdAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA----GGEKC 76

                    ....
gi 1958765569 33685 QFDL 33688
Cdd:cd20967      77 SFEL 80
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
8514-8609 1.04e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 52.26  E-value: 1.04e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8514 RIIPPSFTRKLKETNGLsgssvvmECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIAT 8593
Cdd:cd05736       4 RVYPEFQAKEPGVEASL-------RCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAK 76
                            90
                    ....*....|....*.
gi 1958765569  8594 NVAGSDECSAPLTVRE 8609
Cdd:cd05736      77 NEGGVDEDISSLFVED 92
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
13078-13148 1.04e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 51.86  E-value: 1.04e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 13078 GEKAEFVCTISKESFEVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVVMVGAARAAAHLTV 13148
Cdd:cd20967      12 GHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
17727-17805 1.06e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 51.80  E-value: 1.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17727 PPELILDANmarEQHIKVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDVTPVG--SKLEIRNAAHEDGGIYSLTVE 17804
Cdd:pfam13927     1 KPVITVSPS---SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGsnSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 17805 N 17805
Cdd:pfam13927    78 N 78
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
7204-7290 1.07e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 51.86  E-value: 1.07e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7204 KKLDTSKVAKQGESIQLECKISGsPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAhngvGHAS 7283
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA----GGEK 75

                    ....*..
gi 1958765569  7284 CSTALKV 7290
Cdd:cd20967      76 CSFELFV 82
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
33422-33505 1.07e-06

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 51.83  E-value: 1.07e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33422 LRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKeefiLEILKTETSDGGLYSCTVANSAGSVSSSC 33501
Cdd:cd05728       6 ISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTIYASA 81

                    ....
gi 1958765569 33502 KLTI 33505
Cdd:cd05728      82 ELAV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
19817-19897 1.07e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.07e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIkQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:cd20976      11 LEAVEGQDFVAQCSARGKPVPRITWIRNAQPL-QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVT 89

                    .
gi 1958765569 19897 V 19897
Cdd:cd20976      90 V 90
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
31761-31959 1.09e-06

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 56.90  E-value: 1.09e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKK-------TFMAKFVKVKGTDQVLVK--KEISILN-IARHRNILYLHESFESME 31830
Cdd:cd05099      12 DRLVLGKPLGEGCFGQVVRAEAYGIDKsrpdqtvTVAVKMLKDNATDKDLADliSEMELMKlIGKHKNIINLLGVCTQEG 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 ELVMIFEFIS--------------GLDI-FERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRK 31895
Cdd:cd05099      92 PLYVIVEYAAkgnlreflrarrppGPDYtFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVL--VTE 169
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31896 NSIIKIIEFGQARQL------KPGDNFRLlftAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPF 31959
Cdd:cd05099     170 DNVMKIADFGLARGVhdidyyKKTSNGRL---PVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPY 237
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
8811-8889 1.09e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 52.26  E-value: 1.09e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8811 GDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGEVSSSTFLTVQEQ 8889
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVEDS 93
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7-97 1.09e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 51.95  E-value: 1.09e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     7 TFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPGVQIS-FSDGrarLMIPAVTKANSGRYSLRATNG 85
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRiLADG---LLINKVTQDDTGEYTCRAYQV 77
                            90
                    ....*....|..
gi 1958765569    86 SGQATSTAELLV 97
Cdd:cd20949      78 NSIASDMQERTV 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
6648-6725 1.09e-06

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 51.73  E-value: 1.09e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6648 VLGTSCVLECKVAGSSPISIAWFHEKTKIVsgAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTV 6725
Cdd:cd20952      12 AVGGTVVLNCQATGEPVPTISWLKDGVPLL--GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10808-11185 1.09e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 57.86  E-value: 1.09e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10808 PPAKVPEIPKKPEEKVSVPVPKKEKAPPAKVPEVPKKPVPEEKAPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKKV 10887
Cdd:NF033839    159 PETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELD 238
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10888 EAPPAKAPEV--PPKEVTPEKKVPVVPPKKPEAPPPKVPEppkevvpekkvsmVPPKRPEAPPAKVPEASKevvPEKKVS 10965
Cdd:NF033839    239 ELKKQALSEIdnVNTKVEIENTVHKIFADMDAVVTKFKKG-------------LTQDTPKEPGNKKPSAPK---PGMQPS 302
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10966 VAPKKKPEAPAVKVPEAPKKVVPEKKVPVAAPKkPEAPAAEVPEVPKAAVPQ-KKIPEAVPpkpespppevyeepaeeiv 11044
Cdd:NF033839    303 PQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQ-PEKPKPEVKPQLETPKPEvKPQPEKPK------------------- 362
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11045 peeppeevveepepapppkvtvppkkpvpekkappavvkkpepppakapevPKEAP-PEKKVPSVVPkKPEAPPAKV--- 11120
Cdd:NF033839    363 ---------------------------------------------------PEVKPqPEKPKPEVKP-QPETPKPEVkpq 390
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 11121 PEVPK-EVVPE---KKVAVPKKPEVPPAKVPEVPKKPVVEEKPVIeEKPAIPVAEKVESPPTEVYEEPE 11185
Cdd:NF033839    391 PEKPKpEVKPQpekPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP-EKPKPEVKPQPEKPKPEVKPQPE 458
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
906-989 1.10e-06

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143278 [Multi-domain]  Cd Length: 98  Bit Score: 52.29  E-value: 1.10e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   906 LKNVTVVEGESVTLECHISGYPSPKVTWYREDYQI-----ESSIDFQITF--QSGIARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd05870       8 LKNETTVENGAATLSCKAEGEPIPEITWKRASDGHtfsegDKSPDGRIEVkgQHGESSLHIKDVKLSDSGRYDCEAASRI 87
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd05870      88 GGHQKSMYLDI 98
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
31767-31971 1.12e-06

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 56.04  E-value: 1.12e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31767 EDLGRGEFGIVhrcvetsskktfmaKFVKVKGTDQVLVK-------------KEISILNIARHRNILYLHESFESMEELV 31833
Cdd:cd05113      10 KELGTGQFGVV--------------KYGKWRGQYDVAIKmikegsmsedefiEEAKVMMNLSHEKLVQLYGVCTKQRPIF 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQL--- 31910
Cdd:cd05113      76 IITEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCL--VNDQGVVKVSDFGLSRYVldd 153
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31911 ----KPGDNFRLlftapEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05113     154 eytsSVGSKFPV-----RWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHV 214
PHA03247 PHA03247
large tegument protein UL36; Provisional
10816-11190 1.13e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 1.13e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10816 PKKPEEKVSVPVPKKEK-APPAKVPEVPKKPVPEEKAPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKKVEAP-PAK 10893
Cdd:PHA03247   2589 PDAPPQSARPRAPVDDRgDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrRAR 2668
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10894 APEVPPKevtpekkvpvvppkkPEAPPPKVPEPPKEVVPEKKVSMVPPKRPEAPPAKVPEASKEVVPEKKVSVAPKKK-P 10972
Cdd:PHA03247   2669 RLGRAAQ---------------ASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAsP 2733
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10973 EAPAVKVPEAPKK--VVPEKKVPVAAPKKPEAPAAEVPEVPKAAVPQKKIPEAVPPKPESPPPEVyeepaeeivpeeppe 11050
Cdd:PHA03247   2734 ALPAAPAPPAVPAgpATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL--------------- 2798
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11051 evveepepapppkvtvppKKPVPEKKAPPAVVKKPEPPPAKAPEVPKEAPPEKKVPSVVPKKPEAPPAKVP--------- 11121
Cdd:PHA03247   2799 ------------------PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapgg 2860
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11122 EVPKEVVPEKKVAVPKKPEVPPA-KVPEVPKKPVVEEKPVIEEKPAIPVAEKVESPPTEVYEEPEEVAAQ 11190
Cdd:PHA03247   2861 DVRRRPPSRSPAAKPAAPARPPVrRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
PTZ00121 PTZ00121
MAEBL; Provisional
32980-33612 1.13e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 1.13e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32980 YTTYASQRRDE--EVPKSVFPELTKTEayaissfkrTSEMEAASSVREVKSQMTETR--ESLSSYEHHVSAEMKSAASEE 33055
Cdd:PTZ00121   1081 FDAKEDNRADEatEEAFGKAEEAKKTE---------TGKAEEARKAEEAKKKAEDARkaEEARKAEDARKAEEARKAEDA 1151
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33056 KSLEEKATVRKIKTTLAARILTKPRSItvhegESARfscdtDGEPVPTVTWLRGGQvvstSARHQVTTAKYKSTFEISSV 33135
Cdd:PTZ00121   1152 KRVEIARKAEDARKAEEARKAEDAKKA-----EAAR-----KAEEVRKAEELRKAE----DARKAEAARKAEEERKAEEA 1217
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33136 -QASDEGNYSVVVENTDGKQEAQftltvqKAKAVEKAVTSPPRVKSPEPRV----KSPETVKSPKRVKSPELVASHPKAV 33210
Cdd:PTZ00121   1218 rKAEDAKKAEAVKKAEEAKKDAE------EAKKAEEERNNEEIRKFEEARMahfaRRQAAIKAEEARKADELKKAEEKKK 1291
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33211 SPTETKPTEKGQQlpVPAPPKITQSLKAEASRDIAKltcAVESSALCAKEVAwyKDGKKLKEnghfqfhySADGTYELKI 33290
Cdd:PTZ00121   1292 ADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAE---EAKKKADAAKKKA--EEAKKAAE--------AAKAEAEAAA 1356
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33291 HNLSESDCGEYVCEVSGEGGTSKtsfqftGQSFKSIHEQVSSTTETKKSVQKTAESA-EAKKATQKTAESAEAKKATQKT 33369
Cdd:PTZ00121   1357 DEAEAAEEKAEAAEKKKEEAKKK------ADAAKKKAEEKKKADEAKKKAEEDKKKAdELKKAAAAKKKADEAKKKAEEK 1430
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33370 AESAEAKKPAQKTAESAEAKKPAQKTAEPTEAKKQEPIAPESVSSKpvivtglrdttvssdsvakfviKVTGEPQPtvtw 33449
Cdd:PTZ00121   1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK----------------------KKAEEAKK---- 1484
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33450 TKDGKAIAQSSKYKLSNDKEefileilktetsdgglysctvANSAGSVSSSCKLTIKAVKDTEAQKVSTQKTSEvTAKKK 33529
Cdd:PTZ00121   1485 ADEAKKKAEEAKKKADEAKK---------------------AAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-EAKKA 1542
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33530 ESVQQeiSQKVLTSEEIKMSEVKSHETLAIKEEASKVLI---AEEVKKSAAASLEKSIVHEEVTKTSQAsEEVKTHAEIK 33606
Cdd:PTZ00121   1543 EEKKK--ADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkAEEAKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAK 1619

                    ....*.
gi 1958765569 33607 ALSTQM 33612
Cdd:PTZ00121   1620 IKAEEL 1625
I-set pfam07679
Immunoglobulin I-set domain;
25627-25707 1.13e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.13e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25627 KVVTLRASATLRLFVTIKGRPEPEVKWEKAEGILTE--RAQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVN 25704
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSsdRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                    ...
gi 1958765569 25705 VRV 25707
Cdd:pfam07679    88 LTV 90
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5346-5411 1.14e-06

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 52.11  E-value: 1.14e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5346 KGSLPITVTWLKDNDEITEDDNIRMTFENNVAS-LYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSV 5411
Cdd:cd20959      28 GGDLPLNIRWTLDGQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
19411-19500 1.14e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 51.81  E-value: 1.14e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19411 PPK-ILMPEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSS 19489
Cdd:cd20972       1 PPQfIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569 19490 GTDTQKIKVTV 19500
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
12796-12870 1.14e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 51.81  E-value: 1.14e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12796 PVEFTKPLEDQTVEEEATAVLECEVS-RENAKVKWFKNGTEILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDA 12870
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTgNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLA 76
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6549-6629 1.16e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 51.44  E-value: 1.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6549 MTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVVD 6628
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569  6629 V 6629
Cdd:cd05748      82 V 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
19412-19500 1.17e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.04  E-value: 1.17e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19412 PKILM-PEQITIKAGKKLRVEAHVYGKPNPICKWKKGE---DDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAEN 19487
Cdd:cd20951       1 PEFIIrLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGvpiDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 19488 SSGTDTQKIKVTV 19500
Cdd:cd20951      81 IHGEASSSASVVV 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1801-1879 1.18e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 51.81  E-value: 1.18e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDG-IHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGdLHSLIIAEAFEEDTGRYSCLATNSVG 81
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
5897-5975 1.19e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 51.88  E-value: 1.19e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5897 LKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGVERCYAFLLVQE 5975
Cdd:cd05736      14 PGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
5703-5787 1.19e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 52.13  E-value: 1.19e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5703 PSPVLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGlATFQISNARVENSGTYVCEARNDA-GTASC 5781
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENG-TTLTIRNIRRSDMGIYLCIASNGVpGSVEK 86

                    ....*.
gi 1958765569  5782 SIELKV 5787
Cdd:cd20970      87 RITLQV 92
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
31765-31971 1.20e-06

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 56.03  E-value: 1.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31765 IAEDLGRGEFGIVhrC---VETSSKKTFMA--KFVKVKGTDQVLVK--KEISILNIARHRNILYLhESFESMEELVMIF- 31836
Cdd:cd05066       8 IEKVIGAGEFGEV--CsgrLKLPGKREIPVaiKTLKAGYTEKQRRDflSEASIMGQFDHPNIIHL-EGVVTRSKPVMIVt 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31837 EFIS--GLDIFERINTSAFELneREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIKIIEFGQARQLKpgD 31914
Cdd:cd05066      85 EYMEngSLDAFLRKHDGQFTV--IQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNS--NLVCKVSDFGLSRVLE--D 158
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31915 NFRLLFTAP------EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05066     159 DPEAAYTTRggkipiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWEMSNQDVIKAI 222
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
29699-30003 1.20e-06

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 58.03  E-value: 1.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29699 WVIVEAECLTLSYVVTRLIKNNEYTFRVRAV----NKYGL-------GVPIESEP--IVARNSFTIPSQpgipegvGAGK 29765
Cdd:COG4733     479 WAFGPDELETQLFRVVSIEENEDGTYTITAVqhapEKYAAidagafdDVPPQWPPvnVTTSESLSVVAQ-------GTAV 551
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29766 EHIIIQWTKPESDggneiSNYLVdkrekkslRWTRVNKDYVVY----DTRLKVTSLMEGcDYQFRVTAVNSAGNSEPSEA 29841
Cdd:COG4733     552 TTLTVSWDAPAGA-----VAYEV--------EWRRDDGNWVSVprtsGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAA 617
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29842 SnfiscrePSYT----PGPPSAPRVVDTTKS--SISLAWTKPMydgGTDIIGYvlEMQEKDTDQWcrvhTNTTI-----R 29910
Cdd:COG4733     618 S-------SETTvtgkTAPPPAPTGLTATGGlgGITLSWSFPV---DADTLRT--EIRYSTTGDW----ASATVaqalyP 681
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29911 NNEFTVPDLKMGQKYSFRVAAVNAKGmsDYSETTAEIEPVERLEIPDLELADDLKKTVIIRAGASLRLMVSVSGRPSPVI 29990
Cdd:COG4733     682 GNTYTLAGLKAGQTYYYRARAVDRSG--NVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATV 759
                           330
                    ....*....|...
gi 1958765569 29991 TWSKKGIDLANRA 30003
Cdd:COG4733     760 TDVTAQIDTAVLF 772
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9085-9175 1.20e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 51.73  E-value: 1.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLsETIEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALL-LQVKKASMADAGLYTCKATND 9163
Cdd:cd05744       1 PHFLQAP-GDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569  9164 AGSALCTSSIVI 9175
Cdd:cd05744      80 AGENSFNAELVV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6259-6350 1.20e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.97  E-value: 1.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEH--ELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQN 6336
Cdd:cd20974       1 PVFTQPLQ-SVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569  6337 PAGSTSCSTKVIVK 6350
Cdd:cd20974      80 GSGQATSTAELLVL 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3208-3290 1.21e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 51.44  E-value: 1.21e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3208 VTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFlHDGQEYTLLLI-EAFPEDAAVYTCEAKNDYGvaTTSASL 3286
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQI-ETTASSTSLVIkNAKRSDSGKYTLTLKNSAG--EKSATI 78

                    ....
gi 1958765569  3287 SVEV 3290
Cdd:cd05748      79 NVKV 82
I-set pfam07679
Immunoglobulin I-set domain;
12264-12347 1.23e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12264 KVEKPLYGVEVFVGETARFEIELS---EPDVhgQWKLKGEPLTASPDCEIIEDGKKHVLVLYNCQLDMTGEVSFQAAN-- 12338
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTgtpDPEV--SWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsa 79
                            90
                    ....*....|.
gi 1958765569 12339 --AKSAANLKV 12347
Cdd:pfam07679    80 geAEASAELTV 90
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
31773-32017 1.24e-06

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 55.66  E-value: 1.24e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31773 EFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEisilNIARHRNILYLHESFESMEELVMIFEFISGlDIFERINTSA 31852
Cdd:cd14024       5 EGQELYRAEHYQTEKEYTCKVLSLRSYQECLAPYD----RLGPHEGVCSVLEVVIGQDRAYAFFSRHYG-DMHSHVRRRR 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31853 fELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSIIKIIEFGQARQLK-PGDNFRLLFTAPEYYAPEV- 31930
Cdd:cd14024      80 -RLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNgDDDSLTDKHGCPAYVGPEIl 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31931 -HQHDVVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEeafqEISLEAMDFIDRLLVKERKSRMTAS 32009
Cdd:cd14024     159 sSRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPA----WLSPGARCLVSCMLRRSPAERLKAS 234

                    ....*...
gi 1958765569 32010 EALKHPWL 32017
Cdd:cd14024     235 EILLHPWL 242
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
28085-28153 1.24e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 51.97  E-value: 1.24e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 28085 ISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDNA 28153
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENS 81
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
15626-15705 1.24e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 51.76  E-value: 1.24e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15626 IQIMAGKTLRIPAVVTGRPVPTKVWTI-EEGELDKE-RVVIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAAARV 15703
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRgDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 15704 EV 15705
Cdd:cd05894      85 KV 86
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
31769-31971 1.25e-06

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 55.88  E-value: 1.25e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVETSSKKtfmakfVKVK----GT-DQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLD 31843
Cdd:cd05068      16 LGSGQFGEVWEGLWNNTTP------VAVKtlkpGTmDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGS 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRKNSIIKIIEFGQARQLK--------PGDN 31915
Cdd:cd05068      90 LLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVL--VGENNICKVADFGLARVIKvedeyearEGAK 167
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31916 FRLLFTAPEyyAPEVHQHDVVSsatDMWSLGTLVYVLLS-GINPFLAETNQQMIENI 31971
Cdd:cd05068     168 FPIKWTAPE--AANYNRFSIKS---DVWSFGILLTEIVTyGRIPYPGMTNAEVLQQV 219
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
7865-7943 1.25e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 51.81  E-value: 1.25e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7865 VEAAIGEPTTLQCKV-DGTPEIRISWYKE-HTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSAV 7942
Cdd:pfam00047     6 VTVLEGDSATLTCSAsTGSPGPDVTWSKEgGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTS 85

                    .
gi 1958765569  7943 L 7943
Cdd:pfam00047    86 L 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5416-5491 1.26e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 51.41  E-value: 1.26e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5416 TITEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQN 5491
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PRK10819 PRK10819
transport protein TonB; Provisional
11347-11462 1.27e-06

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 55.84  E-value: 1.27e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11347 ETPPVEEREIERFIQPE-EPgmEPQPE---ETPVQEPEPEKKVIEKPKLKPRPpirapsppkedvkekifqlkavsKKKV 11422
Cdd:PRK10819     59 EPPQAVQPPPEPVVEPEpEP--EPIPEppkEAPVVIPKPEPKPKPKPKPKPKP-----------------------VKKV 113
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1958765569 11423 PEKPE-VVEKVEPTPLKVPTAEKKVRKLLPEPKPQPKEEVV 11462
Cdd:PRK10819    114 EEQPKrEVKPVEPRPASPFENTAPARPTSSTATAAASKPVT 154
I-set pfam07679
Immunoglobulin I-set domain;
12000-12082 1.29e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12000 FAVPLKDVTVPEKRQARFECVLT--REANVIWSKGPDIIKASDKFDIIADGKKHILVINDSQFDDEGVYT--AEVEGKKT 12075
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTgtPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTcvATNSAGEA 82

                    ....*..
gi 1958765569 12076 SAQLFVT 12082
Cdd:pfam07679    83 EASAELT 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
26302-26392 1.29e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.97  E-value: 1.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26302 MMDVKFRDViVVKAGEVLKINADIAGRPLPVISWAKDG--VEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNV 26379
Cdd:cd20974       2 VFTQPLQSV-VVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 26380 AGTRTMAVNCKVL 26392
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7762-7852 1.29e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7762 PATFVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLsQSPNCGITTTERSSILEILESTIEDYAQYACLIENEA 7841
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL-QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  7842 GQDICEALVSV 7852
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
21587-21667 1.32e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.97  E-value: 1.32e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQ--RVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVIT 21664
Cdd:cd20974      10 VVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAE 89

                    ...
gi 1958765569 21665 IQV 21667
Cdd:cd20974      90 LLV 92
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7121-7196 1.33e-06

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 51.09  E-value: 1.33e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7121 GESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNtphLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSV 7196
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSGT---LRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
27792-27868 1.34e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 51.63  E-value: 1.34e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 27792 SVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLgSDARYSIQNTDSsslLVIPQVTRNDTGKYILTIENGVGQPKSS 27868
Cdd:cd05725       6 NQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL-PKGRYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEAS 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
32092-32171 1.34e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.04  E-value: 1.34e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32092 EEGGYVKYVCKIENYDQStQVTWY---FGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAEL 32168
Cdd:cd20951      13 WEKSDAKLRVEVQGKPDP-EVKWYkngVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASV 91

                    ...
gi 1958765569 32169 FVK 32171
Cdd:cd20951      92 VVE 94
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
33898-33985 1.35e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 51.68  E-value: 1.35e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRfhieNTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:cd04978       6 PPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMR----RTVDGRTLIFSNLQPNDTAVYQCNASNVHGYLL 81

                    ....*...
gi 1958765569 33978 ATVNINIR 33985
Cdd:cd04978      82 ANAFLHVL 89
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5790-5878 1.35e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.35e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5790 PPIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMsVFYLHITKCAPSDVGEYQCIIANEG 5869
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAG-VGELHIQDVLPEDHGTYTCLAKNAA 79

                    ....*....
gi 1958765569  5870 GSCACTARV 5878
Cdd:cd20976      80 GQVSCSAWV 88
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
22659-22747 1.36e-06

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 51.79  E-value: 1.36e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22659 PPAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAES--TENN---SLLTIKEACREDVGHYTVK 22733
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDyvTSDGdvvSYVNISSVRVEDGGEYTCT 80
                            90
                    ....*....|....*.
gi 1958765569 22734 LTNSAGEAT--ETLNV 22747
Cdd:cd20956      81 ATNDVGSVShsARINV 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
25627-25707 1.40e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.35  E-value: 1.40e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25627 KVVTLRASATLRLFVTIKGRPEPEVKWEKAEGIL---TERAQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTAFV 25703
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  25704 NVRV 25707
Cdd:smart00410    82 TLTV 85
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
31761-31959 1.41e-06

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 55.72  E-value: 1.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAE-DLGRGEFGIVHRCVETSSKKTFMAKFVKVKGTDQVLVK----KEISILNIARHRNILYLHESFESmEELVMI 31835
Cdd:cd05115       3 DNLLIDEvELGSGNFGCVKKGVYKMRKKQIDVAIKVLKQGNEKAVRdemmREAQIMHQLDNPYIVRMIGVCEA-EALMLV 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31836 FEFISGLDIFERINTSAFELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSiiKIIEFGQARQLKPGDN 31915
Cdd:cd05115      82 MEMASGGPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYA--KISDFGLSKALGADDS 159
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 1958765569 31916 FRLLFTA---P-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPF 31959
Cdd:cd05115     160 YYKARSAgkwPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
5511-5600 1.42e-06

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 51.64  E-value: 1.42e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEIS-ASDKYKFSFH-DNTAFLEISQLEGTDSGTYTCSATNK 5588
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  5589 AGHSQCSGHLTV 5600
Cdd:cd05893      81 QGRISCTGRLMV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4199-4273 1.45e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 51.41  E-value: 1.45e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4199 PTILKPLVDTISEKGDTVHLT--SSISNAKEVNWYFKGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASN 4273
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTceATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
1522-1607 1.45e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 51.42  E-value: 1.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1522 LKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGtKGEAALKIDSTISQDSAWYTATAINKAGRDTT 1601
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDE-DGLCSLIISDVCGDDSGKYTCKAVNSLGEATC 82

                    ....*.
gi 1958765569  1602 RCKVNI 1607
Cdd:cd20973      83 SAELTV 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7293-7381 1.45e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.48  E-value: 1.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKfKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79

                    ....*....
gi 1958765569  7373 GSDTCACTV 7381
Cdd:cd20976      80 GQVSCSAWV 88
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
31769-31996 1.45e-06

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 55.97  E-value: 1.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31769 LGRGEFGIVHRCVetSSKKTFMAK--FVKVKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELVMIFEFISGLD 31843
Cdd:cd14158      23 LGEGGFGVVFKGY--INDKNVAVKklAAMVDISTEDLTKqfeQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGS 100
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31844 IFERI----NTSAFELNERevVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARqlKPGDNFRLL 31919
Cdd:cd14158     101 LLDRLaclnDTPPLSWHMR--CKIAQGTANGINYLHENNHIHRDIKSANILLD--ETFVPKISDFGLAR--ASEKFSQTI 174
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31920 FT-----APEYYAPEVHQHDvVSSATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMnaeytfDEEAFQEISLEamDFI 31994
Cdd:cd14158     175 MTerivgTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDIK------EEIEDEEKTIE--DYV 245

                    ..
gi 1958765569 31995 DR 31996
Cdd:cd14158     246 DK 247
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
3577-3668 1.46e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.58  E-value: 1.46e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTI-IHNPDGSGTFIVNDPQRGDSGLYICKAENL 3655
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVqISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  3656 WGTSTCTAELLVL 3668
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
907-989 1.47e-06

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 51.63  E-value: 1.47e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   907 KNVTVVEGESVTLECHIS-GYPSPKVTWYREDYQIESSiDFQITFQSGiARLMIREAFAEDSGRFTCSAVNEAGT-VSTS 984
Cdd:cd05724       5 SDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLD-NERVRIVDD-GNLLIAEARKSDEGTYKCVATNMVGErESRA 82

                    ....*
gi 1958765569   985 CYLAV 989
Cdd:cd05724      83 ARLSV 87
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
19817-19895 1.48e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 51.59  E-value: 1.48e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTL 91
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
31440-31531 1.49e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 51.69  E-value: 1.49e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEFKGGYHQLIIASVTDDDATVYQVRATNQ 31519
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569 31520 GGSVSGTASLEV 31531
Cdd:cd05892      81 AGVVSCNARLDV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5143-5217 1.49e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 51.43  E-value: 1.49e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5143 PSQLLKKGDATQLVCKV-TGTPPIKITWFANDRELRESSKHKMSFV-ESTAVLRLTDVAIEDSGEYMCEAQNEAGSD 5217
Cdd:pfam00047     4 PTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGrTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
24835-24913 1.51e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 51.42  E-value: 1.51e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24835 VQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVE-ETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVIV 24913
Cdd:cd20973       9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
7576-7666 1.51e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 51.86  E-value: 1.51e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7576 PPSF-IRKLK-DTTATLGASVVLECRVSGSAPISVGWFLDGnEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAAN 7653
Cdd:cd05730       1 PPTIrARQSEvNATANLGQSVTLACDADGFPEPTMTWTKDG-EPIESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAEN 79
                            90
                    ....*....|...
gi 1958765569  7654 VAGQDESSALLTV 7666
Cdd:cd05730      80 KAGEQEAEIHLKV 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4763-4849 1.52e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 51.24  E-value: 1.52e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4763 VKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKgqevikEDGKIKMSFSSGVA--VLTISDVQIGLGGKYTCLAENEAGS 4840
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRK------EDGELPKGRYEILDdhSLKIRKVTAGDMGSYTCVAENMVGK 74

                    ....*....
gi 1958765569  4841 QTSVGELIV 4849
Cdd:cd05725      75 IEASATLTV 83
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9296-9380 1.54e-06

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 51.41  E-value: 1.54e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9296 PQSIRVVEKTTA----TFIAK--VGGDPIPNVKWTKGKwRQLNQGGRILIHQKGdesKLEIRDTTK-TDSGLYRCVAFNK 9368
Cdd:cd20958       1 PPFIRPMGNLTAvagqTLRLHcpVAGYPISSITWEKDG-RRLPLNHRQRVFPNG---TLVIENVQRsSDEGEYTCTARNQ 76
                            90
                    ....*....|...
gi 1958765569  9369 HGEI-ESNVNLQV 9380
Cdd:cd20958      77 QGQSaSRSVFVKV 89
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
3202-3288 1.55e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 51.24  E-value: 1.55e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3202 LQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGfKCKFLHDgqeYTLLLIEAFPEDAAVYTCEAKNDYGVAT 3281
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDD---HSLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  3282 TSASLSV 3288
Cdd:cd05725      77 ASATLTV 83
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
1254-1337 1.55e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 51.62  E-value: 1.55e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1254 KNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRI-RRGERYQMDflqdgRASLRIPVVLPEDEGIYTAFASNIKGNAICS 1332
Cdd:cd20978       9 KNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLqGPMERATVE-----DGTLTIINVQPEDTGYYGCVATNEIGDIYTE 83

                    ....*
gi 1958765569  1333 GKLYV 1337
Cdd:cd20978      84 TLLHV 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8517-8607 1.57e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.48  E-value: 1.57e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8517 PPSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKyQTTLTDNTCALTVNMLEDADAGDYTCIATNVA 8596
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  8597 GSDECSAPLTV 8607
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
5512-5590 1.58e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 51.56  E-value: 1.58e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5512 SFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAG 5590
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS 79
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
32320-32396 1.59e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 51.24  E-value: 1.59e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32320 GQSVCFEIRVSGIPAPTLKWEKDGQPLSLGpHIEIVHEgldyYALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:cd05725      12 DDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDD----HSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
33701-33787 1.61e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 51.24  E-value: 1.61e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33701 ISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPisissnisVSRSRNMYTLeirNASVSDSGKYTVKAKNFRGQC- 33779
Cdd:pfam13895     3 VLTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSA--------ISSSPNFFTL---SVSAEDSGTYTCVARNGRGGKv 71

                    ....*...
gi 1958765569 33780 SATASLTV 33787
Cdd:pfam13895    72 SNPVELTV 79
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7480-7578 1.63e-06

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 51.88  E-value: 1.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7480 PARIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSV 7559
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*....
gi 1958765569  7560 GKSSCTVSVHVSDRVVPPS 7578
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPPA 99
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
28480-28560 1.63e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 51.47  E-value: 1.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDG-----VEIERRMNMEITDVLgstsLFVRDATRDHRGVYTVEAKNVSGSTKA 28554
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGgtdfpAARERRMHVMPEDDV----FFIVDVKIEDTGVYSCTAQNSAGSISA 84

                    ....*.
gi 1958765569 28555 EITVKV 28560
Cdd:cd05763      85 NATLTV 90
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7023-7099 1.65e-06

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 51.72  E-value: 1.65e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7023 TVGLPVTLTCRL-NGSAPIHVCWYRDGVLLRDDENLQMSFVDNVAT-LKILQTDLSHSGQYSCSASNPLGTASSTARLT 7099
Cdd:cd20959      15 QVGMRAQLHCGVpGGDLPLNIRWTLDGQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCHARNSAGSASYTAPLT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7211-7290 1.65e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 51.05  E-value: 1.65e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7211 VAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVGHASCSTALKV 7290
Cdd:cd05748       3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2317-2388 1.67e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 51.34  E-value: 1.67e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2317 AILQGLSDQKVCEGDIVQLEVKVS-LENVEGVWMKDGQEVQHSDRVHIVIDKQ-SHMLLIEDMTKEDAGNYSFT 2388
Cdd:cd05744       2 HFLQAPGDLEVQEGRLCRFDCKVSgLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCI 75
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
16640-16726 1.68e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.58  E-value: 1.68e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16640 VEEGTDVNIVAKIKGVPFPTLTWFKAPPKKPDSKEPvvydtHVNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTASK 16719
Cdd:cd20974      12 VLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLP-----GVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86

                    ....*..
gi 1958765569 16720 EMRLNVL 16726
Cdd:cd20974      87 TAELLVL 93
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
1258-1324 1.70e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 51.35  E-value: 1.70e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1258 ILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRG-ERYQMdfLQDGRaSLRIPVVLPEDEGIYTAFASN 1324
Cdd:cd20970      14 AREGENATFMCRAEGSPEPEISWTRNGNLIIEFnTRYIV--RENGT-TLTIRNIRRSDMGIYLCIASN 78
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7209-7290 1.71e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 51.24  E-value: 1.71e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7209 SKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESwKYNMSFVNSvalLTINEASVEDTGDYICEAHNGVGHASCSTAL 7288
Cdd:cd05725       6 NQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEASATL 81

                    ..
gi 1958765569  7289 KV 7290
Cdd:cd05725      82 TV 83
I-set pfam07679
Immunoglobulin I-set domain;
16332-16420 1.71e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.49  E-value: 1.71e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16332 LICKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKAmkDGIHDIPEDaqletaENSSVIVIPECTRAHSGKYSITAKNKAGQ 16411
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS--SDRFKVTYE------GGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                    ....*....
gi 1958765569 16412 KTANCRVKV 16420
Cdd:pfam07679    82 AEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8431-8511 1.72e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 51.05  E-value: 1.72e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8431 IKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCTVSIQ 8510
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                    .
gi 1958765569  8511 V 8511
Cdd:cd05748      82 V 82
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
23460-23542 1.73e-06

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 51.45  E-value: 1.73e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23460 LRKVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIR--DAAIIDVTSS-FTSLVLDNVNRYDSGKYTLTLENSSGTKSA 23536
Cdd:cd05891       7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIElsEHYSVKLEQGkYASLTIKGVTSEDSGKYSINVKNKYGGETV 86

                    ....*.
gi 1958765569 23537 FVTVRV 23542
Cdd:cd05891      87 DVTVSV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
1516-1609 1.76e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 51.31  E-value: 1.76e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDiIVPHKYPRIRI-EGTKGEAALKIDSTISQDSAWYTATAIN 1594
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNE-MLQYNTDRISLyQDNCGRICLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|....*
gi 1958765569  1595 KAGrdTTRCKVNIEV 1609
Cdd:cd05892      80 EAG--VVSCNARLDV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4862-4935 1.77e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 51.05  E-value: 1.77e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  4862 IQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSS 4935
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
31059-31122 1.77e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 51.09  E-value: 1.77e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31059 GEAAQLSCQIVGrPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNE 31122
Cdd:cd20967      12 GHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGE 74
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
106-193 1.78e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 51.47  E-value: 1.78e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   106 FSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAeiqssLDFQISQE------GDLYSLLIAEAYPEDSGTYSVNAT 179
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGG-----TDFPAARErrmhvmPEDDVFFIVDVKIEDTGVYSCTAQ 76
                            90
                    ....*....|....
gi 1958765569   180 NSVGRATSTADLLV 193
Cdd:cd05763      77 NSAGSISANATLTV 90
fn3 pfam00041
Fibronectin type III domain;
18614-18698 1.80e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.26  E-value: 1.80e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18614 GEPENLHIADKGKTFVYLKWRRPDyDGGSPNLSYHVERRLKGSADWERVHKGSIKETHYMVDKCVENQIYEFRVQTKNEG 18693
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 18694 GESDW 18698
Cdd:pfam00041    80 GEGPP 84
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8243-8325 1.81e-06

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 51.38  E-value: 1.81e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8243 PVETLK-GADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLtsiHILNVDTADIGEYQCKATNDVgsDTCVGS 8321
Cdd:cd20957       9 PVQTVDfGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVL---VIPSVKREDKGMYQCFVRNDG--DSAQAT 83

                    ....
gi 1958765569  8322 VTLK 8325
Cdd:cd20957      84 AELK 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5981-6067 1.81e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.58  E-value: 1.81e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5981 EKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRY--FSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSS 6058
Cdd:cd20974       5 QPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLpgVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQA 84

                    ....*....
gi 1958765569  6059 SCDAYLRVL 6067
Cdd:cd20974      85 TSTAELLVL 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31212-31388 1.83e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 57.32  E-value: 1.83e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31212 YKVQLSNVFG-------TVDAILDVEiqdKPDKPTGpIVIEALLKNSVVISWKAPADDGgswITNYVVEKCEAKEGAeWQ 31284
Cdd:COG3401     300 YRVTAVDAAGnesapsnVVSVTTDLT---PPAAPSG-LTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGT-YT 371
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31285 LVSSAISVTTCRIVNLTENAGYYFRVSAQNTFGI-SEPLEVASVVIIKSPFEKPSVPGKPTITAVTKDSCVVAWKPPASD 31363
Cdd:COG3401     372 KIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNP 451
                           170       180
                    ....*....|....*....|....*
gi 1958765569 31364 GGAKIRNYYLEKREKKQNKWIAVTT 31388
Cdd:COG3401     452 GVSAAVLADGGDTGNAVPFTTTSST 476
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
7480-7561 1.83e-06

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 51.39  E-value: 1.83e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7480 PARIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLK-DGRELSSGSRHhitfvRNLASLKIPSAEMNDKGLYSFEVENS 7558
Cdd:cd04968       1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKvDGSPSSQWEIT-----TSEPVLEIPNVQFEDEGTYECEAENS 75

                    ...
gi 1958765569  7559 VGK 7561
Cdd:cd04968      76 RGK 78
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33424-33505 1.85e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 51.24  E-value: 1.85e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33424 DTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQsSKYKLSNDKEefiLEILKTETSDGGLYSCTVANSAGSVSSSCKL 33503
Cdd:cd05725       6 NQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPK-GRYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEASATL 81

                    ..
gi 1958765569 33504 TI 33505
Cdd:cd05725      82 TV 83
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
3463-3550 1.85e-06

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 51.06  E-value: 1.85e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3463 FIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLtPSADYKFVFDGnnhSLIILFTRFQDEGEYTCMASNEYGRA 3542
Cdd:cd05728       2 WLKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPL-ASENRIEVEAG---DLRITKLSLSDSGMYQCVAENKHGTI 77

                    ....*...
gi 1958765569  3543 VCSAHLKV 3550
Cdd:cd05728      78 YASAELAV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8328-8418 1.86e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 51.65  E-value: 1.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8328 PQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIVRESD--NIWISHSENVATLHFSRAEPANAGKYTCQIKN 8405
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569  8406 DAGVQECYATLSV 8418
Cdd:cd20951      81 IHGEASSSASVVV 93
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
12188-12258 1.86e-06

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 51.53  E-value: 1.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12188 EKDEIILKCEVSKDVP---VKWFKDGEEIVPSPK-HSVKTDGLRRI--LKIKKAELKDKGEYTC----DCGTDTTKANVT 12257
Cdd:cd05895      13 AGSKLVLRCETSSEYPslrFKWFKNGKEINRKNKpENIKIQKKKKKseLRINKASLADSGEYMCkvssKLGNDSASANVT 92

                    .
gi 1958765569 12258 V 12258
Cdd:cd05895      93 I 93
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
22382-22460 1.88e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 51.38  E-value: 1.88e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22382 VTIRACCTLRLFVPIKGRPAPEVKWARehGESLDKAS-----IESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFV 22456
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSR--GDKAFTATegrvrVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 22457 NVRV 22460
Cdd:cd05894      83 FVKV 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
24824-24913 1.88e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 51.43  E-value: 1.88e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAG 24903
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81
                            90
                    ....*....|
gi 1958765569 24904 TATENLSVIV 24913
Cdd:cd20972      82 SDTTSAEIFV 91
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
4582-4653 1.88e-06

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 51.43  E-value: 1.88e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  4582 SYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILdITDVKVDDSGTYSCEATNDAG 4653
Cdd:cd05867       8 SHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGALI-LTDVQPSDTAVYQCEARNRHG 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7578-7666 1.90e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 51.18  E-value: 1.90e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7578 SFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQ 7657
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                    ....*....
gi 1958765569  7658 DESSALLTV 7666
Cdd:cd20949      81 ASDMQERTV 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6463-6530 1.90e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.79  E-value: 1.90e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6463 AELQASIEGAPPISVHWLKEKEEVvRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDGGVREN 6530
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPL-PPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7114-7196 1.92e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 51.42  E-value: 1.92e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7114 VSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGN-TPHLRILKVGKGDSGQYTCQATNDVGKDMCSA 7192
Cdd:cd20973       5 RDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSA 84

                    ....
gi 1958765569  7193 QLSV 7196
Cdd:cd20973      85 ELTV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
20517-20577 1.92e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.79  E-value: 1.92e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 20517 PIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKE 20577
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
31053-31132 1.92e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 51.47  E-value: 1.92e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31053 DVTTKLGEAAQLSCQIVGRPLPDIKWYR-FGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSK 31131
Cdd:cd05763       8 DITIRAGSTARLECAATGHPTPQIAWQKdGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANAT 87

                    .
gi 1958765569 31132 L 31132
Cdd:cd05763      88 L 88
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
9291-9380 1.94e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 51.30  E-value: 1.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9291 FFVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWtkgkwrQLNqgGRILIHQKGDESKLEIRDT------TKTDSGLYRCV 9364
Cdd:cd04978       1 YWIIEPPSLVLSPGETGELICEAEGNPQPTITW------RLN--GVPIEPAPEDMRRTVDGRTlifsnlQPNDTAVYQCN 72
                            90
                    ....*....|....*.
gi 1958765569  9365 AFNKHGEIESNVNLQV 9380
Cdd:cd04978      73 ASNVHGYLLANAFLHV 88
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5976-6074 1.94e-06

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 51.49  E-value: 1.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5976 PAQIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDF 6055
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*....
gi 1958765569  6056 GSSSCDAYLRVLDQDIPPS 6074
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPPA 99
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
8518-8607 1.95e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 51.32  E-value: 1.95e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAIS-SGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVA 8596
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRpDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569  8597 GSDECSAPLTV 8607
Cdd:cd20975      81 GARQCEARLEV 91
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7218-7288 1.95e-06

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 50.64  E-value: 1.95e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  7218 IQLECKISGSPEIKVVWFRNDSELHESWKYNMSfvnSVALLTINEASVEDTGDYICEAHNGVGHASCSTAL 7288
Cdd:cd05746       1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHIS---PEGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2055-2125 1.96e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.79  E-value: 1.96e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  2055 AHFRVRVVGKPDPECEWYKNGVKIERSDRiYWYWPEDNVCELVIRDVTAEDSASIMVKAINIAGETSSHAF 2125
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSR-DSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
I-set pfam07679
Immunoglobulin I-set domain;
26994-27078 1.96e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 1.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26994 PSHTVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTF 27073
Cdd:pfam07679     6 KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEAS 85

                    ....*
gi 1958765569 27074 INIIV 27078
Cdd:pfam07679    86 AELTV 90
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8062-8137 1.97e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 50.86  E-value: 1.97e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8062 GESGSFKCHVTGTAPIKITWAKDNREIRPGGNYkmtlventatlTVLKVAKGDAGQYTCYASN-VAGKDSCSAQLGV 8137
Cdd:pfam13895    14 GEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF-----------FTLSVSAEDSGTYTCVARNgRGGKVSNPVELTV 79
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
25625-25707 1.98e-06

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 51.45  E-value: 1.98e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25625 LRKVVTLRASATLRLFVTIKGRPEPEVKWEK--AEGILTERAQIEVTSS-YTMLVIDNVTRFDSGRYNLTLENNSGSKTA 25701
Cdd:cd05891       7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKndQDIELSEHYSVKLEQGkYASLTIKGVTSEDSGKYSINVKNKYGGETV 86

                    ....*.
gi 1958765569 25702 FVNVRV 25707
Cdd:cd05891      87 DVTVSV 92
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6921-7002 1.99e-06

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 51.25  E-value: 1.99e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6921 LEP--LEASVGDSVSLQCQVA-GTPEITVSWFKGDTKLRSTPEYRTYFTNnvATLVFNKVGINDSGEYTCVAENSIGTAA 6997
Cdd:cd05724       2 VEPsdTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDNERVRIVDD--GNLLIAEARKSDEGTYKCVATNMVGERE 79

                    ....*
gi 1958765569  6998 SKTVF 7002
Cdd:cd05724      80 SRAAR 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15148-15530 2.01e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 56.93  E-value: 2.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15148 VLTYTAKGLEEGKEYQFRVRAENAAGIGEPSRATPPTKAVDPIDAPkvilrtslevkrgdeIALDATISGSPYPTITWIK 15227
Cdd:COG3401     191 TLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAP---------------TGLTATADTPGSVTLSWDP 255
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15228 DENVIVPEEIkkrvappVRRKKgeaEEEEPFT-LPLTERLSINNS--KQGESQlrvrdslrpdhgQYMIKVENDHGVAKA 15304
Cdd:COG3401     256 VTESDATGYR-------VYRSN---SGDGPFTkVATVTTTSYTDTglTNGTTY------------YYRVTAVDAAGNESA 313
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15305 PC-TVSV---LDTPGPPINFVFEDIRKDSVLCKWEPPLDDGgseIINYTLEKKdkTKPDSEWIVITSTLRNCKYSVTKLI 15380
Cdd:COG3401     314 PSnVVSVttdLTPPAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYRS--TSGGGTYTKIAETVTTTSYTDTGLT 388
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15381 EGKEYLFRVRAENRFGPGPPcVSKPLLAKDPFEPPDAPDKPIVDDVTSNSMVVKWNEPKDNGSPILGYWLEKREVNSTHW 15460
Cdd:COG3401     389 PGTTYYYKVTAVDAAGNESA-PSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA 467
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15461 SRVNKallsSLKTKVDGLLEGLTYVFRVCAENAAGPGKFSPPSDPKTARDPISPPGPPVPRVADTSSTTI 15530
Cdd:COG3401     468 VPFTT----TSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGA 533
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
7299-7374 2.01e-06

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 51.04  E-value: 2.01e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7299 KPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSknfDTSLHIFNLEAPDIGEYHCKATNEVGS 7374
Cdd:cd05723       3 KPSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVK---EHNLQVLGLVKSDEGFYQCIAENDVGN 75
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8238-8314 2.01e-06

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 51.25  E-value: 2.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8238 RKKPFPVETLKGADVHLECEL-QGTPPFQVSWYKDKRELR-SGKKYKIMSE-NLLtsihILNVDTADIGEYQCKATNDVG 8314
Cdd:cd05724       1 RVEPSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNlDNERVRIVDDgNLL----IAEARKSDEGTYKCVATNMVG 76
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
1259-1337 2.02e-06

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 51.01  E-value: 2.02e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1259 LEGMGVTFHCKMSGYPLPKIAWYK-DGKRIRRGERYQMDflqdgrASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYV 1337
Cdd:cd04968      14 LKGQTVTLECFALGNPVPQIKWRKvDGSPSSQWEITTSE------PVLEIPNVQFEDEGTYECEAENSRGKDTVQGRIIV 87
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
31761-31948 2.02e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 55.81  E-value: 2.02e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFGIVHRCVETSSKKTFMA-KFVKVKGTDQVLVKKEISILNIARHRnilylhESFESmEELVMIFEF- 31838
Cdd:cd07862       1 QQYECVAEIGEGAYGKVFKARDLKNGGRFVAlKRVRVQTGEEGMPLSTIREVAVLRHL------ETFEH-PNVVRLFDVc 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31839 -ISGLDIFERInTSAFELNEREVVSYVR-----------------QVCEALEFLHSQNIGHFDIRPENIIYQTrkNSIIK 31900
Cdd:cd07862      74 tVSRTDRETKL-TLVFEHVDQDLTTYLDkvpepgvptetikdmmfQLLRGLDFLHSHRVVHRDLKPQNILVTS--SGQIK 150
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*...
gi 1958765569 31901 IIEFGQARQLKPGDNFRLLFTAPEYYAPEVHQHDVVSSATDMWSLGTL 31948
Cdd:cd07862     151 LADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCI 198
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
15918-16006 2.03e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 50.99  E-value: 2.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15918 DTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKPtdalnitkEEVSRSEAKTELS---IPKAVREDKGTYTITASNR 15994
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTAT--------EGRVRVESYKDLSsfvIEGAEREDEGVYTITVTNP 74
                            90
                    ....*....|..
gi 1958765569 15995 LGSVFRNVHVEV 16006
Cdd:cd05894      75 VGEDHASLFVKV 86
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4760-4839 2.04e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 51.24  E-value: 2.04e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4760 PTFVKKVDDFT-ALAGQTVTLQAAVRGSEPISVMWM-KGQEVIKEDGKIKMSFSSgvavLTISDVQIGLGGKYTCLAENE 4837
Cdd:cd20978       1 PKFIQKPEKNVvVKGGQDVTLPCQVTGVPQPKITWLhNGKPLQGPMERATVEDGT----LTIINVQPEDTGYYGCVATNE 76

                    ..
gi 1958765569  4838 AG 4839
Cdd:cd20978      77 IG 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
3208-3288 2.05e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 51.18  E-value: 2.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3208 VTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTSASLS 3287
Cdd:cd20949       9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQERT 88

                    .
gi 1958765569  3288 V 3288
Cdd:cd20949      89 V 89
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
3304-3391 2.06e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 2.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3304 PPAIVTPLQDAVTSEGRPARFQCQVSGTDL-KVSWYcRDKKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAV 3382
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVpRITWI-RNAQPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79

                    ....*....
gi 1958765569  3383 GQVSSTATL 3391
Cdd:cd20976      80 GQVSCSAWV 88
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
24135-24227 2.09e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 51.35  E-value: 2.09e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24135 PRISMDPKfRDTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDfKALLIVKDAIRIDGGQYILRASN 24214
Cdd:cd20970       1 PVISTPQP-SFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVREN-GTTLTIRNIRRSDMGIYLCIASN 78
                            90
                    ....*....|....
gi 1958765569 24215 -VAGSKSFPVNVKV 24227
Cdd:cd20970      79 gVPGSVEKRITLQV 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
3312-3392 2.10e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 50.86  E-value: 2.10e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3312 QDAVTSEGRPARFQCQVSGTDL-KVSWYCRDKKIKPSRFfrmtQFEDTYQLEIAEAFPEDEGTYAFVANNAVGQVSSTAT 3390
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGGDPVpTVRWRKEDGELPKGRY----EILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASAT 80

                    ..
gi 1958765569  3391 LR 3392
Cdd:cd05725      81 LT 82
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
31439-31528 2.14e-06

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 51.32  E-value: 2.14e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31439 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEiIADGLKYRVQEFKGGYHQLIIASVT-DDDATVYQVRAT 31517
Cdd:cd20971       1 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKE-IIADGLKYRIQEFKGGYHQLIIASVtDDDATVYQVRAT 79
                            90
                    ....*....|.
gi 1958765569 31518 NQGGSVSGTAS 31528
Cdd:cd20971      80 NQGGSVSGTAS 90
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
1798-1889 2.16e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 51.24  E-value: 2.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1798 KQKPDIVlfpepVRVLEGETARFRCRVTGYPQPKVNWYLNGQ-LIRKSKRFRVrydGIHYLDIVDCKSYDTGEVKVTAEN 1876
Cdd:cd20978       4 IQKPEKN-----VVVKGGQDVTLPCQVTGVPQPKITWLHNGKpLQGPMERATV---EDGTLTIINVQPEDTGYYGCVATN 75
                            90
                    ....*....|...
gi 1958765569  1877 PEGVTEHKVKLEI 1889
Cdd:cd20978      76 EIGDIYTETLLHV 88
I-set pfam07679
Immunoglobulin I-set domain;
29169-29249 2.18e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 2.18e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29169 ITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLKETDRMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITVV 29248
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                    .
gi 1958765569 29249 V 29249
Cdd:pfam07679    90 V 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
33721-33787 2.20e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 50.67  E-value: 2.20e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33721 ISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQCSATASLTV 33787
Cdd:cd05748      16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
909-989 2.20e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 51.18  E-value: 2.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   909 VTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLA 988
Cdd:cd20949       9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQERT 88

                    .
gi 1958765569   989 V 989
Cdd:cd20949      89 V 89
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8048-8137 2.20e-06

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 51.25  E-value: 2.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTL--VENTATLTVLKVAKGDAGQYTCYASNV 8125
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQrdLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  8126 AGKDSCSAQLGV 8137
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8425-8511 2.20e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 51.34  E-value: 2.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8425 VEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNK-VSGLKIISVAPGDSGVYSFEVQNPVGKD 8503
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRAGEN 83

                    ....*...
gi 1958765569  8504 SCTVSIQV 8511
Cdd:cd05744      84 SFNAELVV 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
33080-33162 2.23e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 51.04  E-value: 2.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33080 RSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQ-VTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQF 33158
Cdd:cd20973       5 RDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQiDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSA 84

                    ....
gi 1958765569 33159 TLTV 33162
Cdd:cd20973      85 ELTV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
31440-31531 2.23e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.20  E-value: 2.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKyRVQ-EFKGGYHQLIIASVTDDDATVYQVRATN 31518
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLP-GVQiSFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|...
gi 1958765569 31519 QGGSVSGTASLEV 31531
Cdd:cd20974      80 GSGQATSTAELLV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
19816-19897 2.24e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 51.05  E-value: 2.24e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19816 LLTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKR-NLCTLELFSVNRKDSGDYTITAENSSGSKSATIK 19894
Cdd:cd05737      10 VVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVT 89

                    ...
gi 1958765569 19895 LKV 19897
Cdd:cd05737      90 VSV 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
5994-6057 2.25e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 51.39  E-value: 2.25e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5994 VTLECVVAGTPELKVKWLKDGKQIVPS-RYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGS 6057
Cdd:cd05857      22 VKFRCPAAGNPTPTMRWLKNGKEFKQEhRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGS 86
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
23464-23543 2.27e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 51.08  E-value: 2.27e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23464 INIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDAA---IIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTV 23540
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAArerRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATL 88

                    ...
gi 1958765569 23541 RVL 23543
Cdd:cd05763      89 TVL 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6732-6818 2.29e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 50.86  E-value: 2.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6732 VKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGdRCNIYFEDTvaeLELFNIDVSQSGEYTCVVSNNAGQAS 6811
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  6812 CTTRLFV 6818
Cdd:cd05725      77 ASATLTV 83
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
33082-33162 2.29e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.85  E-value: 2.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33082 ITVHEGESARFSCDTDGEPVPTVTWLRGGQVVS-TSARHQVTtakyKSTFEISSVQASDEGNYSVVVENTDGKQEAQFTL 33160
Cdd:cd20978      11 VVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQgPMERATVE----DGTLTIINVQPEDTGYYGCVATNEIGDIYTETLL 86

                    ..
gi 1958765569 33161 TV 33162
Cdd:cd20978      87 HV 88
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
4400-4466 2.29e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 51.45  E-value: 2.29e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4400 VGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKH-SLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:cd05729      18 AANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYG 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
32201-32293 2.31e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.85  E-value: 2.31e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFT-LPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKpgDDDKKYTFESDKglyqLTINSVTTDDDAEYAVVAR 32279
Cdd:cd20978       1 PKFIqKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ--GPMERATVEDGT----LTIINVQPEDTGYYGCVAT 74
                            90
                    ....*....|....
gi 1958765569 32280 NKHGEDSCKAKLTV 32293
Cdd:cd20978      75 NEIGDIYTETLLHV 88
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
6271-6349 2.31e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 51.08  E-value: 2.31e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6271 VKAGDSARLECKITGSPEIRVVWYRN-EHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTKVIV 6349
Cdd:cd05763      11 IRAGSTARLECAATGHPTPQIAWQKDgGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATLTV 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6914-6994 2.32e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 51.20  E-value: 2.32e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6914 PPYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSI 6993
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    .
gi 1958765569  6994 G 6994
Cdd:cd05747      83 G 83
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1801-1889 2.33e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 51.25  E-value: 2.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIR--KSKRFRVRYDGIHYLDIVDCKSYDTGEVKVTAENPE 1878
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRpdSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  1879 GVTEHKVKLEI 1889
Cdd:cd20990      81 GQNSFNLELVV 91
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
10826-11016 2.33e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 57.17  E-value: 2.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10826 PVPKKEKAPPAKVPEVPKKPVPEEKAPVPVPKkvepppAKVPEVPKKPVPEKKVPAPTPKKVEAPPAKAPEVPPKEVTPE 10905
Cdd:PRK07003    360 PAVTGGGAPGGGVPARVAGAVPAPGARAAAAV------GASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPP 433
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10906 KKVPVVPPKKPEAPPPKVPEPPKevvpekkvSMVPPKRPEAPPAKVPEASKEVVPEKKVSVAPKKKPEAPAVKVPEAPKK 10985
Cdd:PRK07003    434 ATADRGDDAADGDAPVPAKANAR--------ASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPA 505
                           170       180       190
                    ....*....|....*....|....*....|.
gi 1958765569 10986 VVPEKKVPvAAPKKPEAPAAEVPEVPKAAVP 11016
Cdd:PRK07003    506 AVPDARAP-AAASREDAPAAAAPPAPEARPP 535
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
27781-27868 2.33e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.92  E-value: 2.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27781 PEIDLDVALRTSVIAKAGEdvqLLIPFK--GRPPPTVTWRKDEKNLGSDARYSIqnTDSSSlLVIPQVTRNDTGKYILTI 27858
Cdd:cd04969       1 PDFELNPVKKKILAAKGGD---VIIECKpkASPKPTISWSKGTELLTNSSRICI--LPDGS-LKIKNVTKSDEGKYTCFA 74
                            90
                    ....*....|
gi 1958765569 27859 ENGVGQPKSS 27868
Cdd:cd04969      75 VNFFGKANST 84
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8804-8886 2.35e-06

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 50.96  E-value: 2.35e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8804 EPLKVTV--GDSASLQCQLAGTPEIGVSWYKGDtklRPTTTCKMHFKN-NVATLVFTQVDSNDSGEYICRAENSVGEVSS 8880
Cdd:cd20952       5 GPQNQTVavGGTVVLNCQATGEPVPTISWLKDG---VPLLGKDERITTlENGSLQIKGAEKSDTGEYTCVALNLSGEATW 81

                    ....*.
gi 1958765569  8881 STFLTV 8886
Cdd:cd20952      82 SAVLDV 87
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
900-989 2.40e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 51.25  E-value: 2.40e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIE-SSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRpDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8047-8137 2.41e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 2.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8047 PPFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNyKMTLVENTATLTVLKVAKGDAGQYTCYASNVA 8126
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  8127 GKDSCSAQLGV 8137
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
29956-30046 2.42e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 51.01  E-value: 2.42e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29956 PDLELADDLKKTVIIR-AGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQ 30034
Cdd:cd05856       1 PRFTQPAKMRRRVIARpVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSNR 80
                            90
                    ....*....|..
gi 1958765569 30035 SGKKSATVLVKV 30046
Cdd:cd05856      81 AGEINATYKVDV 92
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
33079-33163 2.43e-06

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 51.01  E-value: 2.43e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33079 PRSITVHEGESARFSCDTDGEPVPTVTWLR-GGQVVSTSARHqvttaKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQ 33157
Cdd:cd04968       8 PADTYALKGQTVTLECFALGNPVPQIKWRKvDGSPSSQWEIT-----TSEPVLEIPNVQFEDEGTYECEAENSRGKDTVQ 82

                    ....*.
gi 1958765569 33158 FTLTVQ 33163
Cdd:cd04968      83 GRIIVQ 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
1417-1507 2.43e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.85  E-value: 2.43e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKC-LEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVikEDGTqsLIIVPALPSDSGEWTVVAQNR 1495
Cdd:cd20978       1 PKFIQKPEKNVVvKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATV--EDGT--LTIINVQPEDTGYYGCVATNE 76
                            90
                    ....*....|..
gi 1958765569  1496 AGKSTISVTLTV 1507
Cdd:cd20978      77 IGDIYTETLLHV 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7107-7196 2.48e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.85  E-value: 2.48e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFdIKPVSIDVIA--GESADFECHVTGAQPMRVTWSKDNKEI-RPGGNYTITcvGNTphLRILKVGKGDSGQYTCQATN 7183
Cdd:cd20978       1 PKF-IQKPEKNVVVkgGQDVTLPCQVTGVPQPKITWLHNGKPLqGPMERATVE--DGT--LTIINVQPEDTGYYGCVATN 75
                            90
                    ....*....|...
gi 1958765569  7184 DVGKDMCSAQLSV 7196
Cdd:cd20978      76 EIGDIYTETLLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1680-1751 2.48e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.41  E-value: 2.48e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  1680 AHFECRLTpiGDPTMVVEWLHDGKPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSAT 1751
Cdd:cd00096       1 VTLTCSAS--GNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Titin_Z pfam09042
Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like ...
463-505 2.48e-06

Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. This interaction is essential for sarcomere assembly.


Pssm-ID: 462662  Cd Length: 43  Bit Score: 49.50  E-value: 2.48e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958765569   463 QKQMRKEAEKTAVTKVVVAADKAKEQELRLRTREEIITKQEQT 505
Cdd:pfam09042     1 QEKVREEDEKTAVSTVVVAVDKAKVLEPVSKSEEEIAAEQEQE 43
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
19817-19898 2.50e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 51.08  E-value: 2.50e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDS-TPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATL 88

                    ...
gi 1958765569 19896 KVL 19898
Cdd:cd05763      89 TVL 91
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
16640-16725 2.51e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 50.93  E-value: 2.51e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16640 VEEGTDVNIVAKIKGVPFPTLTWFK-APPKKPDSKEpvvydthVNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTAS 16718
Cdd:cd20975      12 VREGQDVIMSIRVQGEPKPVVSWLRnRQPVRPDQRR-------FAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQ 84

                    ....*..
gi 1958765569 16719 KEMRLNV 16725
Cdd:cd20975      85 CEARLEV 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5700-5787 2.52e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 50.86  E-value: 2.52e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5700 IKKPSPVLVLRnGQSTTFECQVTGTPEIRVSWYLDGNEITDlRRYGIsfvdgLA--TFQISNARVENSGTYVCEARNDAG 5777
Cdd:cd05725       1 VKRPQNQVVLV-DDSAEFQCEVGGDPVPTVRWRKEDGELPK-GRYEI-----LDdhSLKIRKVTAGDMGSYTCVAENMVG 73
                            90
                    ....*....|
gi 1958765569  5778 TASCSIELKV 5787
Cdd:cd05725      74 KIEASATLTV 83
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6072-6162 2.53e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 2.53e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6072 PPSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKyRLVCHENTVSLEVSNLELEDTANYTCKVSNVA 6151
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  6152 GDNACSGILTV 6162
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8703-8793 2.57e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 51.04  E-value: 2.57e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8703 PAIFVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENAS 8782
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  8783 GKDSCSAQILI 8793
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4949-5038 2.63e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.85  E-value: 2.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFT-KPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAAsDRYQIAFVEGTasLEISRVDMNDAGNFTCRATNSV 5027
Cdd:cd20978       1 PKFIqKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG-PMERATVEDGT--LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  5028 GSKDSRGALIV 5038
Cdd:cd20978      78 GDIYTETLLHV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2407-2476 2.65e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.64  E-value: 2.65e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2407 VITPLKDVNVIEGTKAVLECKVSVPDVTSVKWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYK 2476
Cdd:pfam13927     4 ITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYT 73
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
21982-22064 2.65e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.20  E-value: 2.65e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21982 TITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTG--KLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIF 22059
Cdd:cd20974       9 SVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTA 88

                    ....*
gi 1958765569 22060 NVKVL 22064
Cdd:cd20974      89 ELLVL 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4759-4849 2.67e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 51.04  E-value: 2.67e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4759 PPTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEA 4838
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  4839 GSQTSVGELIV 4849
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
9312-9380 2.70e-06

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 50.68  E-value: 2.70e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9312 KVGGDPIPNVKWTKGKWRqLNQGGRILIhqkgDESKLEIRDTTKTDSGLYRCVAFNKHGEIESNVNLQV 9380
Cdd:cd05728      22 KASGNPRPAYRWLKNGQP-LASENRIEV----EAGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9687-9755 2.71e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.41  E-value: 2.71e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9687 ATFECEVSFD-DAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEPRGEARSTA 9755
Cdd:cd00096       1 VTLTCSASGNpPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8610-8691 2.74e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 50.82  E-value: 2.74e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8610 PPSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEA 8689
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  8690 GR 8691
Cdd:cd05747      83 GK 84
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
32306-32396 2.74e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 50.93  E-value: 2.74e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPH--IEIVHEGLdyYALHIRDTLPEDTGYYRVTATN 32383
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRrfAEEAEGGL--CRLRILAAERGDAGFYTCKAVN 78
                            90
                    ....*....|...
gi 1958765569 32384 TAGSTSCQAHLQV 32396
Cdd:cd20975      79 EYGARQCEARLEV 91
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
8048-8127 2.76e-06

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 51.01  E-value: 2.76e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAK--DNRE---IRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYA 8122
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKqvPGKEnliMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTA 80

                    ....*
gi 1958765569  8123 SNVAG 8127
Cdd:cd05765      81 RNSGG 85
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11286-11617 2.77e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 56.32  E-value: 2.77e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11286 PVTKKPEVLPEKVPEAPKKITPEKRESAPVPEEPEAPPAPVEEIPEETIYEEKATITIGRKETPPVEEREIERFIQPEEP 11365
Cdd:NF033839    172 PTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNV 251
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11366 GMEPQPEETPVQEPEPEKKVIEKPKL-----KPRPPI-RAPSPPKEDVKekifqlkavSKKKVPEKPEVVEKVEPTPLKV 11439
Cdd:NF033839    252 NTKVEIENTVHKIFADMDAVVTKFKKgltqdTPKEPGnKKPSAPKPGMQ---------PSPQPEKKEVKPEPETPKPEVK 322
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11440 PTAEKKVrkllPEPKPQPKEEvvlKSVLRKRPEEEEPKVEPKKVEKVKKPEEPPPPPKAVEVEAPPEPKPKERKVPEPTK 11519
Cdd:NF033839    323 PQLEKPK----PEVKPQPEKP---KPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPK 395
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11520 vPEIKPAIPLPGPEPKPKPEPevktmKAPPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKPK-GPIKGVAKKTPSP-IE 11597
Cdd:NF033839    396 -PEVKPQPEKPKPEVKPQPEK-----PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvKPQPETPKPEVKPqPE 469
                           330       340
                    ....*....|....*....|
gi 1958765569 11598 AERKKLRPGSGGEKPPDEAP 11617
Cdd:NF033839    470 KPKPEVKPQPEKPKPDNSKP 489
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
31050-31132 2.79e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 50.71  E-value: 2.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31050 EMADVTTKL----GEAAQLSCQIVGRPLPDIKWYRFGKELvQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGE 31125
Cdd:cd20976       3 SFSSVPKDLeaveGQDFVAQCSARGKPVPRITWIRNAQPL-QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQ 81

                    ....*..
gi 1958765569 31126 VETSSKL 31132
Cdd:cd20976      82 VSCSAWV 88
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
6929-6996 2.81e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 50.49  E-value: 2.81e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6929 GDSVSLQCQVAGTPEITVSWFKgdtKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTA 6996
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIK---LGGELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSA 74
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7869-7945 2.84e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 50.47  E-value: 2.84e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  7869 IGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPaykmqfknnvaSLVINKVDHSDVGEYTCKAENSVGAVASSAVLVI 7945
Cdd:pfam13895    13 EGEPVTLTCSAPGNPPPSYTWYKDGSAISSSP-----------NFFTLSVSAEDSGTYTCVARNGRGGKVSNPVELT 78
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
1037-1127 2.85e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 50.71  E-value: 2.85e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1037 APFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRyKVSYNKQTGEcrLVISMTFADDAGEYTIVIRN 1116
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGE--LHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|.
gi 1958765569  1117 KHGETSASASL 1127
Cdd:cd20976      78 AAGQVSCSAWV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8345-8411 2.90e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.02  E-value: 2.90e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8345 VQLQTTIEGAEPISVAWFKDkGEIVRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKNDAGVQE 8411
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKN-GKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
33078-33162 2.92e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 50.97  E-value: 2.92e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33078 KPRSITVHEGESARFSCDTDGEPVPTVTWLR-GGQVVSTSARHQVTTakYKSTFEISSVQASDEGNYSVVVEN-TDGKQE 33155
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRnGNLIIEFNTRYIVRE--NGTTLTIRNIRRSDMGIYLCIASNgVPGSVE 85

                    ....*..
gi 1958765569 33156 AQFTLTV 33162
Cdd:cd20970      86 KRITLQV 92
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
900-989 2.94e-06

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 50.87  E-value: 2.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   900 PTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDfQITFQ---SGIARLMIREAFAEDSGRFTCSAVN 976
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSD-HYTIQrdlDGTCSLHTTASTLDDDGNYTIMAAN 79
                            90
                    ....*....|...
gi 1958765569   977 EAGTVSTSCYLAV 989
Cdd:cd05893      80 PQGRISCTGRLMV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5884-5973 2.95e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.96  E-value: 2.95e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDS-VATLQVRSVDNGHSGRYTCQAKNES 5962
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  5963 GVERCYAFLLV 5973
Cdd:cd05744      81 GENSFNAELVV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9182-9272 2.96e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.88  E-value: 2.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9182 PVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSD---RCSFSFASGTAVLELKDTAKADSGDYVCKASN 9258
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  9259 VAGSDTSKCKVTIK 9272
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8802-8886 2.97e-06

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 50.48  E-value: 2.97e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8802 QLEP--LKVTVGDSASLQCQLA-GTPEIGVSWYKGDTKLR----PTTTCKMhfknnvATLVFTQVDSNDSGEYICRAENS 8874
Cdd:cd05724       1 RVEPsdTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNldneRVRIVDD------GNLLIAEARKSDEGTYKCVATNM 74
                            90
                    ....*....|...
gi 1958765569  8875 VGE-VSSSTFLTV 8886
Cdd:cd05724      75 VGErESRAARLSV 87
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
12977-13046 2.98e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.96  E-value: 2.98e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 12977 FTKNLANLEVSEGDTIKLVCEVSK-PGAEVTWYKGDEEVIETGRFEILTDGRKRI-LIIQNAQLEDAGSYNC 13046
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSGlPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTC 74
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33245-33315 2.99e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.02  E-value: 2.99e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 33245 AKLTCAVESSAlcAKEVAWYKDGKKLKENGHFQFHYSaDGTYELKIHNLSESDCGEYVCEVSGEGGTSKTS 33315
Cdd:cd00096       1 VTLTCSASGNP--PPTITWYKNGKPLPPSSRDSRRSE-LGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
101-184 2.99e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 50.82  E-value: 2.99e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   101 TAPPNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATN 180
Cdd:cd05747       1 TLPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVEN 80

                    ....
gi 1958765569   181 SVGR 184
Cdd:cd05747      81 SEGK 84
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7573-7666 2.99e-06

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 50.95  E-value: 2.99e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7573 RVVPPSFirklKDTTATLGASVVLECRVS-GSAPISVGWFLDGNEIISSPKCQPSFADNVCT-LTLSSLEPSDTGAYTCV 7650
Cdd:cd20959       3 RIIPFAF----GEGAAQVGMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCH 78
                            90
                    ....*....|....*.
gi 1958765569  7651 AANVAGQDESSALLTV 7666
Cdd:cd20959      79 ARNSAGSASYTAPLTV 94
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7861-7945 3.00e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 50.97  E-value: 3.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7861 PLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEhTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSV-GAVAS 7939
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRN-GNLIIEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGVpGSVEK 86

                    ....*.
gi 1958765569  7940 SAVLVI 7945
Cdd:cd20970      87 RITLQV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
17338-17420 3.01e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 50.67  E-value: 3.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17338 DKLTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTP-TTLALEKTKAKRSDSGRYCVVVENSTGSRKGFC 17416
Cdd:cd05737       9 DVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDV 88

                    ....
gi 1958765569 17417 QVNV 17420
Cdd:cd05737      89 TVSV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
16629-16712 3.01e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.26  E-value: 3.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16629 PPSIELKEF-MEVEEGTDVNIVAKIKGVPFPTLTWFKAPPKKPDSkepvvydTHVNKQVVDDTCTLVIPQSRRSDTGLYS 16707
Cdd:pfam13927     1 KPVITVSPSsVTVREGETVTLTCEATGSPPPTITWYKNGEPISSG-------STRSRSLSGSNSTLTISNVTRSDAGTYT 73

                    ....*
gi 1958765569 16708 ITAVN 16712
Cdd:pfam13927    74 CVASN 78
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7387-7478 3.01e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 50.81  E-value: 3.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7387 PRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDkGEVIRESE--NVRISFVDNIATLQLGSPEASHSGKYVCQIKN 7464
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRD-GQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569  7465 DAGMRECSALLTVL 7478
Cdd:cd20974      80 GSGQATSTAELLVL 93
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8893-8982 3.06e-06

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 50.87  E-value: 3.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGK---PLKDSPNVQTSfLDNIATLNIFKTDRSLAGQYSCTVTN 8969
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKqisPKSDHYTIQRD-LDGTCSLHTTASTLDDDGNYTIMAAN 79
                            90
                    ....*....|...
gi 1958765569  8970 PIGSASSSAKLIL 8982
Cdd:cd05893      80 PQGRISCTGRLMV 92
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
31762-31959 3.07e-06

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 54.97  E-value: 3.07e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31762 KYMIAEDLGRGEFGIVHRCVETSSK-----KTFMAKFVKvKGTDQVLVK---KEISILNIARHRNILYLHESFESMEELV 31833
Cdd:cd05045       1 NLVLGKTLGEGEFGKVVKATAFRLKgragyTTVAVKMLK-ENASSSELRdllSEFNLLKQVNHPHVIKLYGACSQDGPLL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31834 MIFEFI-----------------SGLDIFERINTSAFE------LNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENII 31890
Cdd:cd05045      80 LIVEYAkygslrsflresrkvgpSYLGSDGNRNSSYLDnpderaLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVL 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31891 YQTRKnsIIKIIEFGQARQLKPGDNF--RLLFTAP-EYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPF 31959
Cdd:cd05045     160 VAEGR--KMKISDFGLSRDVYEEDSYvkRSKGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 230
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6269-6349 3.07e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 50.65  E-value: 3.07e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6269 KIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFI-DSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTKV 6347
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDeDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569  6348 IV 6349
Cdd:cd20973      87 TV 88
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
27797-27873 3.08e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.88  E-value: 3.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27797 AGEDVQLLIPFKGRPPPTVTWRKDE---KNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSS-TVSV 27872
Cdd:cd20951      14 EKSDAKLRVEVQGKPDPEVKWYKNGvpiDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSaSVVV 93

                    .
gi 1958765569 27873 K 27873
Cdd:cd20951      94 E 94
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8611-8701 3.08e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.88  E-value: 3.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVP---GARCNVSLQDSVAELELFDVDTSQSGDYTCIVSN 8687
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  8688 EAGRASCTTQLFVK 8701
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5791-5870 3.10e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.47  E-value: 3.10e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5791 PIFIRELEPVEVVKD-SDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSvfyLHITKCAPSDVGEYQCIIANEG 5869
Cdd:cd20978       1 PKFIQKPEKNVVVKGgQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGT---LTIINVQPEDTGYYGCVATNEI 77

                    .
gi 1958765569  5870 G 5870
Cdd:cd20978      78 G 78
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
7112-7196 3.12e-06

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 50.66  E-value: 3.12e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7112 KPVsiDVIAGESAD--FECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNtphLRILKVGKGDSGQYTCQATNDVGKDM 7189
Cdd:cd05723       3 KPS--NIYAHESMDivFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVGNAQ 77

                    ....*..
gi 1958765569  7190 CSAQLSV 7196
Cdd:cd05723      78 ASAQLII 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
3020-3102 3.13e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.57  E-value: 3.13e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3020 FRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRIK-IQKEKYVHRLLIPSARMSDAGKYTVVA----GG 3093
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSgLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIArnraGE 82

                    ....*....
gi 1958765569  3094 NMSTANLFV 3102
Cdd:cd05744      83 NSFNAELVV 91
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
33892-33984 3.14e-06

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 50.99  E-value: 3.14e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIaEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQ--QGRFHIENTDDLTTLIIMDVQKQDGGLYTLSL 33969
Cdd:cd05732       3 PKITYLENQTAV-ELEQITLTCEAEGDPIPEITWRRATRGISFEEGdlDGRIVVRGHARVSSLTLKDVQLTDAGRYDCEA 81
                            90
                    ....*....|....*
gi 1958765569 33970 GNEFGSDSATVNINI 33984
Cdd:cd05732      82 SNRIGGDQQSMYLEV 96
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
31761-31959 3.15e-06

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 55.41  E-value: 3.15e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31761 EKYMIAEDLGRGEFG--IVHRCVETSSKKTFMAKFVKVKGTDQVLVKKEISIL--------NIARHRNILYLHESFESME 31830
Cdd:cd05101      24 DKLTLGKPLGEGCFGqvVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLvsememmkMIGKHKNIINLLGACTQDG 103
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31831 ELVMIFEFISGLDIFERINTS-------AFELNE--------REVVSYVRQVCEALEFLHSQNIGHFDIRPENIIyqTRK 31895
Cdd:cd05101     104 PLYVIVEYASKGNLREYLRARrppgmeySYDINRvpeeqmtfKDLVSCTYQLARGMEYLASQKCIHRDLAARNVL--VTE 181
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31896 NSIIKIIEFGQARQL------KPGDNFRLlftAPEYYAPEVHQHDVVSSATDMWSLGTLVYVLLS-GINPF 31959
Cdd:cd05101     182 NNVMKIADFGLARDInnidyyKKTTNGRL---PVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPY 249
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
31832-31963 3.16e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 56.34  E-value: 3.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31832 LVMifEFISGLDIFERINTSAfELNEREVVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQtrKNSIIKIIEFGQARQLk 31911
Cdd:NF033483     84 IVM--EYVDGRTLKDYIREHG-PLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT--KDGRVKVTDFGIARAL- 157
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31912 pgDNFRLLFTAP-----EYYAPEVHQHDVVSSATDMWSLGTLVYVLLSGINPFLAET 31963
Cdd:NF033483    158 --SSTTMTQTNSvlgtvHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
903-989 3.16e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 50.47  E-value: 3.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   903 VSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSgiarLMIREAFAEDSGRFTCSAVNEAGTVS 982
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILDDHS----LKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569   983 TSCYLAV 989
Cdd:cd05725      77 ASATLTV 83
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
5712-5778 3.17e-06

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 50.18  E-value: 3.17e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5712 GQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDAGT 5778
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGM 67
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
17046-17124 3.18e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.58  E-value: 3.18e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  17046 IVVHAGGVIRIIAYVSGKPPPTVTWNMNERALPQE---ATIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIV 17122
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAEsgrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  17123 DV 17124
Cdd:smart00410    84 TV 85
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7964-8041 3.19e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.54  E-value: 3.19e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7964 TLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLqmsFVHHVATLQILQTDQSHVGQYNCSASNPLGTASSSAKLIL 8041
Cdd:cd04969      15 AKGGDVIIECKPKASPKPTISWSKGTELLTNSSRI---CILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
22659-22749 3.21e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 50.66  E-value: 3.21e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22659 PPAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSA 22738
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569 22739 GEATETLNVIV 22749
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
19817-19897 3.22e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 50.87  E-value: 3.22e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRN-LCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:cd20990      10 LTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENgVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLEL 89

                    ..
gi 1958765569 19896 KV 19897
Cdd:cd20990      90 VV 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8797-8886 3.25e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 50.87  E-value: 3.25e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNN-VATLVFTQVDSNDSGEYICRAENSV 8875
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENgVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  8876 GEVSSSTFLTV 8886
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
18428-18510 3.25e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.57  E-value: 3.25e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18428 DVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLP-RVELQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd05744       8 GDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRAGENSFNA 87

                    ....
gi 1958765569 18507 IVNV 18510
Cdd:cd05744      88 ELVV 91
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
6914-7001 3.26e-06

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 50.70  E-value: 3.26e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6914 PPYFVTELEPLEASvgdsvsLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNvatLVFNKVGINDSGEYTCVAENSI 6993
Cdd:cd20968       5 PPTNVTIIEGLKAV------LPCTTMGNPKPSVSWIKGDDLIKENNRIAVLESGS---LRIHNVQKEDAGQYRCVAKNSL 75

                    ....*...
gi 1958765569  6994 GTAASKTV 7001
Cdd:cd20968      76 GIAYSKPV 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6636-6726 3.30e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.88  E-value: 3.30e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6636 PSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKI---VSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAAN 6712
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  6713 VAGSDECRALLTVQ 6726
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
4303-4381 3.32e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 50.62  E-value: 3.32e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4303 VALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKC---SIRSSNYISSLEilrtQVV--DCGEYTCKASNEYGSVSCTA 4377
Cdd:cd05857      16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIggyKVRNQHWSLIME----SVVpsDKGNYTCVVENEYGSINHTY 91

                    ....
gi 1958765569  4378 TLTV 4381
Cdd:cd05857      92 HLDV 95
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
8051-8137 3.34e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 50.58  E-value: 3.34e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8051 DLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGgNYKMTLVENTATLTVLKVAKGDAGQYTCYASN-VAGKD 8129
Cdd:cd20970       6 PQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEF-NTRYIVRENGTTLTIRNIRRSDMGIYLCIASNgVPGSV 84

                    ....*...
gi 1958765569  8130 SCSAQLGV 8137
Cdd:cd20970      85 EKRITLQV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1439-1504 3.36e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.02  E-value: 3.36e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1439 KVVGRPMPETFWFHNGQQIVNDYTHKVVIkEDGTQSLIIVPALPSDSGEWTVVAQNRAGKSTISVT 1504
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRS-ELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
29564-29649 3.41e-06

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 50.57  E-value: 3.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29564 LQGDL-VTIRAGSDLVLDAAVGGKPEPKIIWTK-GDKELDLCEKVSLQYTGkraTAVIKYCDRSDSGKYTLTVKNASGTK 29641
Cdd:cd20952       3 LQGPQnQTVAVGGTVVLNCQATGEPVPTISWLKdGVPLLGKDERITTLENG---SLQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569 29642 SVSVMVKV 29649
Cdd:cd20952      80 TWSAVLDV 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6541-6629 3.42e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 50.81  E-value: 3.42e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6541 VIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKL--LTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNV 6618
Cdd:cd20974       2 VFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVisTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|.
gi 1958765569  6619 GKSSCTAVVDV 6629
Cdd:cd20974      82 GQATSTAELLV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8327-8418 3.42e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 50.71  E-value: 3.42e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8327 PPQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIVRESDNIwiSHSENVATLHFSRAEPANAGKYTCQIKND 8406
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRS--TCEAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  8407 AGVQECYATLSV 8418
Cdd:cd20976      79 AGQVSCSAWVTV 90
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
20519-20584 3.45e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.54  E-value: 3.45e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 20519 KGKPAPSVSWKKGEDPLATDTRVSVEStavNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKV 20584
Cdd:cd04969      27 KASPKPTISWSKGTELLTNSSRICILP---DGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
6359-6435 3.46e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 50.27  E-value: 3.46e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6359 PPVVETLKNTEVSLECELS-GTPPFEVVWYKDKRQLRSSKKYKIASKN-FHASIHILNVDSTDIGEYHCKAQNEVGSDT 6435
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRtTQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
104-193 3.49e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.47  E-value: 3.49e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVR-QGSQARLQVRVTGIPTPVVKFYRDGAEIQSSL-DFQISQegdlYSLLIAEAYPEDSGTYSVNATNS 181
Cdd:cd20978       1 PKFIQKPEKNVVVkGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMeRATVED----GTLTIINVQPEDTGYYGCVATNE 76
                            90
                    ....*....|..
gi 1958765569   182 VGRATSTADLLV 193
Cdd:cd20978      77 IGDIYTETLLHV 88
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7977-8039 3.49e-06

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 50.57  E-value: 3.49e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  7977 GSEPLQVSWYKDGQLLKDDSNLQMSFV-HHVATLQILQTDQSHVGQYNCSASNPLGTASSSAKL 8039
Cdd:cd20959      29 GDLPLNIRWTLDGQPISDDLGITVSRLgRRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPL 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8141-8218 3.51e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.57  E-value: 3.51e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8141 PRFIKKLdQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDS-VAILEMHNLSVEDSGDYTCEARN 8218
Cdd:cd05744       1 PHFLQAP-GDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARN 78
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
4400-4467 3.54e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 50.63  E-value: 3.54e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4400 VGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRitDADNKHSLELSNLTVQDRGVYSCKASNKFGA 4467
Cdd:cd05856      18 VGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGE--NKKKKWTLSLKNLKPEDSGKYTCHVSNRAGE 83
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
6554-6619 3.54e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 50.72  E-value: 3.54e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6554 GETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVG 6619
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
25228-25310 3.54e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.20  E-value: 3.54e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  25228 VIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPIT 25307
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  25308 VKV 25310
Cdd:smart00410    83 LTV 85
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
8615-8690 3.58e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 50.58  E-value: 3.58e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8615 QKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARcNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAG 8690
Cdd:cd20970       7 QPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTTLTIRNIRRSDMGIYLCIASNGVP 81
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
1255-1337 3.62e-06

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 50.57  E-value: 3.62e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1255 NYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIR-RGERyqMDFLQDGraSLRIPVVLPEDEGIYTAFASNIKGNAICSG 1333
Cdd:cd20952       8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLgKDER--ITTLENG--SLQIKGAEKSDTGEYTCVALNLSGEATWSA 83

                    ....
gi 1958765569  1334 KLYV 1337
Cdd:cd20952      84 VLDV 87
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
14908-14986 3.62e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.54  E-value: 3.62e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14908 IVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDhisAHLEVPKSVHADAGVYTITLENKLGSA--TASIN 14985
Cdd:cd04969      12 ILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPD---GSLKIKNVTKSDEGKYTCFAVNFFGKAnsTGSLS 88

                    .
gi 1958765569 14986 V 14986
Cdd:cd04969      89 V 89
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
6259-6349 3.62e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 50.54  E-value: 3.62e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEASKIVKaGDSARLECKITGSPEIRVVWYRNEHELTASdkyqmtfIDSVAVMQMNS---------LGTEDSGD 6329
Cdd:cd05892       1 PMFIQKPQNKKVLE-GDPVRLECQISAIPPPQIFWKKNNEMLQYN-------TDRISLYQDNCgriclliqnANKKDAGW 72
                            90       100
                    ....*....|....*....|
gi 1958765569  6330 FICEAQNPAGSTSCSTKVIV 6349
Cdd:cd05892      73 YTVSAVNEAGVVSCNARLDV 92
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
8989-9068 3.68e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 50.58  E-value: 3.68e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVV--GESADLECHVTGT-QPIkVTWAKDNREIRSGgNYQISYLENSAHLTIVKVDKGDSGQYTCYAIN 9065
Cdd:cd20970       1 PVISTPQPSFTVTAreGENATFMCRAEGSpEPE-ISWTRNGNLIIEF-NTRYIVRENGTTLTIRNIRRSDMGIYLCIASN 78

                    ...
gi 1958765569  9066 EVG 9068
Cdd:cd20970      79 GVP 81
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
917-988 3.69e-06

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 49.87  E-value: 3.69e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569   917 VTLECHISGYPSPKVTWYREDYQIESSIDFQITfQSGIarLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLA 988
Cdd:cd05746       1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHIS-PEGY--LAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
5975-6057 3.69e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 50.68  E-value: 3.69e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5975 EPAQIIEKAKSVDVTEKdpVTLECVVAGTPELKVKWLKDGKQIVP-SRYFSMSFENNVASFRIQSVMKQDSGQYTFKVEN 6053
Cdd:cd05729       5 DTEKMEEREHALPAANK--VRLECGAGGNPMPNITWLKDGKEFKKeHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVEN 82

                    ....
gi 1958765569  6054 DFGS 6057
Cdd:cd05729      83 EYGS 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
26706-26773 3.73e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.26  E-value: 3.73e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26706 KTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDST--DSRTSLTIENANRNDSGKYTLTIQN 26773
Cdd:pfam13927     9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSlsGSNSTLTISNVTRSDAGTYTCVASN 78
PTZ00121 PTZ00121
MAEBL; Provisional
10032-10566 3.74e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 3.74e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10032 RRMEEEKV--QVTKVPEVSKKIVPQKPSRTPVQEEIIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKKTVTE 10109
Cdd:PTZ00121   1296 KKAEEKKKadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10110 EKIHVAVSKKIEPPPKVPEPPKKPVPEEVVPVPIPKKVEPPAVKVPEAPKKPvpEEKKPVPIPKKEPAAPPKVPEAPKKP 10189
Cdd:PTZ00121   1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA--EEKKKADEAKKKAEEAKKADEAKKKA 1453
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10190 apEEKTAVPVAKKKEAPPPKVTEVQKKVVTEEKITIIPQREESPPPAVPEIPKK----------KVPEEKRPVPRKEEVP 10259
Cdd:PTZ00121   1454 --EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAaeakkkadeaKKAEEAKKADEAKKAE 1531
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10260 PPKAPPKKPVPEEVVPVPIPKKAPPRAEVSKKTVVEEKKfAAEERLSMAVpQRVELMRHEEEEWTYSEEEEQVSVSVYRE 10339
Cdd:PTZ00121   1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK-KAEEDKNMAL-RKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10340 EERDEEEAEITEYEVLEEPEEYVVEEKLHVISKRVEVEPAKVPEKHEKKIIPRPKVPAKIEEPPPTKVPEPPKKMVPEKK 10419
Cdd:PTZ00121   1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10420 VPAPPPKKVPPAKAPEEPKKPVPERRVPAEVV-EIEEPPPTKVTE------------KHMKITQEEKVLVAVTKKEEPPR 10486
Cdd:PTZ00121   1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELkKAEEENKIKAEEakkeaeedkkkaEEAKKDEEEKKKIAHLKKEEEKK 1769
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10487 ARVPEEPKKVVPEEKFPKLKPRREEEPPAKV------TEVRKRAVKEEKVSIEVPKR-EPRPTKEVTVTeekKWSYTREE 10559
Cdd:PTZ00121   1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIkdifdnFANIIEGGKEGNLVINDSKEmEDSAIKEVADS---KNMQLEEA 1846

                    ....*..
gi 1958765569 10560 ETVLEHR 10566
Cdd:PTZ00121   1847 DAFEKHK 1853
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
12975-13044 3.77e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 50.54  E-value: 3.77e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 12975 AVFTKNLANLEVSEGDTIKLVCEVSK-PGAEVTWYKGDEEV-IETGRFEILTDGRKRI-LIIQNAQLEDAGSY 13044
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAiPPPQIFWKKNNEMLqYNTDRISLYQDNCGRIcLLIQNANKKDAGWY 73
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
26997-27078 3.79e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 50.22  E-value: 3.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26997 TVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATM-RFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTFIN 27075
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                    ...
gi 1958765569 27076 IIV 27078
Cdd:cd05894      84 VKV 86
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
1040-1122 3.80e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 50.41  E-value: 3.80e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1040 FISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGEcrLVISMTFADDAGEYTIVIRNKHG 1119
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADG--LLINKVTQDDTGEYTCRAYQVNS 79

                    ...
gi 1958765569  1120 ETS 1122
Cdd:cd20949      80 IAS 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
20896-20971 3.81e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 50.27  E-value: 3.81e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 20896 IKDGLTVKAGDSIVLSAISILGKPLPKSSWSKAGK-DIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFG 20971
Cdd:pfam00047     2 APPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGtLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGG 78
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
5988-6066 3.82e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 50.55  E-value: 3.82e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5988 VTEKDPVTLECVVAGTPELKVKWLKDGKQIVP-SRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRV 6066
Cdd:cd20975      12 VREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPdQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQCEARLEV 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
4970-5031 3.83e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 50.41  E-value: 3.83e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  4970 CKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKD 5031
Cdd:cd20949      21 CEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
33698-33787 3.84e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.54  E-value: 3.84e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQP--RSQNINEGQNVLFSCEISGEPSPEIEWFKNnlpISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNF 33775
Cdd:cd04969       1 PDFELNPvkKKILAAKGGDVIIECKPKASPKPTISWSKG---TELLTNSSRICILPDGSLKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569 33776 RGQCSATASLTV 33787
Cdd:cd04969      78 FGKANSTGSLSV 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
3577-3667 3.87e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 50.66  E-value: 3.87e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIiHNPDGSGTFIVNDPQRGDSGLYICKAENLW 3656
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQI-HQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  3657 GTSTCTAELLV 3667
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7774-7844 3.87e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 50.28  E-value: 3.87e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  7774 VETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEAGQD 7844
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEK 74
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
14206-14292 3.87e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.57  E-value: 3.87e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14206 VKLLAGLTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRIT-IENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRA 14284
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGEN 83

                    ....*...
gi 1958765569 14285 TAVVEVNV 14292
Cdd:cd05744      84 SFNAELVV 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
5136-5215 3.91e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 50.41  E-value: 3.91e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5136 TFTEKLEPSQLlKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAG 5215
Cdd:cd20949       1 TFTENAYVTTV-KEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
14199-14292 3.93e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 50.33  E-value: 3.93e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14199 APEIfldVKLLAGLTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQ-RITIEnvPKKSTVTITDSKRSDTGTYIIEA 14277
Cdd:cd20976       1 APSF---SSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAdRSTCE--AGVGELHIQDVLPEDHGTYTCLA 75
                            90
                    ....*....|....*
gi 1958765569 14278 VNVCGRATAVVEVNV 14292
Cdd:cd20976      76 KNAAGQVSCSAWVTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
23759-23827 3.93e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 3.93e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 23759 LKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAI 23827
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
8234-8316 3.94e-06

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 50.77  E-value: 3.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8234 PPVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYK-------DKRELRSGKKYKIMSENlltSIHILNVDTADIGEYQ 8306
Cdd:cd20954       1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYDPNVRILPNG---TLVFGHVQKENEGHYL 77
                            90
                    ....*....|
gi 1958765569  8307 CKATNDVGSD 8316
Cdd:cd20954      78 CEAKNGIGSG 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
30248-30327 3.96e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.87  E-value: 3.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30248 PTIdlsTMPQKTIHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKN 30327
Cdd:pfam13927     2 PVI---TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
33441-33507 3.98e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 50.70  E-value: 3.98e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 33441 GEPQPTVTWTKDGKAIAQ-SSKYKLSNDKEEFIleILKTETSDGGLYSCTVANSAGSVSSSCKLTIKA 33507
Cdd:cd05730      29 GFPEPTMTWTKDGEPIESgEEKYSFNEDGSEMT--ILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFA 94
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
6166-6257 3.98e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 50.34  E-value: 3.98e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6166 PSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTNDVG 6245
Cdd:cd05736       1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
                            90
                    ....*....|..
gi 1958765569  6246 SDSCTTMLLVTE 6257
Cdd:cd05736      81 VDEDISSLFVED 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
31442-31531 3.99e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 50.41  E-value: 3.99e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31442 FKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEI---IADGLKYRVQEFKggyhqLIIASVTDDDATVYQVRATN 31518
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPIsasVADMSKYRILADG-----LLINKVTQDDTGEYTCRAYQ 76
                            90
                    ....*....|...
gi 1958765569 31519 QGGSVSGTASLEV 31531
Cdd:cd20949      77 VNSIASDMQERTV 89
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7490-7570 4.00e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 50.27  E-value: 4.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7490 MTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSrhHITFVRN---LASLKIPSAEMNDKGLYSFEVENSVGKSSCTV 7566
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESR--RFQIDQDedgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSA 84

                    ....
gi 1958765569  7567 SVHV 7570
Cdd:cd20973      85 ELTV 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2845-2927 4.00e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 50.27  E-value: 4.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2845 TKTMRNIEVPETKAASFECEVSHFNVPS-MWLKNGVEIEMSEKFKIVVQGK-LHQLIIMNTSTEDSAEYTFVCGNDQVSA 2922
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEvKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*
gi 1958765569  2923 TLTVT 2927
Cdd:cd20973      81 TCSAE 85
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
31063-31132 4.03e-06

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 49.87  E-value: 4.03e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31063 QLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGrthTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:cd05746       2 QIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEG---YLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
33422-33505 4.04e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.47  E-value: 4.04e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33422 LRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSS-KYKLsndkEEFILEILKTETSDGGLYSCTVANSAGSVSSS 33500
Cdd:cd20978       8 EKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMeRATV----EDGTLTIINVQPEDTGYYGCVATNEIGDIYTE 83

                    ....*
gi 1958765569 33501 CKLTI 33505
Cdd:cd20978      84 TLLHV 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4770-4849 4.06e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 49.90  E-value: 4.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4770 TALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEAGSQTSVGELIV 4849
Cdd:cd05748       3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
3305-3391 4.07e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.57  E-value: 4.07e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3305 PAIVTPLQDAVTSEGRPARFQCQVSGTDL-KVSWYCRDKKIKP-SRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAV 3382
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTpDLFWQLNGKPVRPdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                    ....*....
gi 1958765569  3383 GQVSSTATL 3391
Cdd:cd05744      81 GENSFNAEL 89
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
33079-33163 4.10e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 50.34  E-value: 4.10e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33079 PRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQF 33158
Cdd:cd05736       7 PEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDIS 86

                    ....*
gi 1958765569 33159 TLTVQ 33163
Cdd:cd05736      87 SLFVE 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6-97 4.10e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 50.48  E-value: 4.10e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPGVQISfSDGRARLMIPAVTKANSGRYSLRATNG 85
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVR-ENGVHSLIIEPVTSRDAGIYTCIATNR 79
                            90
                    ....*....|..
gi 1958765569    86 SGQATSTAELLV 97
Cdd:cd20990      80 AGQNSFNLELVV 91
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
33894-33984 4.11e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 50.28  E-value: 4.11e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33894 IEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEqqgRFHIE-NTDDLTTLIIMDVQKQDGGLYTLSLGNE 33972
Cdd:cd05737       4 LGGLPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLD---HCNLKvEAGRTVYFTINGVSSEDSGKYGLVVKNK 80
                            90
                    ....*....|..
gi 1958765569 33973 FGSDSATVNINI 33984
Cdd:cd05737      81 YGSETSDVTVSV 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7011-7098 4.11e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.15  E-value: 4.11e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQ--LKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRddENLQMSFVDNvATLKILQTDLSHSGQYSCSASNP 7088
Cdd:cd04969       1 PDFELNpvKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLT--NSSRICILPD-GSLKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|
gi 1958765569  7089 LGTASSTARL 7098
Cdd:cd04969      78 FGKANSTGSL 87
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
4573-4659 4.16e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 50.54  E-value: 4.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4573 PSFVKKVDPSYLmLPGESARLHCKLKGSPVIQVTWFKNNkELSESNTVRMSFA--NSEAI-LDITDVKVDDSGTYSCEAT 4649
Cdd:cd05892       1 PMFIQKPQNKKV-LEGDPVRLECQISAIPPPQIFWKKNN-EMLQYNTDRISLYqdNCGRIcLLIQNANKKDAGWYTVSAV 78
                            90
                    ....*....|
gi 1958765569  4650 NDAGSDSCST 4659
Cdd:cd05892      79 NEAGVVSCNA 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5053-5132 4.19e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 49.90  E-value: 4.19e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5053 VLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVAGSVecSANLFVK 5132
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEK--SATINVK 81
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
6549-6629 4.20e-06

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 50.29  E-value: 4.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6549 MTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYN-KISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVV 6627
Cdd:cd05891      11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTV 90

                    ..
gi 1958765569  6628 DV 6629
Cdd:cd05891      91 SV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6635-6725 4.20e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 50.33  E-value: 4.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6635 PPSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKI-VSGAKYQTtfSDNVCTLQLNSLDSSDMGSYTCVAANV 6713
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTC--EAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  6714 AGSDECRALLTV 6725
Cdd:cd20976      79 AGQVSCSAWVTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
23880-24117 4.21e-06

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 56.11  E-value: 4.21e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23880 TVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENRYGQSFALESEPivaqypYKEPGPPGTPFVTAVSKDS--------- 23950
Cdd:COG4733     477 AVWAFGPDELETQLFRVVSIEENEDGTYTITAVQHAPEKYAAIDAG------AFDDVPPQWPPVNVTTSESlsvvaqgta 550
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23951 ---MVVQWhepinNGGSPVIGYHLE-RKERNSilWTKVNKTiiHDTQFKALNLEEGiEYEFRVYAENIVGV-GKASKNSE 24025
Cdd:COG4733     551 vttLTVSW-----DAPAGAVAYEVEwRRDDGN--WVSVPRT--SGTSFEVPGIYAG-DYEVRVRAINALGVsSAWAASSE 620
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24026 CYVARDPcDPPGTPEAIIVKRN--EITLQWTKPVYDGGSMItgyivEKRDLPEGRWMKASFTNVIETQ--FTVSGLTEDQ 24101
Cdd:COG4733     621 TTVTGKT-APPPAPTGLTATGGlgGITLSWSFPVDADTLRT-----EIRYSTTGDWASATVAQALYPGntYTLAGLKAGQ 694
                           250
                    ....*....|....*.
gi 1958765569 24102 RYEFRVIAKNAAGAIS 24117
Cdd:COG4733     695 TYYYRARAVDRSGNVS 710
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
24834-24913 4.23e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 50.28  E-value: 4.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24834 SVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVE-ETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVI 24912
Cdd:cd05737      12 TIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKvEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVS 91

                    .
gi 1958765569 24913 V 24913
Cdd:cd05737      92 V 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4667-4752 4.27e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.19  E-value: 4.27e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4667 PSFIKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKT-FVFLEITSFNSADIGDYECVVANEV 4745
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80

                    ....*..
gi 1958765569  4746 GKCGCVA 4752
Cdd:cd05744      81 GENSFNA 87
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
8048-8137 4.28e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.15  E-value: 4.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPV--SVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGnyKMTLVENtATLTVLKVAKGDAGQYTCYASNV 8125
Cdd:cd04969       1 PDFELNPVkkKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS--RICILPD-GSLKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569  8126 AGKDSCSAQLGV 8137
Cdd:cd04969      78 FGKANSTGSLSV 89
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12351-12427 4.29e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.50  E-value: 4.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12351 PLIFITPLSDvKVFEKDEAKFECEVSREPK-TFRWLKGTQEI--AGDDR-FELIKDGTRHSLVIKSAAFEDEAKYMFEAE 12426
Cdd:cd20951       1 PEFIIRLQSH-TVWEKSDAKLRVEVQGKPDpEVKWYKNGVPIdpSSIPGkYKIESEYGVHVLHIRRVTVEDSAVYSAVAK 79

                    .
gi 1958765569 12427 D 12427
Cdd:cd20951      80 N 80
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
14214-14290 4.32e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.15  E-value: 4.32e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 14214 VKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIenVPKKsTVTITDSKRSDTGTYIIEAVNVCGRA--TAVVEV 14290
Cdd:cd04969      14 AAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICI--LPDG-SLKIKNVTKSDEGKYTCFAVNFFGKAnsTGSLSV 89
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
12986-13063 4.32e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 50.09  E-value: 4.32e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12986 VSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIETGRFeiltdgrkrilIIQNAQLEDAGSYNCRLPSSRTDGKVKVHELA 13063
Cdd:pfam13895    11 VTEGEPVTLTCSAPgNPPPSYTWYKDGSAISSSPNF-----------FTLSVSAEDSGTYTCVARNGRGGKVSNPVELT 78
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
5142-5226 4.36e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 50.10  E-value: 4.36e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5142 EPSQLLKKGDATQLVCKVTGTPPIKITWFandRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTS 5221
Cdd:cd05731       2 ESSTMVLRGGVLLLECIAEGLPTPDIRWI---KLGGELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTI 78

                    ....*
gi 1958765569  5222 IVIVK 5226
Cdd:cd05731      79 SVTVE 83
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
1251-1338 4.37e-06

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 50.41  E-value: 4.37e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1251 IRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDflqdgRASLRIPVVLPEDEGIYTAFASNIKGNAI 1330
Cdd:cd05851       6 VKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMS-----GAVLKIFNIQPEDEGTYECEAENIKGKDK 80

                    ....*...
gi 1958765569  1331 CSGKLYVE 1338
Cdd:cd05851      81 HQARVYVQ 88
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
6553-6629 4.43e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 50.24  E-value: 4.43e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6553 VGETCSLECKVAGTPELSVEWYKDGKLLTS-----SQKHKFsfynkisSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVV 6627
Cdd:cd05856      18 VGSSVRLKCVASGNPRPDITWLKDNKPLTPpeigeNKKKKW-------TLSLKNLKPEDSGKYTCHVSNRAGEINATYKV 90

                    ..
gi 1958765569  6628 DV 6629
Cdd:cd05856      91 DV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
21296-21376 4.44e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.20  E-value: 4.44e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21296 RTLVVRAGLSIRIFVPIKGRPAPEVTWTKDN---INLKHRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFV 21372
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgklLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  21373 NVRV 21376
Cdd:smart00410    82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
27977-28058 4.45e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 4.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27977 PIRDLSMKDSTKTSVVLSWTKPdFDGGSIITDYLVERKGKG-EQAWSHAGISK-TCEIEIGQLKEQSVLEFRVSARNEKG 28054
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNsGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                    ....
gi 1958765569 28055 QSDP 28058
Cdd:pfam00041    81 EGPP 84
fn3 pfam00041
Fibronectin type III domain;
27884-27962 4.54e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 4.54e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27884 LQVKHVSLGTVTLLWDPPLiDGGSPIINYVIEKRDATK----RTWSIVSHKcsgTSFKVMDLSEKTPFFFRVLAENEIGI 27959
Cdd:pfam00041     6 LTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSgepwNEITVPGTT---TSVTLTGLKPGTEYEVRVQAVNGGGE 81

                    ...
gi 1958765569 27960 GEP 27962
Cdd:pfam00041    82 GPP 84
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
7305-7374 4.58e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 50.10  E-value: 4.58e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7305 ALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKvtsKNFDTSLHIFNLEAPDIGEYHCKATNEVGS 7374
Cdd:cd05731       7 VLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKF---ENFNKTLKIENVSEADSGEYQCTASNTMGS 73
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
7579-7666 4.63e-06

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 49.91  E-value: 4.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7579 FIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADnvctLTLSSLEPSDTGAYTCVAANVAGQD 7658
Cdd:cd05728       2 WLKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTI 77

                    ....*...
gi 1958765569  7659 ESSALLTV 7666
Cdd:cd05728      78 YASAELAV 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
3025-3090 4.63e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 50.43  E-value: 4.63e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  3025 KDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVV 3090
Cdd:cd05747      11 RSLTVSEGESARFSCDVDgEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVV 77
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
32331-32386 4.66e-06

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 50.09  E-value: 4.66e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32331 GIPAPTLKWEKDGQPLSL-GPHIEIVHEGldyyALHIRDTLPEDTGYYRVTATNTAG 32386
Cdd:cd05724      24 GHPEPTVSWRKDGQPLNLdNERVRIVDDG----NLLIAEARKSDEGTYKCVATNMVG 76
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
29962-30039 4.66e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.19  E-value: 4.66e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29962 DDLKktviIRAGASLRLMVSVSGRPSPVITWSKKG----IDLANRAIIDNTESYSLLIVDkVNRYDAGKYTIEAENQSGK 30037
Cdd:cd05744       8 GDLE----VQEGRLCRFDCKVSGLPTPDLFWQLNGkpvrPDSAHKMLVRENGRHSLIIEP-VTKRDAGIYTCIARNRAGE 82

                    ..
gi 1958765569 30038 KS 30039
Cdd:cd05744      83 NS 84
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
3199-3288 4.67e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 50.43  E-value: 4.67e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLST----GFKCKFLHDGQEYTllLIEAFPEDAAVYTCEAK 3274
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTstlpGVQISFSDGRAKLS--IPAVTKANSGRYSLTAT 78
                            90
                    ....*....|....
gi 1958765569  3275 NDYGVATTSASLSV 3288
Cdd:cd20974      79 NGSGQATSTAELLV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
33229-33306 4.72e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.87  E-value: 4.72e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33229 PPKITQSLKAEASR--DIAKLTCAVESSAlcAKEVAWYKDGKKLKENGHfQFHYSADGTYELKIHNLSESDCGEYVCEVS 33306
Cdd:pfam13927     1 KPVITVSPSSVTVRegETVTLTCEATGSP--PPTITWYKNGEPISSGST-RSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33909-33980 4.78e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 4.78e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 33909 LTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENTddlTTLIIMDVQKQDGGLYTLSLGNEF-GSDSATV 33980
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGN---GTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8328-8419 4.81e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 50.43  E-value: 4.81e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8328 PQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEI-VRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKND 8406
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIsTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  8407 AGVQECYATLSVL 8419
Cdd:cd20974      81 SGQATSTAELLVL 93
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
14909-14988 4.83e-06

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 50.20  E-value: 4.83e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14909 VVIEGEKLSIPVPFRAV-PVPTVSWHKDGKEVKA--SDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASIN 14985
Cdd:cd05750      10 TVQEGSKLVLKCEATSEnPSPRYRWFKDGKELNRkrPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGN 89

                    ...
gi 1958765569 14986 VKV 14988
Cdd:cd05750      90 VTV 92
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
7573-7668 4.84e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 50.34  E-value: 4.84e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7573 RVVPPSFIRKLKDTTAtlgasvvLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAA 7652
Cdd:cd05736       4 RVYPEFQAKEPGVEAS-------LRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAK 76
                            90
                    ....*....|....*.
gi 1958765569  7653 NVAGQDESSALLTVQE 7668
Cdd:cd05736      77 NEGGVDEDISSLFVED 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8703-8784 4.86e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 50.43  E-value: 4.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8703 PAIFVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENAS 8782
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  8783 GK 8784
Cdd:cd05747      83 GK 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
32101-32164 4.87e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 4.87e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 32101 CKIENYdQSTQVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSS 32164
Cdd:cd00096       5 CSASGN-PPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7859-7941 4.89e-06

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 50.09  E-value: 4.89e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7859 IEPLEhVEAAIGEPTTLQCKVD-GTPEIRISWYKEHTKLRSA-PAYKMQFKNNvasLVINKVDHSDVGEYTCKAENSVGA 7936
Cdd:cd05724       2 VEPSD-TQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDnERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGE 77

                    ....*
gi 1958765569  7937 VASSA 7941
Cdd:cd05724      78 RESRA 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12814-12871 4.97e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 4.97e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12814 AVLECEVS-RENAKVKWFKNGTEILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAK 12871
Cdd:cd00096       1 VTLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
8061-8137 4.98e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 50.32  E-value: 4.98e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8061 LGESGSFKCHVTGTAPIKITWAKDNREIRPGGNyKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQLGV 8137
Cdd:cd05730      17 LGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8997-9078 4.99e-06

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 50.19  E-value: 4.99e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8997 PVDAVVGESAD--LECHVTGTQPIKVTWAKDNREIRsGGNYQISYLENSAhLTIVKVDKGDSGQYTCYAINEVGKDSCTA 9074
Cdd:cd20952       6 PQNQTVAVGGTvvLNCQATGEPVPTISWLKDGVPLL-GKDERITTLENGS-LQIKGAEKSDTGEYTCVALNLSGEATWSA 83

                    ....
gi 1958765569  9075 QLNI 9078
Cdd:cd20952      84 VLDV 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
19817-19897 5.00e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.88  E-value: 5.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRN-LCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569 19896 KV 19897
Cdd:cd20973      87 TV 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
33072-33162 5.06e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.94  E-value: 5.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33072 AARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHqVTTAKYKSTFEISSVQASDEGNYSVVVENTD 33151
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADR-STCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569 33152 GKQEAQFTLTV 33162
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
6926-6996 5.08e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 50.32  E-value: 5.08e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  6926 ASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEyRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTA 6996
Cdd:cd05730      15 ANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQ 84
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
5139-5218 5.09e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 49.93  E-value: 5.09e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5139 EKLEPSQLLKKGDATQLVCKVTGtPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDH 5218
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFE 79
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
18428-18510 5.10e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.08  E-value: 5.10e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18428 DVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDlprVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:cd20978       9 KNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED---GTLTIINVQPEDTGYYGCVATNEIGDIYTETL 85

                    ...
gi 1958765569 18508 VNV 18510
Cdd:cd20978      86 LHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
15928-15996 5.12e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 5.12e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 15928 VNIPADVTGLPMPKIEWSKNEKVIEkptdalNITKEEVSRSEAKTELSIPKAVREDKGTYTITASNRLG 15996
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLP------PSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12894-12960 5.14e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 5.14e-06
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  12894 DLQVKEKETARFECEIS-KENVKVQWFKDGAE-IKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEVR 12960
Cdd:smart00410     3 SVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAT 71
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
26995-27078 5.14e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 5.14e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26995 SHTVYVRAGSNLKVDIPISGKPLPKVTLSRDG-VPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTF 27073
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  27074 INIIV 27078
Cdd:smart00410    81 TTLTV 85
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
4588-4656 5.14e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 50.02  E-value: 5.14e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDS 4656
Cdd:cd20949      14 GQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
33704-33787 5.14e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 50.28  E-value: 5.14e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33704 PRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMY-TLEIRNASVSDSGKYTVKAKNFRGqcSAT 33782
Cdd:cd05737       8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTvYFTINGVSSEDSGKYGLVVKNKYG--SET 85

                    ....*
gi 1958765569 33783 ASLTV 33787
Cdd:cd05737      86 SDVTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2038-2115 5.21e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.87  E-value: 5.21e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIeRSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAIN 2115
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPI-SSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
7952-8037 5.29e-06

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 50.16  E-value: 5.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQ--TDQSHVGQYNCSASNP 8029
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQLIIasVTDDDATVYQVRATNQ 81

                    ....*...
gi 1958765569  8030 LGTASSSA 8037
Cdd:cd20971      82 GGSVSGTA 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
3019-3102 5.34e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 50.27  E-value: 5.34e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3019 EFRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVA----GG 3093
Cdd:cd20972       3 QFIQKLRSQEVAEGSKVRLECRVTgNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLAtnsvGS 82

                    ....*....
gi 1958765569  3094 NMSTANLFV 3102
Cdd:cd20972      83 DTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
15726-15792 5.36e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 49.72  E-value: 5.36e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 15726 LLNWSdPADDGGSEITGFIIERKDA-KMHTWR-QPIETERSKCDITGLIEGQEYKFRVIAKNKFGCGPP 15792
Cdd:pfam00041    17 TVSWT-PPPDGNGPITGYEVEYRPKnSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
16889-17305 5.38e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.78  E-value: 5.38e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16889 GVSYKVTGLIEGSDYQFRVYAINAAGVGPaslPSDPVTARDPVAPPGPPFP-KVTDWTKSSVDLEWSPPLKDGgskITGY 16967
Cdd:COG3401     191 TLVDGGGDIEPGTTYYYRVAATDTGGESA---PSNEVSVTTPTTPPSAPTGlTATADTPGSVTLSWDPVTESD---ATGY 264
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16968 IVEYKEEGKEEWEKGkdKEVRGTKLVVTGLKEGAFYKFRVRAVNiaGVGEPGEVTDIIEmkdriVSPDlqldasvrdriv 17047
Cdd:COG3401     265 RVYRSNSGDGPFTKV--ATVTTTSYTDTGLTNGTTYYYRVTAVD--AAGNESAPSNVVS-----VTTD------------ 323
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17048 vhaggviriiayvsgKPPPTVtwnmneralPQEATIETTaisssmvikncqrshqgvysllakneggerkktiivdvldv 17127
Cdd:COG3401     324 ---------------LTPPAA---------PSGLTATAV----------------------------------------- 338
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17128 pgpvgipflsdnlTNDSCKLTWFSPEDdggSPITNYVIQKREADRRAWTPVTYTVTRQNATVQGLIQGKSYFFRIAAENS 17207
Cdd:COG3401     339 -------------GSSSITLSWTASSD---ADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDA 402
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17208 IGMG----PFVETPNALVIRDPITVPERPEDLEVKEVTKNTVTLTWNPPKYDGGSEIINYVLESRLIGTEKFH---KVTN 17280
Cdd:COG3401     403 AGNEsapsEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSStvtATTT 482
                           410       420
                    ....*....|....*....|....*
gi 1958765569 17281 DNLLSRKYTVKGLKEGDTYEYRVSA 17305
Cdd:COG3401     483 DTTTANLSVTTGSLVGGSGASSVTN 507
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5511-5600 5.41e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.08  E-value: 5.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRK-MDSIKGSFIDLECIVAGSHPISIQWFKDDQEISAsDKYKFSFHDNTafLEISQLEGTDSGTYTCSATNKA 5589
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG-PMERATVEDGT--LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  5590 GHSQCSGHLTV 5600
Cdd:cd20978      78 GDIYTETLLHV 88
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
4306-4381 5.43e-06

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 49.55  E-value: 5.43e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4306 GHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSnyiSSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTV 4381
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS---GTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
104-193 5.45e-06

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 50.16  E-value: 5.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSlDFQISQEGDL---YSLLIAEAYPEDSGTYSVNATN 180
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIAD-GLKYRIQEFKggyHQLIIASVTDDDATVYQVRATN 80
                            90
                    ....*....|...
gi 1958765569   181 SVGRATSTADLLV 193
Cdd:cd20971      81 QGGSVSGTASLEV 93
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
33698-33787 5.51e-06

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 50.24  E-value: 5.51e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKN-----NLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKA 33772
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQvpgkeNLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTA 80
                            90
                    ....*....|....*
gi 1958765569 33773 KNFRGQCSATASLTV 33787
Cdd:cd05765      81 RNSGGLLRANFPLSV 95
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7107-7196 5.52e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 50.15  E-value: 5.52e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRIL--KVGKGDSGQYTCQATND 7184
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLLiqNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  7185 VGKDMCSAQLSV 7196
Cdd:cd05892      81 AGVVSCNARLDV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
1051-1127 5.53e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 49.89  E-value: 5.53e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1051 EGGSVVFECQI-GGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECRLVISMTFaDDAGEYTIVIRNKHGETSASASL 1127
Cdd:pfam00047    10 EGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTK-EDAGTYTCVVNNPGGSATLSTSL 86
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
20214-20295 5.60e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 49.84  E-value: 5.60e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20214 TLILRAGVTMRLYVPVKGRPPPKITWSK---PNVNLRERIGLDiKSTDFDTFLrCENVNKYDAGKYILTLENSCGKKEYT 20290
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRgdkAFTATEGRVRVE-SYKDLSSFV-IEGAEREDEGVYTITVTNPVGEDHAS 81

                    ....*
gi 1958765569 20291 IVVKV 20295
Cdd:cd05894      82 LFVKV 86
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2844-2926 5.70e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.11  E-value: 5.70e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2844 ITKTMRNIEVPETKAASFECEVSHFNVPSM-WLKNGVEIEMSE---KFKIVVQGKLHQLIIMNTSTEDSAEYTFVCGND- 2918
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVkWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIh 82
                            90
                    ....*....|.
gi 1958765569  2919 ---QVSATLTV 2926
Cdd:cd20951      83 geaSSSASVVV 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5883-5973 5.72e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.89  E-value: 5.72e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5883 PPSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNES 5962
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  5963 GVERCYAFLLV 5973
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
5800-5868 5.72e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 49.55  E-value: 5.72e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5800 VEVVKDSDVELECEVMGTTPfEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQCIIANE 5868
Cdd:cd20967       7 VQVSKGHKIRLTVELADPDA-EVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGE 74
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6367-6443 5.75e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.11  E-value: 5.75e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6367 NTEVSLECELSGTPPFEVVWYKDKRQLRSSK---KYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVGSDTCICAIKLK 6443
Cdd:cd20951      15 KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVVE 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
21587-21667 5.78e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 5.78e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21587 VIARAGDNIKVEIPVLGRPKPTVTWKK-GDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITI 21665
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  21666 QV 21667
Cdd:smart00410    84 TV 85
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
8428-8511 5.79e-06

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 49.91  E-value: 5.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8428 PESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFN-KVSGLKIISVAPGDSGVYSFEVQNPVGKDSCT 8506
Cdd:cd05891       8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYSINVKNKYGGETVD 87

                    ....*
gi 1958765569  8507 VSIQV 8511
Cdd:cd05891      88 VTVSV 92
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
31546-31630 5.83e-06

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 49.87  E-value: 5.83e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31546 MGAVHALRGEVVSIKIPFSGKPDPVITWQK-GQDLIDNngHYQvivtrsftsLVFPNG------VERK-DAGFYVVCAKN 31617
Cdd:cd20958       7 MGNLTAVAGQTLRLHCPVAGYPISSITWEKdGRRLPLN--HRQ---------RVFPNGtlvienVQRSsDEGEYTCTARN 75
                            90
                    ....*....|....
gi 1958765569 31618 RFG-IDQKTVELDV 31630
Cdd:cd20958      76 QQGqSASRSVFVKV 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
23052-23132 5.86e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.49  E-value: 5.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23052 PPRISMDPKykdTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAK 23131
Cdd:pfam13927     1 KPVITVSPS---SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 23132 N 23132
Cdd:pfam13927    78 N 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
27402-27470 5.87e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.25  E-value: 5.87e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27402 VKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRN-AMGSASATI 27470
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
33416-33505 5.90e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.80  E-value: 5.90e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDKEEFILEILKTETS-DGGLYSCTVANSA 33494
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKrDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569 33495 GSVSSSCKLTI 33505
Cdd:cd05744      81 GENSFNAELVV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8423-8511 5.91e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 50.04  E-value: 5.91e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8423 TIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGK--ELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd20974       2 VFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|.
gi 1958765569  8501 GKDSCTVSIQV 8511
Cdd:cd20974      82 GQATSTAELLV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
17340-17413 5.91e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 50.05  E-value: 5.91e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 17340 LTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRK 17413
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQE 86
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
30655-30736 5.94e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 49.84  E-value: 5.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30655 QEGVFVRQGGVIRLTIPIKGKPFPICKWTKEGQ---DVSKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVY 30731
Cdd:cd05894       2 ENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKaftATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS 81

                    ....*
gi 1958765569 30732 IKVKV 30736
Cdd:cd05894      82 LFVKV 86
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
4486-4573 5.99e-06

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 50.24  E-value: 5.99e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4486 LEPVQSAIN--KKIHLECQVDEDRKVSIT--WSKDGQKL----PAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNE 4557
Cdd:cd04970       7 LAPSNADITvgENATLQCHASHDPTLDLTftWSFNGVPIdlekIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTV 86
                            90
                    ....*....|....*.
gi 1958765569  4558 AGSSSSSATVAVREPP 4573
Cdd:cd04970      87 VDSDSASATLVVRGPP 102
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7855-7944 6.00e-06

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 49.87  E-value: 6.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7855 PPyFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLrsaPAYKMQ--FKNnvASLVINKVDH-SDVGEYTCKAE 7931
Cdd:cd20958       1 PP-FIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRL---PLNHRQrvFPN--GTLVIENVQRsSDEGEYTCTAR 74
                            90
                    ....*....|...
gi 1958765569  7932 NSVGAVASSAVLV 7944
Cdd:cd20958      75 NQQGQSASRSVFV 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
27382-27461 6.03e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.49  E-value: 6.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27382 PVIDLPLEYTEVVkyrAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRN 27461
Cdd:pfam13927     2 PVITVSPSSVTVR---EGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
26397-26480 6.03e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 49.72  E-value: 6.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26397 PPAGPLEINGLTAEKCSLSWGRPqEDGGADIDYYIVEKRETSRL-AWTICEAELRTTSCKVTKLLKGNEYIFRVTGVNKY 26475
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                    ....*
gi 1958765569 26476 GVGEP 26480
Cdd:pfam00041    80 GEGPP 84
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
8423-8501 6.10e-06

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 50.24  E-value: 6.10e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8423 TIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKIS--FFNKVSGLKIISVAPG-----DSGVYSFE 8495
Cdd:cd07693       2 RIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRShrIVLPSGSLFFLRVVHGrkgrsDEGVYVCV 81

                    ....*.
gi 1958765569  8496 VQNPVG 8501
Cdd:cd07693      82 AHNSLG 87
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
29561-29842 6.15e-06

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 55.72  E-value: 6.15e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29561 DARLQGDLVTIRAGSDLVLDAAVGGKPEPKIIWTKG--DKELDLCEKVSLQYTGK---RATAV----IKYcDRSDSG-KY 29630
Cdd:COG4733     447 DGTSVARTVQSVAGRTLTVSTAYSETPEAGAVWAFGpdELETQLFRVVSIEENEDgtyTITAVqhapEKY-AAIDAGaFD 525
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29631 TLTVKNASGTKSVSVMVKVLDSPGPCGKLTVSrvteekctlaWSLPQEDGGAEITHyiveRRETSrlNWVIVeAECLTLS 29710
Cdd:COG4733     526 DVPPQWPPVNVTTSESLSVVAQGTAVTTLTVS----------WDAPAGAVAYEVEW----RRDDG--NWVSV-PRTSGTS 588
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29711 YVVtRLIKNNEYTFRVRAVNKYG-LGVPIESEPIVARNSFTIPSQP-GIPegVGAGKEHIIIQWTKPESD---------- 29778
Cdd:COG4733     589 FEV-PGIYAGDYEVRVRAINALGvSSAWAASSETTVTGKTAPPPAPtGLT--ATGGLGGITLSWSFPVDAdtlrteirys 665
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 29779 GGNEISNYLVDKREKKSLRWTrvnkdyvvydtrlkVTSLMEGCDYQFRVTAVNSAGNSEPSEAS 29842
Cdd:COG4733     666 TTGDWASATVAQALYPGNTYT--------------LAGLKAGQTYYYRARAVDRSGNVSAWWVS 715
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
4486-4573 6.16e-06

Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 409440  Cd Length: 102  Bit Score: 50.43  E-value: 6.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4486 LEPVQSAIN--KKIHLECQVDED--RKVSITWSKDGQKL----PAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNE 4557
Cdd:cd05854       7 LAPSSADINqgENLTLQCHASHDptMDLTFTWSLDDFPIdldkPNGHYRRMEVKETIGDLVIVNAQLSHAGTYTCTAQTV 86
                            90
                    ....*....|....*.
gi 1958765569  4558 AGSSSSSATVAVREPP 4573
Cdd:cd05854      87 VDSASASATLVVRGPP 102
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6824-6907 6.25e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.80  E-value: 6.25e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6824 FVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCI-LEILTSTKGDAGHYSCEIENEAGR 6902
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRAGE 82

                    ....*
gi 1958765569  6903 DSCDA 6907
Cdd:cd05744      83 NSFNA 87
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
19817-19897 6.31e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.80  E-value: 6.31e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRN-LCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:cd05744      10 LEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAEL 89

                    ..
gi 1958765569 19896 KV 19897
Cdd:cd05744      90 VV 91
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
8798-8886 6.32e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 49.77  E-value: 6.32e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8798 YFVKQLEPlkVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTtcKMHFKNNvATLVFTQVDSNDSGEYICRAENSVGE 8877
Cdd:cd04969       6 NPVKKKIL--AAKGGDVIIECKPKASPKPTISWSKGTELLTNSS--RICILPD-GSLKIKNVTKSDEGKYTCFAVNFFGK 80

                    ....*....
gi 1958765569  8878 VSSSTFLTV 8886
Cdd:cd04969      81 ANSTGSLSV 89
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
29973-30047 6.35e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 49.93  E-value: 6.35e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 29973 GASLRLMVSVSGRPSPVITWSKKG--IDLANRAIIDNTESySLLIVDKVNRYDAGKYTIEAENQSGKKSATVLVKVY 30047
Cdd:cd05730      18 GQSVTLACDADGFPEPTMTWTKDGepIESGEEKYSFNEDG-SEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVF 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1533-1602 6.41e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.25  E-value: 6.41e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1533 LEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGTKGEaaLKIDSTISQDSAWYTATAINKAGRDTTR 1602
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGT--LTISNVTLEDSGTYTCVASNSAGGSASA 68
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2412-2490 6.43e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 6.43e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2412 KDVNVIEGTKAVLECKVSVPDVTSVKWYLNDEQ-IKPDDRVQSIVKGTKQRLVINRTHASDEGPYKLMV----GRVETSC 2486
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSGT 81

                     ....
gi 1958765569   2487 NLSV 2490
Cdd:smart00410    82 TLTV 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
22160-22364 6.46e-06

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 55.72  E-value: 6.46e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22160 AVDPYGPPDPPKNPEVTT--------ITKDSMVVCWghpdsDGGSEIINYIVERRDKAGqRWVkcNKKALTDLRFKVSGL 22231
Cdd:COG4733     523 AFDDVPPQWPPVNVTTSEslsvvaqgTAVTTLTVSW-----DAPAGAVAYEVEWRRDDG-NWV--SVPRTSGTSFEVPGI 594
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22232 TEGhEYEFRIMAENAAGVSAPSATSPFYkacDSVFKPGPPGNPRVLDTSRS--SISIAWNKPIydgGSEITGYmvEIALP 22309
Cdd:COG4733     595 YAG-DYEVRVRAINALGVSSAWAASSET---TVTGKTAPPPAPTGLTATGGlgGITLSWSFPV---DADTLRT--EIRYS 665
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 22310 EEDEWQVVT-PPAGLKATSYTITNLIENQEYKIRIYAMNSEGLGEPALVPGTPKAE 22364
Cdd:COG4733     666 TTGDWASATvAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASAD 721
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
28485-28561 6.47e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.11  E-value: 6.47e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28485 GDSLRIKALVQGRPVPRVTWFKDGVEIERRM---NMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEITVKVQ 28561
Cdd:cd20951      15 KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVVE 94
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
6927-6999 6.47e-06

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 50.24  E-value: 6.47e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6927 SVGDSVSLQCQVAGTPEITVSWFKG----DTKLRSTPEYRTYFTNnvATLVFNKV-----GINDSGEYTCVAENSIGTAA 6997
Cdd:cd07693      13 SKGDPATLNCKAEGRPTPTIQWLKNgqplETDKDDPRSHRIVLPS--GSLFFLRVvhgrkGRSDEGVYVCVAHNSLGEAV 90

                    ..
gi 1958765569  6998 SK 6999
Cdd:cd07693      91 SR 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
12704-12782 6.52e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.49  E-value: 6.52e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12704 KPRVIGllrPLKDVTVTAGETATFDCELSYEDIP-VEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAK 12782
Cdd:pfam13927     1 KPVITV---SPSSVTVREGETVTLTCEATGSPPPtITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
33705-33787 6.54e-06

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 49.82  E-value: 6.54e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33705 RSQNINEGQNVLFSCEISGE-PSPEIEWFKN--NLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQCSA 33781
Cdd:cd05750       7 KSQTVQEGSKLVLKCEATSEnPSPRYRWFKDgkELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTV 86

                    ....*.
gi 1958765569 33782 TASLTV 33787
Cdd:cd05750      87 TGNVTV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
7199-7292 6.61e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 49.93  E-value: 6.61e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7199 PPKF-IKKLDTSKVAKQGESIQLECKISGSPEIKVVWFRNDSELhESWKYNMSFVNSVALLTINEASVEDTGDYICEAHN 7277
Cdd:cd05730       1 PPTIrARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPI-ESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAEN 79
                            90
                    ....*....|....*
gi 1958765569  7278 GVGHASCSTALKVKA 7292
Cdd:cd05730      80 KAGEQEAEIHLKVFA 94
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6639-6725 6.64e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.88  E-value: 6.64e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6639 TRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTF-SDNVCTLQLNSLDSSDMGSYTCVAANVAGSD 6717
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  6718 ECRALLTV 6725
Cdd:cd20973      81 TCSAELTV 88
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
8703-8791 6.69e-06

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 49.70  E-value: 6.69e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8703 PAIFVKRLND-YSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENA 8781
Cdd:cd20969       1 RAAIRDRKAQqVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANA 80
                            90
                    ....*....|
gi 1958765569  8782 SGKDSCSAQI 8791
Cdd:cd20969      81 GGNDSMPAHL 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4949-5039 6.86e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 49.73  E-value: 6.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEI---AASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATN 5025
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  5026 SVGSKDSRGALIVQ 5039
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5414-5512 6.88e-06

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 49.95  E-value: 6.88e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5414 PATITEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDV 5493
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*....
gi 1958765569  5494 GRSSCKASINVLDLIIPPS 5512
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPPA 99
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
902-980 6.89e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 49.90  E-value: 6.89e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   902 LVSGLKNV-TVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSG-IARLMIREAFAEDSGRFTCSAVNEAG 979
Cdd:cd05737       3 VLGGLPDVvTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGrTVYFTINGVSSEDSGKYGLVVKNKYG 82

                    .
gi 1958765569   980 T 980
Cdd:cd05737      83 S 83
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
26708-26786 6.90e-06

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 49.91  E-value: 6.90e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26708 LTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLR-TRAYIDSTDSR--TSLTIENANRNDSGKYTLTIQNVLSAASMTFVV 26784
Cdd:cd05891      11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIElSEHYSVKLEQGkyASLTIKGVTSEDSGKYSINVKNKYGGETVDVTV 90

                    ..
gi 1958765569 26785 KV 26786
Cdd:cd05891      91 SV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
18723-18795 6.91e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 49.66  E-value: 6.91e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 18723 LTVKAGDTIRLEAGVRGKPFPEVAWTKDkdATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAG 18795
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMRE--GQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
904-984 6.92e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 49.50  E-value: 6.92e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   904 SGLKNVTVVEGESVTLECHIS-GYPSPKVTWYRED-YQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTV 981
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGgTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                    ...
gi 1958765569   982 STS 984
Cdd:pfam00047    81 TLS 83
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
8993-9085 6.93e-06

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 50.24  E-value: 6.93e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8993 IPLAP--VDAVVGESADLECHVT--GTQPIKVTWAKDNREI---RSGGNYQISY-LENSAHLTIVKVDKGDSGQYTCYAI 9064
Cdd:cd04970       5 ITLAPsnADITVGENATLQCHAShdPTLDLTFTWSFNGVPIdleKIEGHYRRRYgKDSNGDLEIVNAQLKHAGRYTCTAQ 84
                            90       100
                    ....*....|....*....|.
gi 1958765569  9065 NEVGKDSCTAQLNIKerlTPP 9085
Cdd:cd04970      85 TVVDSDSASATLVVR---GPP 102
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
7575-7665 7.05e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 49.66  E-value: 7.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7575 VPPSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANV 7654
Cdd:cd05747       2 LPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENS 81
                            90
                    ....*....|.
gi 1958765569  7655 AGQDESSALLT 7665
Cdd:cd05747      82 EGKQEAQFTLT 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9003-9079 7.13e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 49.73  E-value: 7.13e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9003 GESADLECHVTGTQPIKVTWAKDNREIRS---GGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLNIK 9079
Cdd:cd20951      15 KSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVVE 94
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
13-97 7.18e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 49.32  E-value: 7.18e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    13 QSVVVLEGSAATFEAHISGSPVPEVSWFRDGqvistSTLPgvqisfsDGRAR------LMIPAVTKANSGRYSLRATNGS 86
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKED-----GELP-------KGRYEilddhsLKIRKVTAGDMGSYTCVAENMV 72
                            90
                    ....*....|.
gi 1958765569    87 GQATSTAELLV 97
Cdd:cd05725      73 GKIEASATLTV 83
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6914-7000 7.19e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 7.19e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6914 PPYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEyRTYFTNNVATLVFNKVGINDSGEYTCVAENSI 6993
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79

                    ....*..
gi 1958765569  6994 GTAASKT 7000
Cdd:cd20976      80 GQVSCSA 86
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
19813-19897 7.24e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 49.91  E-value: 7.24e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19813 MKSLLTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNL-CTLELFSVNRKDSGDYTITAENSSGSKSA 19891
Cdd:cd05729      10 EEREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKgWSLIIERAIPRDKGKYTCIVENEYGSINH 89

                    ....*.
gi 1958765569 19892 TIKLKV 19897
Cdd:cd05729      90 TYDVDV 95
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
31446-31531 7.25e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.50  E-value: 7.25e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31446 LRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIaDGLKYRVQEFKGGYHQLIIASVTDDDATVYQVRATNQGGSVSG 31525
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIV-ESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATC 82

                    ....*.
gi 1958765569 31526 TASLEV 31531
Cdd:cd20973      83 SAELTV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
23742-23818 7.26e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.10  E-value: 7.26e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 23742 PDVRPAFSSYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVAN 23818
Cdd:pfam13927     2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4963-5038 7.37e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 49.71  E-value: 7.37e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4963 GGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVE-GTASLEISRVDMNDAGNFTCRATNSVGSKDSRGALIV 5038
Cdd:cd20990      15 GKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVREnGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVV 91
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
7858-7945 7.40e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 49.54  E-value: 7.40e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7858 FIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEH-TKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGA 7936
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81

                    ....*....
gi 1958765569  7937 VASSAVLVI 7945
Cdd:cd05763      82 ISANATLTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6549-6629 7.40e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.50  E-value: 7.40e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6549 MTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNK-ISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVV 6627
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569  6628 DV 6629
Cdd:cd20973      87 TV 88
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
33711-33774 7.44e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.81  E-value: 7.44e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 33711 EGQNVLFSCEISGEPSPEIEWFKN-NLPISISSNISVSRSRNMytLEIRNASVSDSGKYTVKAKN 33774
Cdd:cd20970      16 EGENATFMCRAEGSPEPEISWTRNgNLIIEFNTRYIVRENGTT--LTIRNIRRSDMGIYLCIASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13342-13419 7.45e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.43  E-value: 7.45e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13342 EDQTVTEFDDAVFSCQLS-REKANVKWYRNGRE-IKEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVE----DRKSRA 13415
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATnssgSASSGT 81

                     ....
gi 1958765569  13416 RLFV 13419
Cdd:smart00410    82 TLTV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8234-8324 7.48e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 7.48e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8234 PPVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKyKIMSENLLTSIHILNVDTADIGEYQCKATNDV 8313
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  8314 GSDTCVGSVTL 8324
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33898-33975 7.52e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 49.95  E-value: 7.52e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRI-----QSQEQQGRFHIENTDDLTtliIMDVQKQDGGLYTLSLGNE 33972
Cdd:cd05726       6 PRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNllfpyQPPQPSSRFSVSPTGDLT---ITNVQRSDVGYYICQALNV 82

                    ...
gi 1958765569 33973 FGS 33975
Cdd:cd05726      83 AGS 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7391-7477 7.54e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.50  E-value: 7.54e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7391 KKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDkGEVIRESENVRISF-VDNIATLQLGSPEASHSGKYVCQIKNDAGMR 7469
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKD-DNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  7470 ECSALLTV 7477
Cdd:cd20973      81 TCSAELTV 88
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6650-6724 7.55e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 49.66  E-value: 7.55e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6650 GTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLT 6724
Cdd:cd05747      18 GESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTLT 92
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
7113-7200 7.57e-06

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 49.86  E-value: 7.57e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7113 PVSIDVIAGESADFECHVTGAQPMRVT--WSKDNKEI---RPGGNYT----ITCVGNtphLRILKVGKGDSGQYTCQATN 7183
Cdd:cd04970       9 PSNADITVGENATLQCHASHDPTLDLTftWSFNGVPIdleKIEGHYRrrygKDSNGD---LEIVNAQLKHAGRYTCTAQT 85
                            90
                    ....*....|....*..
gi 1958765569  7184 DVGKDMCSAQLSVKEPP 7200
Cdd:cd04970      86 VVDSDSASATLVVRGPP 102
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
6925-6999 7.57e-06

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 49.82  E-value: 7.57e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6925 EASVGDSVSLQCQ-VAGTPEITVSWFKGDTKLRSTPEYRTYFTNN--VATLVFNKVGINDSGEYTCVAENSIGTAASK 6999
Cdd:cd05750      10 TVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENILGKDTVT 87
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
4949-5038 7.61e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 49.38  E-value: 7.61e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTK-PLRNVDSV-VGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRyqIAFVEgTASLEISRVDMNDAGNFTCRATNS 5026
Cdd:cd04969       1 PDFELnPVKKKILAaKGGDVIIECKPKASPKPTISWSKGTELLTNSSR--ICILP-DGSLKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569  5027 VGSKDSRGALIV 5038
Cdd:cd04969      78 FGKANSTGSLSV 89
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8518-8607 7.61e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 49.77  E-value: 7.61e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVnMLEDA---DAGDYTCIATN 8594
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICL-LIQNAnkkDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569  8595 VAGSDECSAPLTV 8607
Cdd:cd05892      80 EAGVVSCNARLDV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
20505-20584 7.61e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.66  E-value: 7.61e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20505 LAKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDT--RVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSI 20582
Cdd:cd20974      11 VVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAEL 90

                    ..
gi 1958765569 20583 KV 20584
Cdd:cd20974      91 LV 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8802-8886 7.62e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 49.32  E-value: 7.62e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8802 QLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTtckmhfknnvaTLVFTQVDSNDSGEYICRAENS-VGEVSS 8880
Cdd:pfam13895     5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSP-----------NFFTLSVSAEDSGTYTCVARNGrGGKVSN 73

                    ....*.
gi 1958765569  8881 STFLTV 8886
Cdd:pfam13895    74 PVELTV 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
14916-14984 7.65e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.86  E-value: 7.65e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 14916 LSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASI 14984
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
14206-14292 7.66e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.50  E-value: 7.66e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14206 VKLLAGLTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRAT 14285
Cdd:cd20972       5 IQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDT 84

                    ....*..
gi 1958765569 14286 AVVEVNV 14292
Cdd:cd20972      85 TSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
24155-24220 7.72e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.86  E-value: 7.72e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 24155 FRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKS 24220
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
6650-6725 7.74e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.81  E-value: 7.74e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  6650 GTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVcTLQLNSLDSSDMGSYTCVAAN-VAGSDECRALLTV 6725
Cdd:cd20970      17 GENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGT-TLTIRNIRRSDMGIYLCIASNgVPGSVEKRITLQV 92
PTZ00121 PTZ00121
MAEBL; Provisional
433-679 7.75e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 7.75e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   433 DMARVREPVISAVEQTAQRTTTTAVHVQPAQKQMRKEAEKTAVTKVVVAADKAKEQ---------ELRLRTREEIITKQE 503
Cdd:PTZ00121   1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieevmklyEEEKKMKAEEAKKAE 1616
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   504 QTHIAHEQIRKETEkafVPKVVISATKAKEQETRITGEITTKQEQKRITQETITK----ETRKTVVPKVIVATPKIKEQD 579
Cdd:PTZ00121   1617 EAKIKAEELKKAEE---EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEA 1693
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   580 VVSRSREAitTKRDQVQITQEKKRKETE----TTALSTIAVATTKAKEQETVLRSREAMTTRQEHIQVTHGKVGVGKKAE 655
Cdd:PTZ00121   1694 LKKEAEEA--KKAEELKKKEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
                           250       260
                    ....*....|....*....|....
gi 1958765569   656 AVATVVAAVDQARVREPREPRHVE 679
Cdd:PTZ00121   1772 EIRKEKEAVIEEELDEEDEKRRME 1795
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
26299-26381 7.81e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.81  E-value: 7.81e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26299 PRIMMDVKFRDVIVVKaGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDsNTTLTVKDCVRRDTGQYVLTLKN 26378
Cdd:cd20970       1 PVISTPQPSFTVTARE-GENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVREN-GTTLTIRNIRRSDMGIYLCIASN 78

                    ...
gi 1958765569 26379 VAG 26381
Cdd:cd20970      79 GVP 81
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
5252-5318 7.84e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.50  E-value: 7.84e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5252 VAGTPPFEITWFKDNTTLRSGRKYKtFIQDQ--LVSLQILKFVASDAGEYQCRVTNEVGSSTCSARVTL 5318
Cdd:cd20973      21 VEGYPDPEVKWMKDDNPIVESRRFQ-IDQDEdgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7111-7196 7.89e-06

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 49.32  E-value: 7.89e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7111 IKPVSIDVIAGESADFEChvtgaQPMR------VTWSKDNKEIRPGGN-YTITCVGNtphLRILKVGKGDSGQYTCQATN 7183
Cdd:cd05724       2 VEPSDTQVAVGEMAVLEC-----SPPRghpeptVSWRKDGQPLNLDNErVRIVDDGN---LLIAEARKSDEGTYKCVATN 73
                            90
                    ....*....|....
gi 1958765569  7184 DVG-KDMCSAQLSV 7196
Cdd:cd05724      74 MVGeRESRAARLSV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
7021-7099 7.91e-06

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 49.42  E-value: 7.91e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7021 EQTVGLPVT--LTCRLNGSAPIHVCWYRDGVLLRDdENLQMSFVDNvATLKILQTDLSHSGQYSCSASNPLGTASSTARL 7098
Cdd:cd20952       8 NQTVAVGGTvvLNCQATGEPVPTISWLKDGVPLLG-KDERITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVL 85

                    .
gi 1958765569  7099 T 7099
Cdd:cd20952      86 D 86
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8237-8315 7.92e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 49.54  E-value: 7.92e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8237 FRKKPFPVETLKGADVHLECELQGTPPFQVSWYKD-------KRELRsgkkYKIMSEnlLTSIHILNVDTADIGEYQCKA 8309
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDggtdfpaARERR----MHVMPE--DDVFFIVDVKIEDTGVYSCTA 75

                    ....*.
gi 1958765569  8310 TNDVGS 8315
Cdd:cd05763      76 QNSAGS 81
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
31054-31121 7.97e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 49.64  E-value: 7.97e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31054 VTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATN 31121
Cdd:cd20949       9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQ 76
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5887-5963 8.08e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 49.32  E-value: 8.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5887 IKKIENVTTVLKSSATFQSTVAGSPPISITWLKDD--------QILEENdnvhisfedsvaTLQVRSVDNGHSGRYTCQA 5958
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDgelpkgryEILDDH------------SLKIRKVTAGDMGSYTCVA 68

                    ....*
gi 1958765569  5959 KNESG 5963
Cdd:cd05725      69 ENMVG 73
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7576-7666 8.08e-06

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 49.87  E-value: 8.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7576 PPSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQ-----PSFADNVCTLTLSSLEPSDTGAYTCV 7650
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRvgdyvTSDGDVVSYVNISSVRVEDGGEYTCT 80
                            90
                    ....*....|....*.
gi 1958765569  7651 AANVAGQDESSALLTV 7666
Cdd:cd20956      81 ATNDVGSVSHSARINV 96
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
9002-9078 8.10e-06

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 49.43  E-value: 8.10e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9002 VGESADLECHVTGTQP-IKVTWAKDNREIRSGGNYQISYLEN--SAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLNI 9078
Cdd:cd05750      13 EGSKLVLKCEATSENPsPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1679-1755 8.17e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 49.73  E-value: 8.17e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1679 PAHFECRLTpiGDPTMVVEWLHDGKPLEAAN---RLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIVK 1755
Cdd:cd20951      17 DAKLRVEVQ--GKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVVE 94
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
3461-3550 8.21e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 49.71  E-value: 8.21e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNN-HSLIILFTRFQDEGEYTCMASNEY 3539
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGvHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  3540 GRAVCSAHLKV 3550
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
21296-21377 8.23e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.66  E-value: 8.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21296 RTLVVRAGLSIRIFVPIKGRPAPEVTWTKD----NINLKHRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGF 21371
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDgqviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*.
gi 1958765569 21372 VNVRVL 21377
Cdd:cd20974      88 AELLVL 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7758-7852 8.23e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 49.31  E-value: 8.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7758 FVKEPatfvkrLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPncGITTTERSSILeILESTIEDYAQYACLI 7837
Cdd:cd20978       3 FIQKP------EKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPM--ERATVEDGTLT-IINVQPEDTGYYGCVA 73
                            90
                    ....*....|....*
gi 1958765569  7838 ENEAGQDICEALVSV 7852
Cdd:cd20978      74 TNEIGDIYTETLLHV 88
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
33698-33787 8.28e-06

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 49.71  E-value: 8.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKN--NLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNF 33775
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDgkQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569 33776 RGQCSATASLTV 33787
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8141-8218 8.31e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 49.31  E-value: 8.31e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8141 PRFIKKLDQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSkFRMSFEDSvaILEMHNLSVEDSGDYTCEARN 8218
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPM-ERATVEDG--TLTIINVQPEDTGYYGCVATN 75
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
14213-14294 8.37e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 49.95  E-value: 8.37e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14213 TVKAGTKIELPATVTGKPEPKITWTK--ADTLL---RPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAV 14287
Cdd:cd05726      10 VVALGRTVTFQCETKGNPQPAIFWQKegSQNLLfpyQPPQPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVAGSILAK 89

                    ....*..
gi 1958765569 14288 VEVNVLD 14294
Cdd:cd05726      90 AQLEVTD 96
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
5518-5600 8.38e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 49.16  E-value: 8.38e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5518 RKMDSIKGSFIDLECIVAGsHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCsatnKAGHSQCSGH 5597
Cdd:cd20967       5 PAVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC----VAGGEKCSFE 79

                    ...
gi 1958765569  5598 LTV 5600
Cdd:cd20967      80 LFV 82
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
32318-32396 8.48e-06

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 49.48  E-value: 8.48e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32318 HEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIvheGlDYYALH--------IRDTLPEDTGYYRVTATNTAGSTS 32389
Cdd:cd20956      14 QPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRV---G-DYVTSDgdvvsyvnISSVRVEDGGEYTCTATNDVGSVS 89

                    ....*..
gi 1958765569 32390 CQAHLQV 32396
Cdd:cd20956      90 HSARINV 96
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
4390-4466 8.54e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 49.37  E-value: 8.54e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4390 LSRPKSLTTFVGKAAKFLCTVSG--TPVIEtiWQKDGTALSPSPDCRiTDADNKHSLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:cd04978       3 IIEPPSLVLSPGETGELICEAEGnpQPTIT--WRLNGVPIEPAPEDM-RRTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
30660-30736 8.54e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.43  E-value: 8.54e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  30660 VRQGGVIRLTIPIKGKPFPICKWTKEGQDV---SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVKV 30736
Cdd:smart00410     6 VKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
4499-4569 8.65e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 49.54  E-value: 8.65e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  4499 LECQVDEDRKVSITWSKDG-QKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAGSSSSSATVAV 4569
Cdd:cd05763      19 LECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATLTV 90
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8892-8980 8.66e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 8.66e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8892 PPSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPL-KDSPNVQTSFLdnIATLNIFKTDRSLAGQYSCTVTNP 8970
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTCEAG--VGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|
gi 1958765569  8971 IGSASSSAKL 8980
Cdd:cd20976      79 AGQVSCSAWV 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8428-8511 8.73e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.93  E-value: 8.73e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8428 PESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELtgdSKYKISFFNKVSglkiisvaPGDSGVYSFEVQNP-VGKDSCT 8506
Cdd:pfam13895     6 PSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAI---SSSPNFFTLSVS--------AEDSGTYTCVARNGrGGKVSNP 74

                    ....*
gi 1958765569  8507 VSIQV 8511
Cdd:pfam13895    75 VELTV 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
17350-17412 8.77e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.86  E-value: 8.77e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 17350 LTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSR 17412
Cdd:cd00096       3 LTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGS 65
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2234-2306 8.88e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.43  E-value: 8.88e-06
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569   2234 QDIEVPESYSGELECIIS-PENIEGKWYHNDVE-LKSNGKYSITSRRGRQNLTVKDVTKEDQGEY-CFVVDGKKTT 2306
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYtCAATNSSGSA 77
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
4957-5038 8.89e-06

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 49.42  E-value: 8.89e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4957 NVDSVVGGACRLDCKIAGS-LPMrVSWFKDGKEIAASDryQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSRGA 5035
Cdd:cd20952       8 NQTVAVGGTVVLNCQATGEpVPT-ISWLKDGVPLLGKD--ERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAV 84

                    ...
gi 1958765569  5036 LIV 5038
Cdd:cd20952      85 LDV 87
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
19417-19493 8.97e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.42  E-value: 8.97e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 19417 PEQITIKAGKKLRVEAHVYGKPNPICKWKKgEDDVVT--SSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDT 19493
Cdd:cd05744       7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWQL-NGKPVRpdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENS 84
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
27796-27878 9.04e-06

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 49.57  E-value: 9.04e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27796 KAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQpKSSTVSVKVL 27875
Cdd:cd05762      14 RAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGS-RQAQVNLTVV 92

                    ...
gi 1958765569 27876 DTP 27878
Cdd:cd05762      93 DKP 95
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
4949-5038 9.22e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.43  E-value: 9.22e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLR--NVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTaSLEISRVDMNDAGNFTCRATNS 5026
Cdd:cd20970       1 PVISTPQPsfTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGT-TLTIRNIRRSDMGIYLCIASNG 79
                            90
                    ....*....|...
gi 1958765569  5027 V-GSKDSRGALIV 5038
Cdd:cd20970      80 VpGSVEKRITLQV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
9085-9175 9.26e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.66  E-value: 9.26e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLSETIEEtEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTS--NCEITFKNNALLLQVKKASMADAGLYTCKATN 9162
Cdd:cd20974       1 PVFTQPLQSVVVL-EGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|...
gi 1958765569  9163 DAGSALCTSSIVI 9175
Cdd:cd20974      80 GSGQATSTAELLV 92
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
7870-7935 9.26e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 48.94  E-value: 9.26e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7870 GEPTTLQCKVDGTPEIRISWYKEHTKLrsaPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVG 7935
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIKLGGEL---PKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMG 72
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
8235-8318 9.28e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 49.39  E-value: 9.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELR-SGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDV 8313
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRpDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80

                    ....*
gi 1958765569  8314 GSDTC 8318
Cdd:cd20975      81 GARQC 85
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7214-7290 9.35e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.93  E-value: 9.35e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7214 QGESIQLECKISGSPEIKVVWFRNDSELheSWKYNMSfvnsvalltINEASVEDTGDYICEAHNG-VGHASCSTALKV 7290
Cdd:pfam13895    13 EGEPVTLTCSAPGNPPPSYTWYKDGSAI--SSSPNFF---------TLSVSAEDSGTYTCVARNGrGGKVSNPVELTV 79
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
7386-7467 9.37e-06

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 49.62  E-value: 9.37e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7386 PPRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDKGEVIRE----SENVRISFVDNiATLQLGSPEASHSGKYVCQ 7461
Cdd:cd20954       1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKATGSTPGEykdlLYDPNVRILPN-GTLVFGHVQKENEGHYLCE 79

                    ....*.
gi 1958765569  7462 IKNDAG 7467
Cdd:cd20954      80 AKNGIG 85
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7109-7198 9.50e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 49.57  E-value: 9.50e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7109 FDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKD--------NKEIRPGGNYTITCVGNtphLRILKVGKGDSGQYTCQ 7180
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEgsqnllfpYQPPQPSSRFSVSPTGD---LTITNVQRSDVGYYICQ 78
                            90
                    ....*....|....*...
gi 1958765569  7181 ATNDVGKDMCSAQLSVKE 7198
Cdd:cd05726      79 ALNVAGSILAKAQLEVTD 96
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
9000-9079 9.61e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 49.13  E-value: 9.61e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9000 AVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTaqLNIK 9079
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSAT--INVK 81
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8160-8231 9.63e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.11  E-value: 9.63e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8160 RYECKIGGSPEIKVLWYKDEVEIQESSKFRMSF-EDSVAILEMHNLSVEDSGDYTCEARNAAGSASSSTSLKV 8231
Cdd:cd20973      16 RFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
32218-32284 9.67e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.86  E-value: 9.67e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32218 VRFGVTITVHPEPRVTWYKSGQKIKPGDDDKKYTFESDkglYQLTINSVTTDDDAEYAVVARNKHGE 32284
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGN---GTLTISNVTLEDSGTYTCVASNSAGG 64
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
2845-2926 9.68e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.50  E-value: 9.68e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2845 TKTMRNIEVPETKAASFECEVSHFNVPSM-WLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTF----VCGNDQ 2919
Cdd:cd20972       5 IQKLRSQEVAEGSKVRLECRVTGNPTPVVrWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSClatnSVGSDT 84

                    ....*..
gi 1958765569  2920 VSATLTV 2926
Cdd:cd20972      85 TSAEIFV 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
5520-5592 9.68e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.43  E-value: 9.68e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5520 MDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKyKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHS 5592
Cdd:cd20970      12 VTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTTLTIRNIRRSDMGIYLCIASNGVPGS 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
13066-13135 9.70e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.42  E-value: 9.70e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 13066 FISKPQNLEILEGEKAEFVCTISK-ESFEVQWKRDDQTLESGDKYDIIADGKKRV-LVVKDATLQDMGTYVV 13135
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSGlPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTC 74
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8905-8977 9.73e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.93  E-value: 9.73e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8905 TVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNvqtSFLDNIATLNifktdrslAGQYSCTVTNPIGSASSS 8977
Cdd:pfam13895    12 TEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN---FFTLSVSAED--------SGTYTCVARNGRGGKVSN 73
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
30273-30336 9.77e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.48  E-value: 9.77e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 30273 PITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKN-VTGTTSETI 30336
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3600-3667 9.79e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 9.79e-06
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   3600 VHGEPAPTVLWFKEDMPLYTNVCYTIIHNPDGSGTFIVNDPQRGDSGLYICKAENLWGTSTCTAELLV 3667
Cdd:smart00410    18 ASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
6360-6437 9.80e-06

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 49.16  E-value: 9.80e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6360 PVVETLKNTEVSLECELSGtPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAqnevGSDTCI 6437
Cdd:cd20967       5 PAVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA----GGEKCS 77
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
32313-32396 9.87e-06

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 49.12  E-value: 9.87e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32313 ANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEgldyYALHIRDTLPEDTGYYRVTATNTAGSTSCQA 32392
Cdd:cd05723       5 SNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKE----HNLQVLGLVKSDEGFYQCIAENDVGNAQASA 80

                    ....
gi 1958765569 32393 HLQV 32396
Cdd:cd05723      81 QLII 84
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5229-5319 1.01e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 49.34  E-value: 1.01e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDN---TTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTN 5305
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGvpiDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  5306 EVGSSTCSARVTLR 5319
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4588-4663 1.02e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 49.10  E-value: 1.02e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRmSFANseAILDITDV-KVDDSGTYSCEATNDAG-SDSCSTEVVI 4663
Cdd:cd20958      15 GQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQR-VFPN--GTLVIENVqRSSDEGEYTCTARNQQGqSASRSVFVKV 89
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
20898-20981 1.02e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 49.14  E-value: 1.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20898 DGLTVKAGDSIVLSAiSILGKPLPKSSWSKAGKDIRPSD--IAQITSTPTSSMlTVKYATRKDAGEYTITATNPFGTKEE 20975
Cdd:cd05891       9 DVVTIMEGKTLNLTC-TVFGNPDPEVIWFKNDQDIELSEhySVKLEQGKYASL-TIKGVTSEDSGKYSINVKNKYGGETV 86

                    ....*.
gi 1958765569 20976 HVKVSV 20981
Cdd:cd05891      87 DVTVSV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
33698-33788 1.02e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.27  E-value: 1.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNN--LPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNF 33775
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 33776 RGQCSATASLTVL 33788
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
33427-33505 1.02e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 49.47  E-value: 1.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33427 VSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSK---YKLSNDKEEFILEilKTETSDGGLYSCTVANSAGSVSSSCKL 33503
Cdd:cd05857      16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKVRNQHWSLIME--SVVPSDKGNYTCVVENEYGSINHTYHL 93

                    ..
gi 1958765569 33504 TI 33505
Cdd:cd05857      94 DV 95
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
25929-25986 1.03e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.48  E-value: 1.03e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 25929 PFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAG 25986
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
18429-18510 1.03e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 49.25  E-value: 1.03e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18429 VITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIV 18508
Cdd:cd20949       8 VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQER 87

                    ..
gi 1958765569 18509 NV 18510
Cdd:cd20949      88 TV 89
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
20898-20988 1.04e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 49.57  E-value: 1.04e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20898 DGLTVKAGDSIVLSAISILGKPLpKSSWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEHV 20977
Cdd:cd05762       9 EDMKVRAGESVELFCKVTGTQPI-TCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQV 87
                            90
                    ....*....|.
gi 1958765569 20978 KVSVLDVPGPP 20988
Cdd:cd05762      88 NLTVVDKPDPP 98
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4578-4653 1.04e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 48.94  E-value: 1.04e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4578 KVDPSYLM-LPGESARLHCKL-KGSPVIQVTWFKNNKELSESNTVRMSFanSEAILDITDVKVDDSGTYSCEATNDAG 4653
Cdd:cd05724       1 RVEPSDTQvAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIV--DDGNLLIAEARKSDEGTYKCVATNMVG 76
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
5130-5216 1.04e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 49.16  E-value: 1.04e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5130 FVKEPATFTeklepsqlLKKGDATQLVCKVTGTPPIKITW-------FANDRELResskhkMSFVESTAVLRLTDVAIED 5202
Cdd:cd05763       2 FTKTPHDIT--------IRAGSTARLECAATGHPTPQIAWqkdggtdFPAARERR------MHVMPEDDVFFIVDVKIED 67
                            90
                    ....*....|....
gi 1958765569  5203 SGEYMCEAQNEAGS 5216
Cdd:cd05763      68 TGVYSCTAQNSAGS 81
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8249-8325 1.05e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 48.74  E-value: 1.05e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8249 GADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDTcvGSVTLK 8325
Cdd:cd05748       7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS--ATINVK 81
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8896-8982 1.05e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.11  E-value: 1.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8896 SRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSF-LDNIATLNIFKTDRSLAGQYSCTVTNPIGSA 8974
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  8975 SSSAKLIL 8982
Cdd:cd20973      81 TCSAELTV 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4585-4658 1.06e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 48.93  E-value: 1.06e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  4585 MLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTvRMSFANSeaiLDITDVKVDDSGTYSCEATNDAGSDSCS 4658
Cdd:cd05725       9 VLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRY-EILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEAS 78
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8999-9078 1.06e-05

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 49.41  E-value: 1.06e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8999 DAVVGESADLECHVT-GTQPIKVTWAKDNREIRSGGNYQISYLEN-SAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQL 9076
Cdd:cd20959      13 AAQVGMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRrSSILSIDSLEASHAGNYTCHARNSAGSASYTAPL 92

                    ..
gi 1958765569  9077 NI 9078
Cdd:cd20959      93 TV 94
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
8240-8314 1.07e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.43  E-value: 1.07e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8240 KPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSG-KKYKIMSENllTSIHILNVDTADIGEYQCKATNDVG 8314
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFnTRYIVRENG--TTLTIRNIRRSDMGIYLCIASNGVP 81
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
17739-17809 1.07e-05

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 49.47  E-value: 1.07e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 17739 EQHIKVGDTLRLSAIIKGVPFPKVTWKK--EDREA------PTKAQIDVTPVGsKLEIRNAAHEDGGIYSLTVENPAGS 17809
Cdd:cd05765       9 HQTVKVGETASFHCDVTGRPQPEITWEKqvPGKENlimrpnHVRGNVVVTNIG-QLVIYNAQPQDAGLYTCTARNSGGL 86
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
24546-24625 1.07e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 49.16  E-value: 1.07e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24546 IVVRAGGSARIHIPFKGRPTPEITWSKEEGefTD---------KVQIEKGINFtqlsIDNCDRNDAGKYILKLENSSGSK 24616
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGG--TDfpaarerrmHVMPEDDVFF----IVDVKIEDTGVYSCTAQNSAGSI 82

                    ....*....
gi 1958765569 24617 SAFVTVKVL 24625
Cdd:cd05763      83 SANATLTVL 91
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
1516-1607 1.07e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.17  E-value: 1.07e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDiivPHKYPRIRIEGTKGEAALKIDSTISQDSAWYTATAINK 1595
Cdd:cd20976       2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQ---PLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  1596 AGRDTTRCKVNI 1607
Cdd:cd20976      79 AGQVSCSAWVTV 90
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
4948-5038 1.07e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.17  E-value: 1.07e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4948 APLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIA-ASDRYQIAfvEGTASLEISRVDMNDAGNFTCRATNS 5026
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQyAADRSTCE--AGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  5027 VGSKDSRGALIV 5038
Cdd:cd20976      79 AGQVSCSAWVTV 90
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
24838-24908 1.08e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 49.38  E-value: 1.08e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 24838 GEDLKIEIPVIGRPRPKISWVKDGEPLRQTT-RVNVEETATSTI-LHIKESSKDDFGKYSVTATNNAGTATEN 24908
Cdd:cd05892      15 GDPVRLECQISAIPPPQIFWKKNNEMLQYNTdRISLYQDNCGRIcLLIQNANKKDAGWYTVSAVNEAGVVSCN 87
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
33898-33977 1.09e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.04  E-value: 1.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQgrfHIENTDDlTTLIIMDVQKQDGGLYTLSLGNE-FGSD 33976
Cdd:cd20970       9 SFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTR---YIVRENG-TTLTIRNIRRSDMGIYLCIASNGvPGSV 84

                    .
gi 1958765569 33977 S 33977
Cdd:cd20970      85 E 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8328-8418 1.09e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.03  E-value: 1.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8328 PQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDkGEIVRESDNIWISHSEN-VATLHFSRAEPANAGKYTCQIKND 8406
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLN-GKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569  8407 AGVQECYATLSV 8418
Cdd:cd05744      80 AGENSFNAELVV 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
32205-32293 1.10e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.04  E-value: 1.10e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32205 LPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGddDKKYTFESDKGLyqLTINSVTTDDDAEYAVVARNK-HG 32283
Cdd:cd20970       7 QPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEF--NTRYIVRENGTT--LTIRNIRRSDMGIYLCIASNGvPG 82
                            90
                    ....*....|
gi 1958765569 32284 EDSCKAKLTV 32293
Cdd:cd20970      83 SVEKRITLQV 92
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
33424-33505 1.10e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 49.33  E-value: 1.10e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33424 DTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKL---SNDKEEFILEilKTETSDGGLYSCTVANSAGSVSSS 33500
Cdd:cd20990       9 DLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMlvrENGVHSLIIE--PVTSRDAGIYTCIATNRAGQNSFN 86

                    ....*
gi 1958765569 33501 CKLTI 33505
Cdd:cd20990      87 LELVV 91
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
31052-31124 1.10e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 49.08  E-value: 1.10e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31052 ADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVqSRKYKMSSDGrthTLTVMTEEQEDEGVYTCVATNEVG 31124
Cdd:cd04968       9 ADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPS-SQWEITTSEP---VLEIPNVQFEDEGTYECEAENSRG 77
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
31173-31238 1.11e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 49.57  E-value: 1.11e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31173 TWYHGQKLLQNSESITIENTEHYTHLVMKNVQRKtHAGKYKVQLSNVFGTVDAILDVEIQDKPDKP 31238
Cdd:cd05762      34 TWMKFRKQIQEGEGIKIENTENSSKLTITEGQQE-HCGCYTLEVENKLGSRQAQVNLTVVDKPDPP 98
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
5697-5787 1.11e-05

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 49.47  E-value: 1.11e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSW--YLDGNEITDLRR---YGISFVDGLATFQISNARVENSGTYVCE 5771
Cdd:cd05765       1 PALVNSPTHQTV-KVGETASFHCDVTGRPQPEITWekQVPGKENLIMRPnhvRGNVVVTNIGQLVIYNAQPQDAGLYTCT 79
                            90
                    ....*....|....*.
gi 1958765569  5772 ARNDAGTASCSIELKV 5787
Cdd:cd05765      80 ARNSGGLLRANFPLSV 95
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7011-7098 1.13e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 49.34  E-value: 1.13e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKdiEQTV--GLPVTLTCRLNGSAPIHVCWYRDGVLL---RDDENLQMSFVDNVATLKILQTDLSHSGQYSCSA 7085
Cdd:cd20951       1 PEFIIRLQ--SHTVweKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVA 78
                            90
                    ....*....|...
gi 1958765569  7086 SNPLGTASSTARL 7098
Cdd:cd20951      79 KNIHGEASSSASV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
19817-19897 1.14e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 49.34  E-value: 1.14e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEG---VKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATI 19893
Cdd:cd20951      10 HTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSA 89

                    ....
gi 1958765569 19894 KLKV 19897
Cdd:cd20951      90 SVVV 93
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
106-193 1.17e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 49.25  E-value: 1.17e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   106 FSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRA 185
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIA 81

                    ....*...
gi 1958765569   186 TSTADLLV 193
Cdd:cd20949      82 SDMQERTV 89
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
19814-19897 1.17e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 49.08  E-value: 1.17e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19814 KSLLTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTE---GVKMAMKRNLCTLElfSVNRKDSGDYTITAENSSGSKS 19890
Cdd:cd05857      11 KKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHrigGYKVRNQHWSLIME--SVVPSDKGNYTCVVENEYGSIN 88

                    ....*..
gi 1958765569 19891 ATIKLKV 19897
Cdd:cd05857      89 HTYHLDV 95
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
17738-17819 1.19e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 49.16  E-value: 1.19e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17738 REQHIKVGDTLRLSAIIKGVPFPKVTWKKE---DREAPTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSV 17814
Cdd:cd05763       7 HDITIRAGSTARLECAATGHPTPQIAWQKDggtDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANA 86

                    ....*
gi 1958765569 17815 KVLVL 17819
Cdd:cd05763      87 TLTVL 91
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
6550-6629 1.21e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.55  E-value: 1.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6550 TVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKhkfSFynkisslkILSVEKEDAGTYTFQVQN-NVGKSSCTAVVD 6628
Cdd:pfam13895    10 VVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN---FF--------TLSVSAEDSGTYTCVARNgRGGKVSNPVELT 78

                    .
gi 1958765569  6629 V 6629
Cdd:pfam13895    79 V 79
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
15455-15622 1.21e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 54.62  E-value: 1.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15455 VNSTHWSRVNKALLSSLKTKVDGLLEGLTYVFRVCAENAAGPGKFSPPSDPKTARDpiSPPGPPVPRVADTSSTTIELEW 15534
Cdd:COG3401     176 ATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTT--PPSAPTGLTATADTPGSVTLSW 253
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15535 EPPAFNGggeIMGYFVDKQLVGTNEWSRCTEkmVKVRQFTVKEIREGADYKLRVSAVNAAG-EGPPgeTEPVTVAEPQEP 15613
Cdd:COG3401     254 DPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP--SNVVSVTTDLTP 326

                    ....*....
gi 1958765569 15614 PTVELDVSV 15622
Cdd:COG3401     327 PAAPSGLTA 335
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8611-8701 1.22e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.27  E-value: 1.22e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKG----SSELVPGARcnVSLQDSVAELELFDVDTSQSGDYTCIVS 8686
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDgqviSTSTLPGVQ--ISFSDGRAKLSIPAVTKANSGRYSLTAT 78
                            90
                    ....*....|....*
gi 1958765569  8687 NEAGRASCTTQLFVK 8701
Cdd:cd20974      79 NGSGQATSTAELLVL 93
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6549-6629 1.22e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.17  E-value: 1.22e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6549 MTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHkFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVVD 6628
Cdd:cd20976      11 LEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADR-STCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVT 89

                    .
gi 1958765569  6629 V 6629
Cdd:cd20976      90 V 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
1254-1329 1.22e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 48.73  E-value: 1.22e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  1254 KNYRILEGMGVTFHCKMS-GYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNA 1329
Cdd:pfam00047     4 PTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
32330-32396 1.24e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 49.03  E-value: 1.24e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 32330 SGIPAPTLKWEKDGQPLS-LGPHIEIVHEGldyyALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:cd20952      24 TGEPVPTISWLKDGVPLLgKDERITTLENG----SLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
4956-5023 1.24e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 48.78  E-value: 1.24e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4956 RNVDSVVGGACRLDCKIAGSlPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRA 5023
Cdd:cd20967       5 PAVQVSKGHKIRLTVELADP-DAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA 71
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7111-7194 1.24e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 49.07  E-value: 1.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7111 IKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVgntPHLRILKVGKGDSGQYTCQATNDVGKDMC 7190
Cdd:cd20957       6 IDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSE---DVLVIPSVKREDKGMYQCFVRNDGDSAQA 82

                    ....
gi 1958765569  7191 SAQL 7194
Cdd:cd20957      83 TAEL 86
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12192-12245 1.25e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.48  E-value: 1.25e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12192 IILKCEVSKDVP--VKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC 12245
Cdd:cd00096       1 VTLTCSASGNPPptITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTC 56
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
6830-6901 1.26e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 49.18  E-value: 1.26e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  6830 DHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAG 6901
Cdd:cd05762      10 DMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLG 81
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
13249-13330 1.26e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.03  E-value: 1.26e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13249 IEPLKDIETMEKKSVTFWCKVNRL-NVTLKWTKNGEEVAFDNRISYRIDKY-KHSLIIKDCGFPDEGEYIVTA----GQD 13322
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLpTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIArnraGEN 83

                    ....*...
gi 1958765569 13323 KSVAELLI 13330
Cdd:cd05744      84 SFNAELVV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6073-6163 1.27e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 48.96  E-value: 1.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEI---STSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSN 6149
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  6150 VAGDNACSGILTVK 6163
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
8797-8880 1.27e-05

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 49.09  E-value: 1.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDtklRPTTTCKMHFKNN-----VATLVFTQVDSN-----DSGE 8866
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNG---QPLETDKDDPRSHrivlpSGSLFFLRVVHGrkgrsDEGV 77
                            90
                    ....*....|....
gi 1958765569  8867 YICRAENSVGEVSS 8880
Cdd:cd07693      78 YVCVAHNSLGEAVS 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
24142-24234 1.27e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 49.18  E-value: 1.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24142 KFRDTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSF 24221
Cdd:cd05762       6 QFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQA 85
                            90
                    ....*....|...
gi 1958765569 24222 PVNVKVLDRPGPP 24234
Cdd:cd05762      86 QVNLTVVDKPDPP 98
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10144-10255 1.28e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 54.39  E-value: 1.28e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10144 PKKVEPPAVKVPEAPKKPV-PEEKKPVPIPKKEPAAP-PKVPEAPKKPAPE-----EKTAVPVAKKKEAPPPKVTEVQKK 10216
Cdd:NF033839    325 LEKPKPEVKPQPEKPKPEVkPQLETPKPEVKPQPEKPkPEVKPQPEKPKPEvkpqpETPKPEVKPQPEKPKPEVKPQPEK 404
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1958765569 10217 VVTEEKitiiPQrEESPPPAVPEIPKKKVPEEKrPVPRK 10255
Cdd:NF033839    405 PKPEVK----PQ-PEKPKPEVKPQPEKPKPEVK-PQPEK 437
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8706-8793 1.29e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.03  E-value: 1.29e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8706 FVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEK-SAILEILSSTVEDSGQYNCYIENASGK 8784
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRAGE 82

                    ....*....
gi 1958765569  8785 DSCSAQILI 8793
Cdd:cd05744      83 NSFNAELVV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
31148-31231 1.30e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.30e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  31148 EKYYGAVGSTLRLHVMYIGRPVPAMTWYH-GQKLLQNSESITIENTEHYTHLVMKNVQRKtHAGKYKVQLSNVFGTVDAI 31226
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPE-DSGTYTCAATNSSGSASSG 80

                     ....*
gi 1958765569  31227 LDVEI 31231
Cdd:smart00410    81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
31154-31231 1.30e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.79  E-value: 1.30e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31154 VGSTLRLHVMYIGRPVPAMTWYHGQKLLQNSESITIENTEHYTHLVMKNVQRkTHAGKYKVQLSNVFGTVDAILDVEI 31231
Cdd:pfam07679    14 EGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQP-DDSGKYTCVATNSAGEAEASAELTV 90
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
28478-28560 1.31e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 48.68  E-value: 1.31e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28478 DGLVIKSGDSLRIKALVQGRPVPRVTWFKDG---VEIERRMNMEITDvlGSTSLFVRDATRDHRGVYTVEAKNVSGSTKA 28554
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDkafTATEGRVRVESYK--DLSSFVIEGAEREDEGVYTITVTNPVGEDHA 80

                    ....*.
gi 1958765569 28555 EITVKV 28560
Cdd:cd05894      81 SLFVKV 86
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
23746-23821 1.31e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 49.00  E-value: 1.31e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23746 PAFSSYSV------QVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSldlTTLSIKETHKDDGGHYGITVANV 23819
Cdd:cd04969       1 PDFELNPVkkkilaAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPD---GSLKIKNVTKSDEGKYTCFAVNF 77

                    ..
gi 1958765569 23820 VG 23821
Cdd:cd04969      78 FG 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6258-6349 1.32e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.79  E-value: 1.32e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6258 PPKFVKKLEASKIVKAGDSArLECKITGSPEIRVVWYRNEHELT-ASDKYQMTfiDSVAVMQMNSLGTEDSGDFICEAQN 6336
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFV-AQCSARGKPVPRITWIRNAQPLQyAADRSTCE--AGVGELHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|...
gi 1958765569  6337 PAGSTSCSTKVIV 6349
Cdd:cd20976      78 AAGQVSCSAWVTV 90
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8517-8619 1.32e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 49.18  E-value: 1.32e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8517 PPSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVA 8596
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90       100
                    ....*....|....*....|...
gi 1958765569  8597 GSDECSAPLTVreppsfVQKPDP 8619
Cdd:cd05762      81 GSRQAQVNLTV------VDKPDP 97
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
1251-1337 1.32e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 48.72  E-value: 1.32e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1251 IR-IKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERyQMDFlQDGraSLRI-PVVLPEDEGIYTAFASNIKGN 1328
Cdd:cd20958       4 IRpMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR-QRVF-PNG--TLVIeNVQRSSDEGEYTCTARNQQGQ 79

                    ....*....
gi 1958765569  1329 AIcSGKLYV 1337
Cdd:cd20958      80 SA-SRSVFV 87
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5510-5600 1.33e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 49.10  E-value: 1.33e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5510 PPSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFH-----DNTAFLEISQLEGTDSGTYTCS 5584
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYvtsdgDVVSYVNISSVRVEDGGEYTCT 80
                            90
                    ....*....|....*.
gi 1958765569  5585 ATNKAGHSQCSGHLTV 5600
Cdd:cd20956      81 ATNDVGSVSHSARINV 96
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
6263-6349 1.34e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 48.78  E-value: 1.34e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6263 KKLEASKIVKAGDSARLECKITGsPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEaqnpAGSTS 6342
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV----AGGEK 75

                    ....*..
gi 1958765569  6343 CSTKVIV 6349
Cdd:cd20967      76 CSFELFV 82
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
4586-4655 1.34e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 48.70  E-value: 1.34e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4586 LPGESARLHCKLKGSPVIQVTWFKnnkeLSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSD 4655
Cdd:cd04968      14 LKGQTVTLECFALGNPVPQIKWRK----VDGSPSSQWEITTSEPVLEIPNVQFEDEGTYECEAENSRGKD 79
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
9669-9759 1.36e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.12  E-value: 1.36e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9669 PIQFTKRIQNIVVSEHQSATFECEVS-FDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARlEP 9747
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTgNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLAT-NS 79
                            90
                    ....*....|..
gi 1958765569  9748 RGEARSTAELYL 9759
Cdd:cd20972      80 VGSDTTSAEIFV 91
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
913-989 1.36e-05

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 48.88  E-value: 1.36e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   913 EGESVTLECHISGY-PSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAV 989
Cdd:cd20927      13 EGGHVKYVCKIENYdQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 90
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
33698-33781 1.37e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 49.01  E-value: 1.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRN-MYTLEIRNASVSDSGKYTVKAKNFR 33776
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGgLCRLRILAAERGDAGFYTCKAVNEY 80

                    ....*..
gi 1958765569 33777 G--QCSA 33781
Cdd:cd20975      81 GarQCEA 87
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
33712-33787 1.38e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 49.14  E-value: 1.38e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33712 GQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNM-YTLEIRNASVSDSGKYTVKAKNFRGQCSATASLTV 33787
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKgWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
5229-5316 1.38e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 49.01  E-value: 1.38e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLR-SGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNEV 5307
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRpDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80

                    ....*....
gi 1958765569  5308 GSSTCSARV 5316
Cdd:cd20975      81 GARQCEARL 89
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
1429-1507 1.39e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 48.75  E-value: 1.39e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  1429 LEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRAGKSTISVTLTV 1507
Cdd:cd05891      14 MEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7307-7374 1.40e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.55  E-value: 1.40e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7307 KGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFkvtsknfdtslHIFNLEAPDIGEYHCKATNEVGS 7374
Cdd:pfam13895    13 EGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF-----------FTLSVSAEDSGTYTCVARNGRGG 69
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
13065-13137 1.40e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 48.33  E-value: 1.40e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 13065 EFISKPQNLEILEGEKAEFVCTISKESF-EVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVVMV 13137
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPpTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8248-8324 1.42e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 48.40  E-value: 1.42e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8248 KGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLtsiHILNVDTADIGEYQCKATNDVGSDTCVGSVTL 8324
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSGTL---RISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7780-7842 1.42e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.09  E-value: 1.42e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  7780 IVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEAG 7842
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8900-8981 1.45e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 48.55  E-value: 1.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8900 RDVQETVGLPVVFECA--VSGSEPiSVSWYKDGKPLKDSPNVQTSFLDniATLNIFKTDRSLAGQYSCTVTNPIGS-ASS 8976
Cdd:cd05724       5 SDTQVAVGEMAVLECSppRGHPEP-TVSWRKDGQPLNLDNERVRIVDD--GNLLIAEARKSDEGTYKCVATNMVGErESR 81

                    ....*
gi 1958765569  8977 SAKLI 8981
Cdd:cd05724      82 AARLS 86
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6548-6629 1.45e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 48.55  E-value: 1.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6548 SMTVTVGETCSLECKVA-GTPELSVEWYKDGKLLTSSQKHKFSFynKISSLKILSVEKEDAGTYTFQVQNNVG-KSSCTA 6625
Cdd:cd05724       6 DTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDNERVRIV--DDGNLLIAEARKSDEGTYKCVATNMVGeRESRAA 83

                    ....
gi 1958765569  6626 VVDV 6629
Cdd:cd05724      84 RLSV 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
29569-29649 1.45e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.45e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29569 VTIRAGSDLVLDAAVGGKPEPKIIWTK-GDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMV 29647
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  29648 KV 29649
Cdd:smart00410    84 TV 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8422-8511 1.46e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 49.00  E-value: 1.46e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8422 ATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKyKISFFNKVSG---LKIISVAPGDSGVYSFEVQN 8498
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTD-RISLYQDNCGricLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569  8499 PVGKDSCTVSIQV 8511
Cdd:cd05892      80 EAGVVSCNARLDV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
4300-4379 1.47e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 48.73  E-value: 1.47e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4300 PLEVALGHLAKFTCEI-QGAPNVRFQWFKAGREIYESDKCS-IRSSNYISSLEILRTQVVDCGEYTCKASNEYGSVSCTA 4377
Cdd:pfam00047     5 TVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKhDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84

                    ..
gi 1958765569  4378 TL 4379
Cdd:pfam00047    85 SL 86
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
9191-9271 1.48e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 48.74  E-value: 1.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9191 VTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASG-TAVLELKDTAKADSGDYVCKASNVAGSDTSKCKV 9269
Cdd:cd05737      11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGrTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTV 90

                    ..
gi 1958765569  9270 TI 9271
Cdd:cd05737      91 SV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
18431-18510 1.48e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 48.72  E-value: 1.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18431 TVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLP-RVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVN 18509
Cdd:cd20973       8 EVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87

                    .
gi 1958765569 18510 V 18510
Cdd:cd20973      88 V 88
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7303-7374 1.49e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 48.61  E-value: 1.49e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  7303 VGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSknfDTSLHIFNLEAPDIGEYHCKATNEVGS 7374
Cdd:cd04969      12 ILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILP---DGSLKIKNVTKSDEGKYTCFAVNFFGK 80
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8893-8980 1.49e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 48.54  E-value: 1.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSF-SRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLkDSPNVQTSFLDNIATL-NIFKTDRslaGQYSCTVTNP 8970
Cdd:cd20978       1 PKFiQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDGTLTIiNVQPEDT---GYYGCVATNE 76
                            90
                    ....*....|
gi 1958765569  8971 IGSASSSAKL 8980
Cdd:cd20978      77 IGDIYTETLL 86
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7111-7196 1.50e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.55  E-value: 1.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7111 IKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTitcvgntphlrILKVGKGDSGQYTCQATND-VGKDM 7189
Cdd:pfam13895     4 LTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFF-----------TLSVSAEDSGTYTCVARNGrGGKVS 72

                    ....*..
gi 1958765569  7190 CSAQLSV 7196
Cdd:pfam13895    73 NPVELTV 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
21587-21654 1.50e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 48.33  E-value: 1.50e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 21587 VIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKN 21654
Cdd:pfam13927    11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
3022-3102 1.51e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 48.66  E-value: 1.51e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3022 KHIKDIKVLEKKRAMFECEVS--EPDITVQWMKDGQEL--QIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVA----GG 3093
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEATseNPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVenilGK 83

                    ....*....
gi 1958765569  3094 NMSTANLFV 3102
Cdd:cd05750      84 DTVTGNVTV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
13062-13148 1.52e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.89  E-value: 1.52e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13062 LAAEFISKPQNLEILEGEKAEFVCTISKESF-EVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVVMV--G 13138
Cdd:cd05747       2 LPATILTKPRSLTVSEGESARFSCDVDGEPApTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVenS 81
                            90
                    ....*....|
gi 1958765569 13139 AARAAAHLTV 13148
Cdd:cd05747      82 EGKQEAQFTL 91
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
18430-18500 1.52e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.89  E-value: 1.52e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 18430 ITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSG 18500
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
3462-3550 1.53e-05

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 48.73  E-value: 1.53e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3462 VFIKEISDVEISIEdvaklsvtVVGCPKPKIQWFFNGMLLTPSADYKFVFDgnnHSLIILFTRFQDEGEYTCMASNEYGR 3541
Cdd:cd05723       7 IYAHESMDIVFECE--------VTGKPTPTVKWVKNGDVVIPSDYFKIVKE---HNLQVLGLVKSDEGFYQCIAENDVGN 75

                    ....*....
gi 1958765569  3542 AVCSAHLKV 3550
Cdd:cd05723      76 AQASAQLII 84
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3602-3667 1.55e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 48.35  E-value: 1.55e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  3602 GEPAPTVLWFKEDMPLYTNVCYTiIHNPDGSGTFIVNDPQRGDSGLYICKAENLWGTSTCTAELLV 3667
Cdd:cd05748      18 GRPTPTVTWSKDGQPLKETGRVQ-IETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
25231-25310 1.57e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 48.65  E-value: 1.57e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25231 VRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMeikSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPITVKV 25310
Cdd:cd20952      11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERI---TTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
8244-8312 1.57e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 48.39  E-value: 1.57e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8244 VETLKGADVHLECELQGtPPFQVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATND 8312
Cdd:cd20967       7 VQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGE 74
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33891-33984 1.59e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 48.68  E-value: 1.59e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSqeqQGRFHIENTDdltTLIIMDVQKQDGGLYTLSLG 33970
Cdd:cd20957       1 PLSATIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGH---SSRVQILSED---VLVIPSVKREDKGMYQCFVR 74
                            90
                    ....*....|....
gi 1958765569 33971 NEFGSDSATVNINI 33984
Cdd:cd20957      75 NDGDSAQATAELKL 88
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
1428-1505 1.59e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 48.73  E-value: 1.59e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  1428 CLEGQTARFDLKVV-GRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRAGKSTISVTL 1505
Cdd:pfam00047     8 VLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5977-6066 1.62e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 48.68  E-value: 1.62e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5977 AQIIEKAKSVDVTEkdPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVasfRIQSVMKQDSGQYTFKVENDFG 6056
Cdd:cd20957       4 ATIDPPVQTVDFGR--TAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVL---VIPSVKREDKGMYQCFVRNDGD 78
                            90
                    ....*....|
gi 1958765569  6057 SSSCDAYLRV 6066
Cdd:cd20957      79 SAQATAELKL 88
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
32319-32396 1.63e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 48.01  E-value: 1.63e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 32319 EGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGldyyALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSG----TLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8703-8780 1.64e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 48.33  E-value: 1.64e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8703 PAIFVKRlNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIEN 8780
Cdd:pfam13927     2 PVITVSP-SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
11732-11802 1.66e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.66e-05
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  11732 EEVTVVKGQPLYLSCELNKERD--VVWRKDGKIVVEKPGRIVPGVIGLMRALTINDADDTDAGTYTVTVENAN 11802
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPpeVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12537-12601 1.68e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.68e-05
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  12537 QDYTGVEKDEVVLQCEISKADAP-VKWFKDG-KEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC 12601
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPeVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTC 68
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8525-8607 1.69e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 48.55  E-value: 1.69e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8525 KETNGLSGSSVVMECKV-FGSPPISVLWLHDGNAISSGRKYQTTLTDNTcaLTVNMLEDADAGDYTCIATNVAGSDECS- 8602
Cdd:cd05724       5 SDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIVDDGN--LLIAEARKSDEGTYKCVATNMVGERESRa 82

                    ....*
gi 1958765569  8603 APLTV 8607
Cdd:cd05724      83 ARLSV 87
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6270-6349 1.69e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 48.35  E-value: 1.69e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6270 IVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTKVIV 6349
Cdd:cd05748       3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
19410-19499 1.70e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.89  E-value: 1.70e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19410 LPPKILM-PEQITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENS 19488
Cdd:cd05747       2 LPATILTkPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENS 81
                            90
                    ....*....|.
gi 1958765569 19489 SGTDTQKIKVT 19499
Cdd:cd05747      82 EGKQEAQFTLT 92
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1683-1754 1.71e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 48.56  E-value: 1.71e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  1683 ECRLTpiGDPTMVVEWLHDGKPL--EAANRLrLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:cd20990      21 DCKVS--GLPTPDLSWQLDGKPIrpDSAHKM-LVRENGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVV 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
3463-3542 1.71e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 48.48  E-value: 1.71e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3463 FIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYGRA 3542
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIA 81
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
1040-1127 1.72e-05

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 48.80  E-value: 1.72e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1040 FISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGV--------PLTTGYRYKVSynkQTGEcrLVISMTFADDAGEYT 1111
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSqnllfpyqPPQPSSRFSVS---PTGD--LTITNVQRSDVGYYI 76
                            90
                    ....*....|....*.
gi 1958765569  1112 IVIRNKHGETSASASL 1127
Cdd:cd05726      77 CQALNVAGSILAKAQL 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
15203-15310 1.74e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 48.35  E-value: 1.74e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15203 VKRGDEIALDATISGSPYPTITWIKDENVIVPeeikkrvappvrrkkgeaeeeepftlplTERLSINNSKQgESQLRVRD 15282
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKE----------------------------TGRVQIETTAS-STSLVIKN 54
                            90       100
                    ....*....|....*....|....*...
gi 1958765569 15283 SLRPDHGQYMIKVENDHGVAKAPCTVSV 15310
Cdd:cd05748      55 AKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
5414-5502 1.75e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.51  E-value: 1.75e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5414 PATITEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDV 5493
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ....*....
gi 1958765569  5494 GRSSCKASI 5502
Cdd:cd05747      83 GKQEAQFTL 91
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
31044-31128 1.77e-05

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 48.62  E-value: 1.77e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31044 APGVRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKElVQSRKYKMSSDGR---THTLTVMTEEQEDEGVYTCVAT 31120
Cdd:cd20971       1 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKE-IIADGLKYRIQEFkggYHQLIIASVTDDDATVYQVRAT 79

                    ....*...
gi 1958765569 31121 NEVGEVET 31128
Cdd:cd20971      80 NQGGSVSG 87
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
6354-6435 1.78e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 48.75  E-value: 1.78e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6354 VFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIA-SKNFHASIHILNVDSTDIGEYHCKAQNEVG 6432
Cdd:cd05891       3 VIGGLPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKlEQGKYASLTIKGVTSEDSGKYSINVKNKYG 82

                    ...
gi 1958765569  6433 SDT 6435
Cdd:cd05891      83 GET 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
8062-8137 1.78e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 48.39  E-value: 1.78e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8062 GESGSFKCHVTGtAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCyasnVAGKDSCSAQLGV 8137
Cdd:cd20967      12 GHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC----VAGGEKCSFELFV 82
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
3577-3667 1.79e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 48.55  E-value: 1.79e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNV-CYTIIHNPDGSGTFIVNDPQRGDSGLYICKAENL 3655
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSdHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  3656 WGTSTCTAELLV 3667
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
5708-5787 1.81e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 48.26  E-value: 1.81e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5708 VLRNGQSTTFECQVTGTPEIRVSWYLDGNEI--TDLRrygiSFVDGLATFQISNARVENSGTYVCEARNDAGTASCSIEL 5785
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKDGVPLlgKDER----ITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVL 85

                    ..
gi 1958765569  5786 KV 5787
Cdd:cd20952      86 DV 87
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
5511-5600 1.83e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 48.61  E-value: 1.83e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAF--LEISQLEGTDSGTYTCSATNK 5588
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRicLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  5589 AGHSQCSGHLTV 5600
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
1525-1607 1.83e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 48.75  E-value: 1.83e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1525 VNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGTKgEAALKIDSTISQDSAWYTATAINKAGRDTTRCK 1604
Cdd:cd05891      11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGK-YASLTIKGVTSEDSGKYSINVKNKYGGETVDVT 89

                    ...
gi 1958765569  1605 VNI 1607
Cdd:cd05891      90 VSV 92
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
32314-32396 1.84e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 48.37  E-value: 1.84e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32314 NAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDYYALHIrdtlpEDTGYYRVTATNTAGSTSCQAH 32393
Cdd:cd05728       8 DTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGDLRITKLSL-----SDSGMYQCVAENKHGTIYASAE 82

                    ...
gi 1958765569 32394 LQV 32396
Cdd:cd05728      83 LAV 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7200-7291 1.85e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 48.50  E-value: 1.85e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLdTSKVAKQGESIQLECKISGSPEIKVVWFRND--SELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHN 7277
Cdd:cd20974       1 PVFTQPL-QSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569  7278 GVGHASCSTALKVK 7291
Cdd:cd20974      80 GSGQATSTAELLVL 93
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
7586-7662 1.87e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 48.35  E-value: 1.87e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7586 TTATLGASVVLECRVSGSAP-ISVGWFLDGNEIISSPKCQPSFADN-VCTLTLSSLEPSDTGAYTCVAANVAGQDESSA 7662
Cdd:pfam00047     6 VTVLEGDSATLTCSASTGSPgPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
6926-7002 1.88e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 48.66  E-value: 1.88e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  6926 ASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNvATLVFNKVGINDSGEYTCVAENSIGTAASKTVF 7002
Cdd:cd20970      14 AREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENG-TTLTIRNIRRSDMGIYLCIASNGVPGSVEKRIT 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
26716-26773 1.88e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 47.71  E-value: 1.88e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26716 FTMTVPFRGRPIPNVSWSKPDTDLRTRAY--IDSTDSRTSLTIENANRNDSGKYTLTIQN 26773
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRdsRRSELGNGTLTISNVTLEDSGTYTCVASN 60
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8905-8980 1.89e-05

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 48.64  E-value: 1.89e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8905 TVGLPVVFECAVSGSE-PISVSWYKDGKPLKDSPNVQTSFLDNIAT-LNIFKTDRSLAGQYSCTVTNPIGSASSSAKL 8980
Cdd:cd20959      15 QVGMRAQLHCGVPGGDlPLNIRWTLDGQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCHARNSAGSASYTAPL 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8249-8324 1.89e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 48.34  E-value: 1.89e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8249 GADVHLECELQGTPPFQVSWYKDKRELRSGKKYKI-MSENLLTSIHILNVDTADIGEYQCKATNDVGSDTCVGSVTL 8324
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8421-8511 1.89e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 48.30  E-value: 1.89e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8421 PATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISffnKVSGLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd20957       1 PLSATIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQIL---SEDVLVIPSVKREDKGMYQCFVRNDG 77
                            90
                    ....*....|.
gi 1958765569  8501 GKDSCTVSIQV 8511
Cdd:cd20957      78 DSAQATAELKL 88
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
5709-5787 1.89e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 48.62  E-value: 1.89e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5709 LRNGQSTTFECQVTGTPEIRVSWYLDGNEI-TDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd20975      12 VREGQDVIMSIRVQGEPKPVVSWLRNRQPVrPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQCEARLEV 91
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33082-33163 1.92e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 48.33  E-value: 1.92e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33082 ITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTakyKSTFEISSVQ-ASDEGNYSVVVENTDGkQEAQFTL 33160
Cdd:cd20958      10 LTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFP---NGTLVIENVQrSSDEGEYTCTARNQQG-QSASRSV 85

                    ...
gi 1958765569 33161 TVQ 33163
Cdd:cd20958      86 FVK 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
26994-27079 1.92e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 48.50  E-value: 1.92e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26994 PSHTVYVRAGSNLKVDIPISGKPLPKVTLSRDG--VPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTK 27071
Cdd:cd20974       6 PLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQAT 85

                    ....*...
gi 1958765569 27072 TFINIIVL 27079
Cdd:cd20974      86 STAELLVL 93
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7107-7196 1.96e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 48.55  E-value: 1.96e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGN-YTITC-VGNTPHLRILKVGKGDSGQYTCQATND 7184
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDhYTIQRdLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  7185 VGKDMCSAQLSV 7196
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4387-4467 1.96e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 48.54  E-value: 1.96e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFV-GKAAKFLCTVSGTPVIETIWQKDGTALS-PSPDCRITDadnkHSLELSNLTVQDRGVYSCKASNK 4464
Cdd:cd20978       1 PKFIQKPEKNVVVKgGQDVTLPCQVTGVPQPKITWLHNGKPLQgPMERATVED----GTLTIINVQPEDTGYYGCVATNE 76

                    ...
gi 1958765569  4465 FGA 4467
Cdd:cd20978      77 IGD 79
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
6173-6246 1.98e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 48.76  E-value: 1.98e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6173 ERQQAIP-DSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSF-LNLYSVDASKTGQYTCQVTNDVGS 6246
Cdd:cd05729      11 EREHALPaANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWsLIIERAIPRDKGKYTCIVENEYGS 86
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6363-6442 1.98e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 48.34  E-value: 1.98e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6363 ETLKNTEVS------LECELSGTPPFEVVWYKDKRQLRSSKKYKIA-SKNFHASIHILNVDSTDIGEYHCKAQNEVGSDT 6435
Cdd:cd20973       2 QTLRDKEVVegsaarFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569  6436 CICAIKL 6442
Cdd:cd20973      82 CSAELTV 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
25216-25310 1.99e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.40  E-value: 1.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25216 APNASLDPKYRDVIivrAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKSTLQKttLTVKDCIRTDGGQYTLKL 25295
Cdd:cd20976       1 APSFSSVPKDLEAV---EGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVGE--LHIQDVLPEDHGTYTCLA 75
                            90
                    ....*....|....*
gi 1958765569 25296 SNVGGTKTIPITVKV 25310
Cdd:cd20976      76 KNAAGQVSCSAWVTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
18724-18796 1.99e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 48.35  E-value: 1.99e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 18724 TVKAGDTIRLEAGVRGKPFPEVAWTKDkdATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAGS 18796
Cdd:cd20972      12 EVAEGSKVRLECRVTGNPTPVVRWFCE--GKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGS 82
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5157-5225 2.01e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.40  E-value: 2.01e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5157 CKVTGTPPIKITWFANDRELRESSKHKMSFVEsTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTSIVIV 5225
Cdd:cd20976      23 CSARGKPVPRITWIRNAQPLQYAADRSTCEAG-VGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
4499-4569 2.02e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 48.26  E-value: 2.02e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  4499 LECQVDEDRKVSITWSKDGQKLPaGKDYKIYFEDKiASLEIPLAKLKDSGTYSCTASNEAGSSSSSATVAV 4569
Cdd:cd20952      19 LNCQATGEPVPTISWLKDGVPLL-GKDERITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
28877-28958 2.02e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 48.50  E-value: 2.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28877 QTHIVRAGASIRLFIAYQGRPTPTAVWSKP----DSNLSIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSIT 28952
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDgqviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*.
gi 1958765569 28953 FTVKVL 28958
Cdd:cd20974      88 AELLVL 93
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8906-8980 2.03e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 48.35  E-value: 2.03e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8906 VGLPVVFECAVSGSEP-ISVSWYKDGKPLKDSPNVQTSFLDN-IATLNIFKTDRSLAGQYSCTVTNPIGSASSSAKL 8980
Cdd:pfam00047    10 EGDSATLTCSASTGSPgPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
25227-25310 2.04e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 48.37  E-value: 2.04e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25227 DVIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPI 25306
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDV 88

                    ....
gi 1958765569 25307 TVKV 25310
Cdd:cd05891      89 TVSV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6445-6535 2.04e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.51  E-value: 2.04e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6445 PPKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVrESENVRISFVNNVATLQFAKAEPANAGKYICQVKND 6524
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIV-SSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENS 81
                            90
                    ....*....|.
gi 1958765569  6525 GGVRENMASLT 6535
Cdd:cd05747      82 EGKQEAQFTLT 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
28485-28558 2.04e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.40  E-value: 2.04e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 28485 GDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVlGSTSLFVRDATRDHRGVYTVEAKNVSG--STKAEITV 28558
Cdd:cd20976      16 GQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEA-GVGELHIQDVLPEDHGTYTCLAKNAAGqvSCSAWVTV 90
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
6539-6637 2.05e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 48.80  E-value: 2.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6539 PAVIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNV 6618
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*....
gi 1958765569  6619 GKSSCTAVVDVSDRMVPPS 6637
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPPA 99
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6929-6996 2.06e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 48.71  E-value: 2.06e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  6929 GDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRT--YFTNN---VATLVFNKVGINDSGEYTCVAENSIGTA 6996
Cdd:cd20956      16 GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgdYVTSDgdvVSYVNISSVRVEDGGEYTCTATNDVGSV 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5525-5600 2.07e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 48.16  E-value: 2.07e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5525 GSFIDLECIVAGSHPISIQWFKDDQEISASdKYKFsFHDNTafLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTV 5600
Cdd:cd05725      12 DDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEI-LDDHS--LKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7110-7186 2.07e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 48.27  E-value: 2.07e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7110 DIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGG-NYTITCVGNTphLRILKVGKGDSGQYTCQATNDVG 7186
Cdd:cd20970       6 PQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNtRYIVRENGTT--LTIRNIRRSDMGIYLCIASNGVP 81
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
8432-8511 2.08e-05

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 48.45  E-value: 2.08e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8432 KVTTGDTCTLEC-MVSGTPELSTKWFKDGKELTGDSK---YKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCTV 8507
Cdd:cd05895      10 EVAAGSKLVLRCeTSSEYPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSASA 89

                    ....
gi 1958765569  8508 SIQV 8511
Cdd:cd05895      90 NVTI 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7669-7746 2.09e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.95  E-value: 2.09e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7669 PPSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTN 7746
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
909-989 2.09e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 48.30  E-value: 2.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   909 VTVVEGESVTLECHISGYPSPKVTWYREDYQI-ESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYL 987
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFtATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569   988 AV 989
Cdd:cd05894      85 KV 86
fn3 pfam00041
Fibronectin type III domain;
28568-28649 2.13e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.18  E-value: 2.13e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28568 VGPIRFTNITGEKMTLWWEAPLNDGcAPVTHYIIEKRETSRL-AWALIEDHCEAQSYTAIKLITGNEYQFRVSAVNKFGV 28646
Cdd:pfam00041     3 PSNLTVTDVTSTSLTVSWTPPPDGN-GPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                    ...
gi 1958765569 28647 GRP 28649
Cdd:pfam00041    82 GPP 84
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8988-9078 2.15e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.40  E-value: 2.15e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8988 PPFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNyQISYLENSAHLTIVKVDKGDSGQYTCYAINEV 9067
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  9068 GKDSCTAQLNI 9078
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
8235-8322 2.15e-05

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 48.41  E-value: 2.15e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKREL--RSGKKYKIMSENllTSIHILNVDTADIGEYQCKATND 8312
Cdd:cd05736       1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDInpKLSKQLTLIANG--SELHISNVRYEDTGAYTCIAKNE 78
                            90
                    ....*....|
gi 1958765569  8313 VGSDTCVGSV 8322
Cdd:cd05736      79 GGVDEDISSL 88
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
14212-14293 2.16e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 48.38  E-value: 2.16e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14212 LTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQR-ITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEV 14290
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAAReRRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATL 88

                    ...
gi 1958765569 14291 NVL 14293
Cdd:cd05763      89 TVL 91
I-set pfam07679
Immunoglobulin I-set domain;
2318-2388 2.16e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.41  E-value: 2.16e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  2318 ILQGLSDQKVCEGDIVQLEVKVS-LENVEGVWMKDGQEVQHSDRVHIVIDKQSHMLLIEDMTKEDAGNYSFT 2388
Cdd:pfam07679     3 FTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV 74
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
1052-1127 2.19e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 48.39  E-value: 2.19e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1052 GGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRyKVSYNKQTGEcrLVISMTFADDAGEYTIVIRNKHGETSASASL 1127
Cdd:cd05730      18 GQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSE--MTILDVDKLDEAEYTCIAENKAGEQEAEIHL 90
I-set pfam07679
Immunoglobulin I-set domain;
22380-22460 2.21e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.41  E-value: 2.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22380 KVVTIRACCTLRLFVPIKGRPAPEVKWAREhGESL---DKASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFV 22456
Cdd:pfam07679     8 KDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLrssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASA 86

                    ....
gi 1958765569 22457 NVRV 22460
Cdd:pfam07679    87 ELTV 90
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
19818-19897 2.21e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 48.24  E-value: 2.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19818 TVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTE-GVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:cd20975      11 SVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQrRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQCEARLE 90

                    .
gi 1958765569 19897 V 19897
Cdd:cd20975      91 V 91
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33419-33508 2.24e-05

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 48.41  E-value: 2.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33419 VTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDG--------KAIAQSSKYKLSNDKEefiLEILKTETSDGGLYSCTV 33490
Cdd:cd05726       3 VVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGsqnllfpyQPPQPSSRFSVSPTGD---LTITNVQRSDVGYYICQA 79
                            90
                    ....*....|....*...
gi 1958765569 33491 ANSAGSVSSSCKLTIKAV 33508
Cdd:cd05726      80 LNVAGSILAKAQLEVTDV 97
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
7485-7570 2.24e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 48.37  E-value: 2.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7485 EKPEPmtvtTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLA-SLKIPSAEMNDKGLYSFEVENSVGKSS 7563
Cdd:cd05729      13 EHALP----AANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGSIN 88

                    ....*..
gi 1958765569  7564 CTVSVHV 7570
Cdd:cd05729      89 HTYDVDV 95
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2761-2839 2.25e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.27  E-value: 2.25e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2761 PKDVTALENATVAFEVSVSHDTVPVKWFHKN--VEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVV----GQLECK 2834
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSG 80

                     ....*
gi 1958765569   2835 AKLFV 2839
Cdd:smart00410    81 TTLTV 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
4671-4744 2.25e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 48.01  E-value: 2.25e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  4671 KTLEPAHIV-RGANALLQCEVAGTGPfEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANE 4744
Cdd:cd20967       1 KKAQPAVQVsKGHKIRLTVELADPDA-EVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGE 74
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4764-4849 2.27e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 48.34  E-value: 2.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4764 KKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSS-GVAVLTISDVQIGLGGKYTCLAENEAGSQT 4842
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEdGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569  4843 SVGELIV 4849
Cdd:cd20973      82 CSAELTV 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8796-8886 2.28e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.40  E-value: 2.28e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8796 PPYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDtklRPTTTCKMHFKNN--VATLVFTQVDSNDSGEYICRAEN 8873
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNA---QPLQYAADRSTCEagVGELHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|...
gi 1958765569  8874 SVGEVSSSTFLTV 8886
Cdd:cd20976      78 AAGQVSCSAWVTV 90
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4387-4476 2.29e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 48.17  E-value: 2.29e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRIT--DADNKHSLELSNLTVQDRGVYSCKASNK 4464
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIqrDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  4465 FGADICQAELTI 4476
Cdd:cd05893      81 QGRISCTGRLMV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
18032-18112 2.29e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 48.30  E-value: 2.29e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18032 LVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYT-VETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHL 18110
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVrVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569 18111 TV 18112
Cdd:cd05894      85 KV 86
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
27796-27854 2.29e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 48.10  E-value: 2.29e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 27796 KAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKY 27854
Cdd:cd20949      12 KEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEY 70
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
27792-27864 2.30e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.51  E-value: 2.30e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 27792 SVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQ 27864
Cdd:cd05747      12 SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
23753-23838 2.30e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 48.41  E-value: 2.30e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23753 VQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIEIITL 23832
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*.
gi 1958765569 23833 DKPDPP 23838
Cdd:cd05762      93 DKPDPP 98
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
19805-19897 2.30e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 48.32  E-value: 2.30e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19805 PRIELSVEMKSLLTVK-AGTNVCLDATVFGKPMPTVSWKKDSTPI-KQTEGVKmamKRNLCTLELFSVNRKDSGDYTITA 19882
Cdd:cd05856       1 PRFTQPAKMRRRVIARpVGSSVRLKCVASGNPRPDITWLKDNKPLtPPEIGEN---KKKKWTLSLKNLKPEDSGKYTCHV 77
                            90
                    ....*....|....*
gi 1958765569 19883 ENSSGSKSATIKLKV 19897
Cdd:cd05856      78 SNRAGEINATYKVDV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
17754-17813 2.31e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 47.71  E-value: 2.31e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 17754 IKGVPFPKVTWKKEDREAPTKAQIDVTPV--GSKLEIRNAAHEDGGIYSLTVENPAGSKTVS 17813
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLPPSSRDSRRSElgNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
17727-17818 2.33e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 48.35  E-value: 2.33e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17727 PPELIldaNMAREQHIKVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDVTPVGS--KLEIRNAAHEDGGIYSLTVE 17804
Cdd:cd20972       1 PPQFI---QKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDlhSLIIAEAFEEDTGRYSCLAT 77
                            90
                    ....*....|....
gi 1958765569 17805 NPAGSKTVSVKVLV 17818
Cdd:cd20972      78 NSVGSDTTSAEIFV 91
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
29956-30041 2.36e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 48.23  E-value: 2.36e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29956 PDLELaDDLKKTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDkVNRYDAGKYTIEAENQS 30035
Cdd:cd04969       1 PDFEL-NPVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGSLKIKN-VTKSDEGKYTCFAVNFF 78

                    ....*.
gi 1958765569 30036 GKKSAT 30041
Cdd:cd04969      79 GKANST 84
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5712-5787 2.36e-05

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 48.26  E-value: 2.36e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5712 GQSTTFECQVT-GTPEIRVSWYLDGNEITDLRRYGISFVDGLAT-FQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd20959      17 GMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
3577-3658 2.36e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 48.16  E-value: 2.36e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKE-LKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIIHNpdgsGTFIVNDPQRGDSGLYICKAENL 3655
Cdd:cd20978       1 PKFIQKpEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED----GTLTIINVQPEDTGYYGCVATNE 76

                    ...
gi 1958765569  3656 WGT 3658
Cdd:cd20978      77 IGD 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
22659-22749 2.37e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.40  E-value: 2.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22659 PPAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPL-KQTTRVNAESteNNSLLTIKEACREDVGHYTVKLTNS 22737
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTCEA--GVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569 22738 AGEATETLNVIV 22749
Cdd:cd20976      79 AGQVSCSAWVTV 90
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7209-7290 2.37e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 48.28  E-value: 2.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7209 SKVAKQGESIQLECK-ISGSPEIKVVWFRNDSELHESWKYNMSFVNS--VALLTINEASVEDTGDYICEAHNGVGHASCS 7285
Cdd:cd05750       8 SQTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENILGKDTVT 87

                    ....*
gi 1958765569  7286 TALKV 7290
Cdd:cd05750      88 GNVTV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6823-6898 2.37e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.95  E-value: 2.37e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6823 TFVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIEN 6898
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
5697-5787 2.38e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 48.17  E-value: 2.38e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPvLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEI-TDLRRYGISFVDGLATFQISNARVENSGTYVCEARND 5775
Cdd:cd20990       1 PHFLQAPGD-LTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIrPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNR 79
                            90
                    ....*....|..
gi 1958765569  5776 AGTASCSIELKV 5787
Cdd:cd20990      80 AGQNSFNLELVV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4292-4381 2.38e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 48.26  E-value: 2.38e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCS-IRSSNYISSLEILRTQVVDCGEYTCKASNEY 4370
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  4371 GSVSCTATLTV 4381
Cdd:cd05744      81 GENSFNAELVV 91
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4968-5029 2.39e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 48.33  E-value: 2.39e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4968 LDCKIAGSLPMRVSWFKDGKEIAASDRYQIA-FV----EGTASLEISRVDMNDAGNFTCRATNSVGS 5029
Cdd:cd20956      21 LKCVASGNPLPQITWTLDGFPIPESPRFRVGdYVtsdgDVVSYVNISSVRVEDGGEYTCTATNDVGS 87
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6353-6431 2.41e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 48.30  E-value: 2.41e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6353 PVFSSFPPVVETLKNTEVS-LECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNfhaSIHILNVDSTDIGEYHCKAQNEV 6431
Cdd:cd20957       1 PLSATIDPPVQTVDFGRTAvFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDG 77
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
906-984 2.44e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 48.28  E-value: 2.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   906 LKNVTVVEGESVTLECH-ISGYPSPKVTWYREDYQIESSIDFQITFQSG--IARLMIREAFAEDSGRFTCSAVNEAGTVS 982
Cdd:cd05750       6 MKSQTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENILGKDT 85

                    ..
gi 1958765569   983 TS 984
Cdd:cd05750      86 VT 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5414-5504 2.45e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 48.35  E-value: 2.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5414 PATITEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDV 5493
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  5494 GRSSCKASINV 5504
Cdd:cd20972      81 GSDTTSAEIFV 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8425-8511 2.47e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 48.17  E-value: 2.47e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8425 VEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFF-NKVSGLKIISVAPGDSGVYSFEVQNPVGKD 8503
Cdd:cd20990       4 LQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVReNGVHSLIIEPVTSRDAGIYTCIATNRAGQN 83

                    ....*...
gi 1958765569  8504 SCTVSIQV 8511
Cdd:cd20990      84 SFNLELVV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6636-6725 2.48e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 48.26  E-value: 2.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6636 PSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDN-VCTLQLNSLDSSDMGSYTCVAANVA 6714
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  6715 GSDECRALLTV 6725
Cdd:cd05744      81 GENSFNAELVV 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
23752-23829 2.48e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 48.16  E-value: 2.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23752 SVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTT-RINVIDSldltTLSIKETHKDDGGHYGITVANVVG--QKTAAIE 23828
Cdd:cd20978      12 VVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMeRATVEDG----TLTIINVQPEDTGYYGCVATNEIGdiYTETLLH 87

                    .
gi 1958765569 23829 I 23829
Cdd:cd20978      88 V 88
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
7870-7937 2.49e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 47.98  E-value: 2.49e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7870 GEPTTLQCKVDGTPEIRISWYKEHTKLrsaPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAV 7937
Cdd:cd05876      10 GQSLVLECIAEGLPTPTVKWLRPSGPL---PPDRVKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSA 74
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
24839-24915 2.51e-05

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 48.01  E-value: 2.51e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 24839 EDLKIEIP--VIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKessKDDFGKYSVTATNNAGTATENLSVIVLE 24915
Cdd:cd20968      13 EGLKAVLPctTMGNPKPSVSWIKGDDLIKENNRIAVLESGSLRIHNVQ---KEDAGQYRCVAKNSLGIAYSKPVTIEVE 88
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
4572-4655 2.56e-05

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 48.46  E-value: 2.56e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4572 PPSF-VKKVDPSYLMlpGESARLHCKLKGSPVIQVTWFKNN-------KELSESNTVRMsFANSEaiLDITDVKVDDSGT 4643
Cdd:cd20954       1 PPRWiVEPVDANVAA--GQDVMLHCQADGFPTPTVTWKKATgstpgeyKDLLYDPNVRI-LPNGT--LVFGHVQKENEGH 75
                            90
                    ....*....|..
gi 1958765569  4644 YSCEATNDAGSD 4655
Cdd:cd20954      76 YLCEAKNGIGSG 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2583-2664 2.58e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.95  E-value: 2.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2583 SKPLTDQTVAESQEAVFECEV-ANPESEGEWLKDGKHLTLSNNFRSESDGHKR-RLVIAAAKLDDIGEYTYKVATS---- 2656
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVeGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLcSLIISDVCGDDSGKYTCKAVNSlgea 80

                    ....*...
gi 1958765569  2657 KTSAKLKV 2664
Cdd:cd20973      81 TCSAELTV 88
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
8522-8607 2.61e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 47.98  E-value: 2.61e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8522 RKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDntcaLTVNMLEDADAGDYTCIATNVAGSDEC 8601
Cdd:cd05728       4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTIYA 79

                    ....*.
gi 1958765569  8602 SAPLTV 8607
Cdd:cd05728      80 SAELAV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6445-6536 2.66e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 2.66e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6445 PPKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESEnvRISFVNNVATLQFAKAEPANAGKYICQVKND 6524
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD--RSTCEAGVGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  6525 GGVRENMASLTV 6536
Cdd:cd20976      79 AGQVSCSAWVTV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
10-95 2.66e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.96  E-value: 2.66e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    10 QPLQSVVVLEGSAATFEAHIS-GSPVPEVSWFRDGQVIsTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQ 88
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTL-IESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                    ....*..
gi 1958765569    89 ATSTAEL 95
Cdd:pfam00047    80 ATLSTSL 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
9185-9267 2.67e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 48.27  E-value: 2.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9185 DQHLTPVTASEGDFLQLSCHVQGS-EPIrIQWLRAGREIKPSDRCSFSFASGTaVLELKDTAKADSGDYVCKASNVAGSD 9263
Cdd:cd20970       6 PQPSFTVTAREGENATFMCRAEGSpEPE-ISWTRNGNLIIEFNTRYIVRENGT-TLTIRNIRRSDMGIYLCIASNGVPGS 83

                    ....
gi 1958765569  9264 TSKC 9267
Cdd:cd20970      84 VEKR 87
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
33080-33162 2.68e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 48.37  E-value: 2.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33080 RSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKS-TFEISSVQASDEGNYSVVVENTDGKQEAQF 33158
Cdd:cd05729      12 REHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGSINHTY 91

                    ....
gi 1958765569 33159 TLTV 33162
Cdd:cd05729      92 DVDV 95
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
8062-8139 2.68e-05

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409398  Cd Length: 101  Bit Score: 48.25  E-value: 2.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8062 GESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLV------ENTATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQL 8135
Cdd:cd05735      18 GQKKEMSCTAHGEKPIIVRWEKEDTIINPSEMSRYLVTtkevgdEVISTLQILPTVREDSGFFSCHAINSYGEDRGIIQL 97

                    ....
gi 1958765569  8136 GVQE 8139
Cdd:cd05735      98 TVQE 101
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
8910-8982 2.68e-05

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 47.96  E-value: 2.68e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8910 VVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRslaGQYSCTVTNPIGSASSSAKLIL 8982
Cdd:cd05723      15 IVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKSDE---GFYQCIAENDVGNAQASAQLII 84
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2414-2490 2.68e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 47.62  E-value: 2.68e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  2414 VNVIEGTKAVLECKVSVPDvTSVKWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYKLMVGRVETSCNLSV 2490
Cdd:cd20967       7 VQVSKGHKIRLTVELADPD-AEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33441-33505 2.70e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 47.78  E-value: 2.70e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33441 GEPQPTVTWTKDGKAIA-QSSKYKLSNDKEefiLEILKTETSDGGLYSCTVANSAGS-VSSSCKLTI 33505
Cdd:cd05724      24 GHPEPTVSWRKDGQPLNlDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGErESRAARLSV 87
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7584-7666 2.70e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 47.78  E-value: 2.70e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7584 KDTTATLGASVVLECRVS-GSAPISVGWFLDGNEIISSPKCQPSFADNvcTLTLSSLEPSDTGAYTCVAANVAGQDESS- 7661
Cdd:cd05724       5 SDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDNERVRIVDDG--NLLIAEARKSDEGTYKCVATNMVGERESRa 82

                    ....*
gi 1958765569  7662 ALLTV 7666
Cdd:cd05724      83 ARLSV 87
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7579-7668 2.72e-05

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 48.41  E-value: 2.72e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7579 FIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDG--NEIISSPKCQPSFADNVCT---LTLSSLEPSDTGAYTCVAAN 7653
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGsqNLLFPYQPPQPSSRFSVSPtgdLTITNVQRSDVGYYICQALN 81
                            90
                    ....*....|....*
gi 1958765569  7654 VAGQDESSALLTVQE 7668
Cdd:cd05726      82 VAGSILAKAQLEVTD 96
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7011-7098 2.73e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.88  E-value: 2.73e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMsFVDN--VATLKILQTDLSHSGQYSCSASNP 7088
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM-LVREngRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|
gi 1958765569  7089 LGTASSTARL 7098
Cdd:cd05744      80 AGENSFNAEL 89
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
3224-3288 2.73e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 47.84  E-value: 2.73e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  3224 GRPQPKISWYKEEQLLSTGFKCKFLHDGqeyTLLLIEAFPEDAAVYTCEAKNDYGVATTSASLSV 3288
Cdd:cd04969      28 ASPKPTISWSKGTELLTNSSRICILPDG---SLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
22868-23095 2.75e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 53.41  E-value: 2.75e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22868 SMEVQWhepvsDGGSRVIGYHLE-RKERNSilWVKLNKTPipQTKFKTTGLEEGiEYEFRVSAENIVGI-GKPSKPSECY 22945
Cdd:COG4733     553 TLTVSW-----DAPAGAVAYEVEwRRDDGN--WVSVPRTS--GTSFEVPGIYAG-DYEVRVRAINALGVsSAWAASSETT 622
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22946 AAHDPcDPPGRPEAIIVTRN--SVTLQWKKPTYDGGSKItgyvvEKKELPDGRWMKASFTNIIDTQ--FEVTGLIEDHRY 23021
Cdd:COG4733     623 VTGKT-APPPAPTGLTATGGlgGITLSWSFPVDADTLRT-----EIRYSTTGDWASATVAQALYPGntYTLAGLKAGQTY 696
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 23022 EFRVIARNAAGVFSEPsesTGAITARDEVEPPRISMDPKYKDTVVVQAGESFKIDADIYGKPIPTTQWVKGDQE 23095
Cdd:COG4733     697 YYRARAVDRSGNVSAW---WVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQID 767
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
24834-24907 2.76e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 48.10  E-value: 2.76e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 24834 SVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATE 24907
Cdd:cd20949      10 TVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASD 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
32908-32971 2.76e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 47.32  E-value: 2.76e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 32908 NVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTN-YKGEASDYA 32971
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
32093-32170 2.78e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.88  E-value: 2.78e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 32093 EGGYVKYVCKIENyDQSTQVTWYFGVRQL-ENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 32170
Cdd:cd05744      14 EGRLCRFDCKVSG-LPTPDLFWQLNGKPVrPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
16335-16421 2.79e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 48.00  E-value: 2.79e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16335 KAGSQIRIPAVIKGRPTPKSSWEFDGKAK--KAMKDGIHDIPEDAqletaenssVIVIPECTRAHSGKYSITAKNKAGQK 16412
Cdd:cd05763      12 RAGSTARLECAATGHPTPQIAWQKDGGTDfpAARERRMHVMPEDD---------VFFIVDVKIEDTGVYSCTAQNSAGSI 82

                    ....*....
gi 1958765569 16413 TANCRVKVM 16421
Cdd:cd05763      83 SANATLTVL 91
fn3 pfam00041
Fibronectin type III domain;
29254-29338 2.80e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.79  E-value: 2.80e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29254 GPVTGPiEVSSVSAESCVLSWSEPKDDGGtEITNYIVEKRESGTT-AWQLINSSVKRTQIKVTHLTKYKEYCFRVSSENR 29332
Cdd:pfam00041     1 SAPSNL-TVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*.
gi 1958765569 29333 FGVSKP 29338
Cdd:pfam00041    79 GGEGPP 84
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4852-4941 2.82e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.12  E-value: 2.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4852 PAKIIERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEV 4931
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82
                            90
                    ....*....|
gi 1958765569  4932 GSSSCETTFT 4941
Cdd:cd05747      83 GKQEAQFTLT 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
30256-30340 2.82e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.77  E-value: 2.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30256 PQKTIHVPAGRPIELVIPITGRPPPTASWFFAGSKL-RESERVTVETHTkvakLTIRETTIRDTGEYMLELKNVTGTTSE 30334
Cdd:cd20978       7 PEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLqGPMERATVEDGT----LTIINVQPEDTGYYGCVATNEIGDIYT 82

                    ....*.
gi 1958765569 30335 TIKVVI 30340
Cdd:cd20978      83 ETLLHV 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8620-8700 2.82e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.95  E-value: 2.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8620 MDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSL-QDSVAELELFDVDTSQSGDYTCIVSNEAGRASCTTQL 8698
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569  8699 FV 8700
Cdd:cd20973      87 TV 88
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
5712-5787 2.83e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 48.00  E-value: 2.83e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5712 GQSTTFECQVTGTPEIRVSWYLDGNEITDlRRYGISFVDGLATFQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd05730      18 GQSVTLACDADGFPEPTMTWTKDGEPIES-GEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
31059-31135 2.83e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 47.77  E-value: 2.83e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRFGKELvqsrkykmSSDGRTHTLTVmteEQEDEGVYTCVATNEVGeVETSSKLLLQ 31135
Cdd:pfam13895    14 GEPVTLTCSAPGNPPPSYTWYKDGSAI--------SSSPNFFTLSV---SAEDSGTYTCVARNGRG-GKVSNPVELT 78
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
27398-27474 2.84e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 47.98  E-value: 2.84e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 27398 AGTSVKLRAGISGKPEPTIEWYKDDKEL-QTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRVQI 27474
Cdd:cd05729      18 AANKVRLECGAGGNPMPNITWLKDGKEFkKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6370-6441 2.85e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 47.58  E-value: 2.85e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  6370 VSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVGSDTCICAIK 6441
Cdd:cd05748      10 LRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6171-6255 2.85e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 47.78  E-value: 2.85e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6171 KPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGpKCFIGLEGStsfLNLYSVDASKTGQYTCQVTNDVGSDSCT 6250
Cdd:cd05725       3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEAS 78

                    ....*
gi 1958765569  6251 TMLLV 6255
Cdd:cd05725      79 ATLTV 83
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7487-7570 2.88e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 47.77  E-value: 2.88e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7487 PEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHitfvrnlaslkIPSAEMNDKGLYSFEVENS-VGKSSCT 7565
Cdd:pfam13895     6 PSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFF-----------TLSVSAEDSGTYTCVARNGrGGKVSNP 74

                    ....*
gi 1958765569  7566 VSVHV 7570
Cdd:pfam13895    75 VELTV 79
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
33441-33505 2.90e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 47.84  E-value: 2.90e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 33441 GEPQPTVTWTKDGKAIAQSSKYKLSNDKEefiLEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd04969      28 ASPKPTISWSKGTELLTNSSRICILPDGS---LKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
31442-31531 2.90e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 48.00  E-value: 2.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31442 FKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQeFKGGYHQLIIASVTDDDATVYQVRATNQGG 31521
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARERRMH-VMPEDDVFFIVDVKIEDTGVYSCTAQNSAG 80
                            90
                    ....*....|
gi 1958765569 31522 SVSGTASLEV 31531
Cdd:cd05763      81 SISANATLTV 90
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
33076-33162 2.90e-05

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 48.29  E-value: 2.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33076 LTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSA-----RHQVTTAKYKSTFEISSVQASDEGNYSVVVENT 33150
Cdd:cd05732       5 ITYLENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEEgdldgRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNR 84
                            90
                    ....*....|..
gi 1958765569 33151 DGKQEAQFTLTV 33162
Cdd:cd05732      85 IGGDQQSMYLEV 96
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
5887-5973 2.90e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.95  E-value: 2.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5887 IKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISF-EDSVATLQVRSVDNGHSGRYTCQAKNESGVE 5965
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  5966 RCYAFLLV 5973
Cdd:cd20973      81 TCSAELTV 88
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
1052-1124 2.92e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 47.98  E-value: 2.92e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  1052 GGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGeCRLVISMTFADDAGEYTIVIRNKHGETSAS 1124
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKG-WSLIIERAIPRDKGKYTCIVENEYGSINHT 90
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
3591-3665 2.93e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 47.91  E-value: 2.93e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  3591 GIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIIHNPdgsgTFIVNDPQRGDSGLYICKAENLWGTSTCTAEL 3665
Cdd:cd20957      16 GRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED----VLVIPSVKREDKGMYQCFVRNDGDSAQATAEL 86
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
6550-6629 2.94e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 48.00  E-value: 2.94e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6550 TVTVGETCSLECKVAGTPELSVEWYKDGKLLtSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVVDV 6629
Cdd:cd05730      14 TANLGQSVTLACDADGFPEPTMTWTKDGEPI-ESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
15627-15705 2.95e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.96  E-value: 2.95e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15627 QIMAGKTLRIPAVVTGRPVPTKVWTIEEGELDKE-RVVIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAAARVEV 15705
Cdd:cd20972      12 EVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSpDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
31059-31132 2.95e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 47.24  E-value: 2.95e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGrthTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSG---TLRISRVALHDQGQYECQAVNIVGSQRTVAQL 72
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5159-5225 2.96e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 47.58  E-value: 2.96e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5159 VTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTSIVIV 5225
Cdd:cd05748      16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
6823-6907 2.97e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 47.85  E-value: 2.97e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6823 TFVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEK-TCILEILTSTKGDAGHYSCEIENEAG 6901
Cdd:cd20975       2 TFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGgLCRLRILAAERGDAGFYTCKAVNEYG 81

                    ....*.
gi 1958765569  6902 RDSCDA 6907
Cdd:cd20975      82 ARQCEA 87
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
14907-14988 3.02e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 3.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14907 DIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEV-KASDRLTMknDHISAHLEVPKSVHADAGVYTITLENKLGSATASIN 14985
Cdd:cd20976      10 DLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTC--EAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAW 87

                    ...
gi 1958765569 14986 VKV 14988
Cdd:cd20976      88 VTV 90
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
26309-26391 3.04e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 47.91  E-value: 3.04e-05
                            10        20        30        40        50        60        70        80
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gi 1958765569 26309 DVIVVKAGEVLKINADIAGRPLPVISWAK-DGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAV 26387
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRgDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 26388 NCKV 26391
Cdd:cd05894      83 FVKV 86
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
7856-7945 3.05e-05

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 48.32  E-value: 3.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYK--EHTKLRSAPAYKMQFKNNVASLVINKVDH-----SDVGEYTC 7928
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKngQPLETDKDDPRSHRIVLPSGSLFFLRVVHgrkgrSDEGVYVC 80
                            90
                    ....*....|....*...
gi 1958765569  7929 KAENSVG-AVASSAVLVI 7945
Cdd:cd07693      81 VAHNSLGeAVSRNASLEV 98
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
22668-22745 3.05e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.12  E-value: 3.05e-05
                            10        20        30        40        50        60        70        80
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gi 1958765569 22668 TFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAG--EATETL 22745
Cdd:cd05747      12 SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGkqEAQFTL 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
1807-1887 3.05e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 47.78  E-value: 3.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSkRFRVRYDgiHYLDIVDCKSYDTGEVKVTAENPEGVTEHKVK 1886
Cdd:cd05725       4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDD--HSLKIRKVTAGDMGSYTCVAENMVGKIEASAT 80

                    .
gi 1958765569  1887 L 1887
Cdd:cd05725      81 L 81
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
4592-4661 3.06e-05

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 47.18  E-value: 3.06e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4592 RLHCKLKGSPVIQVTWFKNNKELSESNTVRMSfanSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEV 4661
Cdd:cd05746       2 QIPCSAQGDPEPTITWNKDGVQVTESGKFHIS---PEGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
22673-22749 3.07e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 47.98  E-value: 3.07e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 22673 AGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNS-LLTIKEACREDVGHYTVKLTNSAGEATETLNVIV 22749
Cdd:cd05729      18 AANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
18435-18510 3.07e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 47.84  E-value: 3.07e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 18435 GQTIRILARVKGRPEPDITWSKEGKVLVKD-KRVDLIHD-LPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVNV 18510
Cdd:cd05892      15 GDPVRLECQISAIPPPQIFWKKNNEMLQYNtDRISLYQDnCGRICLLIQNANKKDAGWYTVSAVNEAGVVSCNARLDV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7308-7382 3.08e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 47.58  E-value: 3.08e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  7308 GSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCACTVK 7382
Cdd:cd05748       7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4386-4467 3.16e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 47.94  E-value: 3.16e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4386 PPTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHS-----LELSNLTVQDRGVYSCK 4460
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYVTSDGdvvsyVNISSVRVEDGGEYTCT 80

                    ....*..
gi 1958765569  4461 ASNKFGA 4467
Cdd:cd20956      81 ATNDVGS 87
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
4953-5038 3.19e-05

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 48.07  E-value: 3.19e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4953 KPLRNVDSVVGGACRLDCKIAGSLP-MRVSWFKDGKEIAASDRYQ---IAFVEGTASLEISRVDMNDAGNFTCRATNSVG 5028
Cdd:cd05895       4 KEMKSQEVAAGSKLVLRCETSSEYPsLRFKWFKNGKEINRKNKPEnikIQKKKKKSELRINKASLADSGEYMCKVSSKLG 83
                            90
                    ....*....|
gi 1958765569  5029 SKDSRGALIV 5038
Cdd:cd05895      84 NDSASANVTI 93
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7294-7377 3.20e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 47.84  E-value: 3.20e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVR-SSKKFKVTSKNFD-TSLHIFNLEAPDIGEYHCKATNE 7371
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNCGrICLLIQNANKKDAGWYTVSAVNE 80

                    ....*.
gi 1958765569  7372 VGSDTC 7377
Cdd:cd05892      81 AGVVSC 86
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
906-989 3.20e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 47.84  E-value: 3.20e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   906 LKNVT-VVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQsgiARLMIREAFAEDSGRFTCSAVNEAGTVSTS 984
Cdd:cd04969       8 VKKKIlAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPD---GSLKIKNVTKSDEGKYTCFAVNFFGKANST 84

                    ....*
gi 1958765569   985 CYLAV 989
Cdd:cd04969      85 GSLSV 89
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
7107-7196 3.24e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 47.85  E-value: 3.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGN-YTITCVGNTPHLRILKVGKGDSGQYTCQATNDV 7185
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRrFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569  7186 GKDMCSAQLSV 7196
Cdd:cd20975      81 GARQCEARLEV 91
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
5712-5791 3.26e-05

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 48.32  E-value: 3.26e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5712 GQSTTFECQVTGTP--EIRVSWYLDGNEItDLRRYGISF-----VDGLATFQISNARVENSGTYVCEARNDAGTASCSIE 5784
Cdd:cd04970      17 GENATLQCHASHDPtlDLTFTWSFNGVPI-DLEKIEGHYrrrygKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSDSASAT 95

                    ....*..
gi 1958765569  5785 LKVKEPP 5791
Cdd:cd04970      96 LVVRGPP 102
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
28894-28957 3.26e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 47.84  E-value: 3.26e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 28894 QGRPTPTAVWSKPDSNLSIRADIHTTDSfSTLTVENCNRNDAGKYTLTVENNSGRKSITFTVKV 28957
Cdd:cd04969      27 KASPKPTISWSKGTELLTNSSRICILPD-GSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
1678-1754 3.26e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.77  E-value: 3.26e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1678 GPAHFECRLTpiGDPTMVVEWLHDGKPLEAA--------NRLRLINEFGYcsldyeaaysrDSGVITCRATNKYGTDHTS 1749
Cdd:cd20978      17 QDVTLPCQVT--GVPQPKITWLHNGKPLQGPmeratvedGTLTIINVQPE-----------DTGYYGCVATNEIGDIYTE 83

                    ....*
gi 1958765569  1750 ATLIV 1754
Cdd:cd20978      84 TLLHV 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
18021-18112 3.27e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 3.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18021 SVELDVKLIEGLVVKAGTTVRfpaiirGVPVPTAKWATDGTEITTD-DHYTVetDSFSSVLTIKNCLRKDTGEYQLTVSN 18099
Cdd:cd20976       6 SVPKDLEAVEGQDFVAQCSAR------GKPVPRITWIRNAQPLQYAaDRSTC--EAGVGELHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|...
gi 1958765569 18100 AAGTKTVAVHLTV 18112
Cdd:cd20976      78 AAGQVSCSAWVTV 90
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7577-7666 3.28e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.79  E-value: 3.28e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADN-VCTLTLSSLEPSDTGAYTCVAANVA 7655
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENgVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  7656 GQDESSALLTV 7666
Cdd:cd20990      81 GQNSFNLELVV 91
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
6636-6725 3.29e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 47.84  E-value: 3.29e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6636 PSFTRR--LKDIGGVLGTSCVLECKVAGSSPISIAWfHEKTKIVSGAKYQTTFSDNvcTLQLNSLDSSDMGSYTCVAANV 6713
Cdd:cd04969       1 PDFELNpvKKKILAAKGGDVIIECKPKASPKPTISW-SKGTELLTNSSRICILPDG--SLKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569  6714 AGSDECRALLTV 6725
Cdd:cd04969      78 FGKANSTGSLSV 89
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
7576-7667 3.30e-05

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 47.71  E-value: 3.30e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7576 PPSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFAdnvcTLTLSSLEPSDTGAYTCVAANVA 7655
Cdd:cd05851       1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSGA----VLKIFNIQPEDEGTYECEAENIK 76
                            90
                    ....*....|..
gi 1958765569  7656 GQDESSALLTVQ 7667
Cdd:cd05851      77 GKDKHQARVYVQ 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
1807-1889 3.32e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 47.84  E-value: 3.32e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIR-KSKRFRVRYD--GIHYLDIVDCKSYDTGEVKVTAENPEGVTEH 1883
Cdd:cd05892       7 PQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDncGRICLLIQNANKKDAGWYTVSAVNEAGVVSC 86

                    ....*.
gi 1958765569  1884 KVKLEI 1889
Cdd:cd05892      87 NARLDV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
1810-1879 3.32e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 47.73  E-value: 3.32e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  1810 VRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRY---DGIHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd20974      10 VVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQIsfsDGRAKLSIPAVTKANSGRYSLTATNGSG 82
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
31440-31531 3.33e-05

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 47.93  E-value: 3.33e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31440 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEF---KGG--YHQLIIASVTDDDATVYQV 31514
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRIvlpSGSlfFLRVVHGRKGRSDEGVYVC 80
                            90
                    ....*....|....*...
gi 1958765569 31515 RATNQ-GGSVSGTASLEV 31531
Cdd:cd07693      81 VAHNSlGEAVSRNASLEV 98
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
26312-26384 3.36e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.49  E-value: 3.36e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 26312 VVKAGEVLKINADIAGRPLPVISWAKDGVEIeeRAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRT 26384
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKDGVPL--LGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEAT 80
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
21592-21659 3.36e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 47.59  E-value: 3.36e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 21592 GDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTAtstiLNINECVRSDSGAYPLTAKNTVGEV 21659
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTI 77
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
3113-3193 3.39e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 47.62  E-value: 3.39e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3113 KKEVQVIEKQRAVVEFEVNEDDVDAHWYKDGIEINFQVEERHQYVVERRihRMFISEARHSDAGEYTFVAGRNRSSVTLY 3192
Cdd:cd20967       4 QPAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKR--TLTVQQASLADAGEYQCVAGGEKCSFELF 81

                    .
gi 1958765569  3193 V 3193
Cdd:cd20967      82 V 82
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
7107-7196 3.41e-05

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 47.93  E-value: 3.41e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSK--DNKE---IRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQA 7181
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKqvPGKEnliMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTA 80
                            90
                    ....*....|....*
gi 1958765569  7182 TNDVGKDMCSAQLSV 7196
Cdd:cd05765      81 RNSGGLLRANFPLSV 95
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
3304-3391 3.43e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 47.74  E-value: 3.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3304 PPAIVTPLQDAVTSEGRPARFQCQVSGTDL-KVSWYCRDKKIKPSRFFRMT--QFEDTYQLEIAEAfpEDEGTYAFVANN 3380
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPApTVTWMREGQIIVSSQRHQITstEYKSTFEISKVQM--SDEGNYTVVVEN 80
                            90
                    ....*....|.
gi 1958765569  3381 AVGQVSSTATL 3391
Cdd:cd05747      81 SEGKQEAQFTL 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
30660-30736 3.43e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.80  E-value: 3.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30660 VRQGGVIRLTIPIKGKPFPICKWTKEGQDVSKRAMIATSETHTE-----LVIKEADRNDSGTYDLVLENKCGKKTVYIKV 30734
Cdd:cd20951      12 VWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEygvhvLHIRRVTVEDSAVYSAVAKNIHGEASSSASV 91

                    ..
gi 1958765569 30735 KV 30736
Cdd:cd20951      92 VV 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
19115-19194 3.44e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.18  E-value: 3.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19115 PPEIDLDASMrklVVVRAGCPIRLFAIVRGRPAPKVTWRKVG-IDNVVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLV 19193
Cdd:pfam13927     1 KPVITVSPSS---VTVREGETVTLTCEATGSPPPTITWYKNGePISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 19194 N 19194
Cdd:pfam13927    78 N 78
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
32314-32396 3.47e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 48.00  E-value: 3.47e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32314 NAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEglDYYALHIRDTLPEDTGYYRVTATNTAGSTSCQAH 32393
Cdd:cd05730      12 NATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNE--DGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIH 89

                    ...
gi 1958765569 32394 LQV 32396
Cdd:cd05730      90 LKV 92
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
33706-33787 3.47e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 47.40  E-value: 3.47e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33706 SQNINEGQNVLFSCEISGEPSPEIEWFKNN--LPISISSNISVSRsrnmyTLEIRNASVSDSGKYTVKAKNFRGQCSATA 33783
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGgeLPKGRTKFENFNK-----TLKIENVSEADSGEYQCTASNTMGSARHTI 78

                    ....
gi 1958765569 33784 SLTV 33787
Cdd:cd05731      79 SVTV 82
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8797-8886 3.49e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 47.73  E-value: 3.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKgDTKLRPTTT---CKMHFKNNVATLVFTQVDSNDSGEYICRAEN 8873
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFR-DGQVISTSTlpgVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|...
gi 1958765569  8874 SVGEVSSSTFLTV 8886
Cdd:cd20974      80 GSGQATSTAELLV 92
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
9177-9271 3.50e-05

First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 47.97  E-value: 3.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9177 EPKKPPVFDQ-HLTPVTASEGDFLQLSCHVQgSEPIRIQWLRAGREIKPSDRCSFSfasgTAVLELKDTAKADSGDYVCK 9255
Cdd:cd04973       4 PPEAPPTYQIsEVESYSAHPGDLLQLRCRLR-DDVQSINWTKDGVQLGENNRTRIT----GEEVQIKDAVPRDSGLYACV 78
                            90
                    ....*....|....*.
gi 1958765569  9256 ASNVAGSDTSKCKVTI 9271
Cdd:cd04973      79 TSSPSGSDTTYFSVNV 94
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
12977-13046 3.51e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.58  E-value: 3.51e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 12977 FTKNLANLEVSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNC 13046
Cdd:cd20972       4 FIQKLRSQEVAEGSKVRLECRVTgNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSC 74
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
33416-33505 3.54e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 47.85  E-value: 3.54e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIaQSSKYKLSNDKEEFI--LEILKTETSDGGLYSCTVANS 33493
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPV-RPDQRRFAEEAEGGLcrLRILAAERGDAGFYTCKAVNE 79
                            90
                    ....*....|..
gi 1958765569 33494 AGSVSSSCKLTI 33505
Cdd:cd20975      80 YGARQCEARLEV 91
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
28089-28152 3.54e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 48.00  E-value: 3.54e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 28089 IGHNVHLELPYKGKPKPSISWLKDGLPLkESEYVRFSKTENKITLSIKNVKKENGGKYTVILDN 28152
Cdd:cd05730      17 LGQSVTLACDADGFPEPTMTWTKDGEPI-ESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAEN 79
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
6915-6995 3.56e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 47.93  E-value: 3.56e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTElEPLE-----ASVGDSVSLQCQVAGTPEITVSWFKGDTKLRstPEYRT---YFTNNVATLVFNKVGINDSGEYT 6986
Cdd:cd05857       1 PYWTNP-EKMEkklhaVPAANTVKFRCPAAGNPTPTMRWLKNGKEFK--QEHRIggyKVRNQHWSLIMESVVPSDKGNYT 77

                    ....*....
gi 1958765569  6987 CVAENSIGT 6995
Cdd:cd05857      78 CVVENEYGS 86
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
4392-4463 3.57e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 47.39  E-value: 3.57e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  4392 RPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDcritdadnkhsLELSNLTVQDRGVYSCKASN 4463
Cdd:pfam13895     5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN-----------FFTLSVSAEDSGTYTCVARN 65
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
6542-6619 3.60e-05

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 47.93  E-value: 3.60e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6542 IVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKI--SSLKILSV-----EKEDAGTYTFQV 6614
Cdd:cd07693       3 IVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRIVLpsGSLFFLRVvhgrkGRSDEGVYVCVA 82

                    ....*
gi 1958765569  6615 QNNVG 6619
Cdd:cd07693      83 HNSLG 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
26310-26391 3.63e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 3.63e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  26310 VIVVKAGEVLKINADIAGRPLPVISWAKDGVE-IEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVN 26388
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  26389 CKV 26391
Cdd:smart00410    83 LTV 85
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9002-9078 3.64e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 47.53  E-value: 3.64e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9002 VGESADLECHVTGTqPIK-VTWAKDNREIRSGGNYQISyLENSAHLTIVKvdKGDSGQYTCYAINEVGKDSCTAQLNI 9078
Cdd:cd20957      15 FGRTAVFNCSVTGN-PIHtVLWMKDGKPLGHSSRVQIL-SEDVLVIPSVK--REDKGMYQCFVRNDGDSAQATAELKL 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6729-6819 3.66e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 47.73  E-value: 3.66e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6729 PSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRG--ARELVKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNN 6806
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDgqVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  6807 AGQASCTTRLFVK 6819
Cdd:cd20974      81 SGQATSTAELLVL 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
22389-22460 3.66e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 3.66e-05
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  22389 TLRLFVPIKGRPAPEVKWAREHGESL---DKASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFVNVRV 22460
Cdd:smart00410    11 SVTLSCEASGSPPPEVTWYKQGGKLLaesGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
6085-6162 3.67e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.49  E-value: 3.67e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6085 VLGSSIHMECKVSGS-LPInAQWFKDGKEISTSAKyRLVCHENTvSLEVSNLELEDTANYTCKVSNVAGDNACSGILTV 6162
Cdd:cd20952      12 AVGGTVVLNCQATGEpVPT-ISWLKDGVPLLGKDE-RITTLENG-SLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8711-8797 3.68e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 48.03  E-value: 3.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8711 NDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKDSCSAQ 8790
Cdd:cd05762       9 EDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVN 88

                    ....*..
gi 1958765569  8791 ILILEPP 8797
Cdd:cd05762      89 LTVVDKP 95
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
29585-29644 3.70e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.94  E-value: 3.70e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29585 GKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVS 29644
Cdd:cd00096       9 GNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2138-2207 3.71e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 47.24  E-value: 3.71e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2138 QELQDVVAKEKDTMATFECETSEPFVKVKWYKDGIEVHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSCV 2207
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV 70
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
14212-14284 3.79e-05

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 47.62  E-value: 3.79e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 14212 LTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITienVPKKSTVTITDSKRSDTGTYIIEAVNVCGRA 14284
Cdd:cd20968       9 VTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIA---VLESGSLRIHNVQKEDAGQYRCVAKNSLGIA 78
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
12711-12783 3.80e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.49  E-value: 3.80e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12711 LRPLKDVTVTAGETATFDCELSYEDIP-VEWYLKGKKLEPND--KVVTRSEGRvHTLTLRDVKLEDAGEVQLTAKD 12783
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPdLFWQLNGKPVRPDSahKMLVRENGR-HSLIIEPVTKRDAGIYTCIARN 78
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
1044-1127 3.82e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 47.53  E-value: 3.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1044 PVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVsynkqTGECRLVISMTFADDAGEYTIVIRNKHGETSA 1123
Cdd:cd20957       8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQI-----LSEDVLVIPSVKREDKGMYQCFVRNDGDSAQA 82

                    ....
gi 1958765569  1124 SASL 1127
Cdd:cd20957      83 TAEL 86
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
15981-16198 3.86e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 53.03  E-value: 3.86e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15981 REDKGTYTITASNRLGSVFRNVHVEVYDRPSP---PRNLAVT--------DIKAESCYLTWDAPLDNGGSEITHYiidkR 16049
Cdd:COG4733     498 ENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPqwpPVNVTTSeslsvvaqGTAVTTLTVSWDAPAGAVAYEVEWR----R 573
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16050 DASrkksEW---EEVTNTAVERRygiwkLIPNGQYEFRVRAVNKYGT-SDECKSDKVVIQDpyrLPGPPGKPKVLERTKG 16125
Cdd:COG4733     574 DDG----NWvsvPRTSGTSFEVP-----GIYAGDYEVRVRAINALGVsSAWAASSETTVTG---KTAPPPAPTGLTATGG 641
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 16126 --SMLVSWTPPLDnggSPITGYwlEKREEGGAYWsrvSRAPITKVGLKGVEFSVPRLIEGVKYQFRAMAINAAGI 16198
Cdd:COG4733     642 lgGITLSWSFPVD---ADTLRT--EIRYSTTGDW---ASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGN 708
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
9672-9744 3.88e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 47.71  E-value: 3.88e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  9672 FTKRIQNIVVSEHQSATFECEVSFD-DAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIAR 9744
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEpQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAY 75
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
4301-4381 3.88e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 47.71  E-value: 3.88e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4301 LEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLT 4380
Cdd:cd20949       9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQERT 88

                    .
gi 1958765569  4381 V 4381
Cdd:cd20949      89 V 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12005-12082 3.89e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 3.89e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12005 KDVTVPEKRQARFECVLT--REANVIWSK-GPDIIKASDKFDIIADGKKHILVINDSQFDDEGVYT--AEVEGKKTSAQL 12079
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgsPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTcaATNSSGSASSGT 81

                     ...
gi 1958765569  12080 FVT 12082
Cdd:smart00410    82 TLT 84
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
16638-16725 3.89e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.57  E-value: 3.89e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16638 MEVEEGTDVNIVAKIKGVPFPTLTWFKappkkpdSKEPVVYDTHVN-KQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGT 16716
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMK-------DDNPIVESRRFQiDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGE 79

                    ....*....
gi 1958765569 16717 ASKEMRLNV 16725
Cdd:cd20973      80 ATCSAELTV 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
19421-19500 3.89e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.57  E-value: 3.89e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19421 TIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAI-HKADSSSVLIIKDVTRKDSGYYSLTAENSSGTDTQKIKVT 19499
Cdd:cd20973       8 EVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87

                    .
gi 1958765569 19500 V 19500
Cdd:cd20973      88 V 88
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
1249-1337 3.90e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 47.85  E-value: 3.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1249 FDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGN 1328
Cdd:cd20975       3 FKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGA 82

                    ....*....
gi 1958765569  1329 AICSGKLYV 1337
Cdd:cd20975      83 RQCEARLEV 91
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
33081-33163 3.90e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 47.40  E-value: 3.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33081 SITVHEGESARFSCDTDGEPVPTVTWLR-GGQVVSTSArhqvTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQFT 33159
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKlGGELPKGRT----KFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTIS 79

                    ....
gi 1958765569 33160 LTVQ 33163
Cdd:cd05731      80 VTVE 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9182-9264 3.92e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.49  E-value: 3.92e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9182 PVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCS-FSFASGTAVLELKDTAKADSGDYVCKASNVA 9260
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                    ....
gi 1958765569  9261 GSDT 9264
Cdd:cd05744      81 GENS 84
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
9192-9271 3.94e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.51  E-value: 3.94e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9192 TASEGDFLQLSCHVQGSEP-IRIQWLRAGREI--KPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSDTSKCK 9268
Cdd:cd05750      10 TVQEGSKLVLKCEATSENPsPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGN 89

                    ...
gi 1958765569  9269 VTI 9271
Cdd:cd05750      90 VTV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
6454-6527 4.02e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.57  E-value: 4.02e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6454 SLTVVAGEPAELQASI-EGAPPISVHWLKEKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDGGV 6527
Cdd:pfam00047     5 TVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5890-5964 4.02e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.57  E-value: 4.02e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5890 IENVTTVLK--SSATFQ-STVAGSPPISITWLKDDQILEENDNVHISF-EDSVATLQVRSVDNGHSGRYTCQAKNESGV 5964
Cdd:pfam00047     1 SAPPTVTVLegDSATLTcSASTGSPGPDVTWSKEGGTLIESLKVKHDNgRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
20508-20575 4.05e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.80  E-value: 4.05e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 20508 ENSNFRLKIPIKGKPAPSVSWKKGE---DPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGT 20575
Cdd:cd20951      14 EKSDAKLRVEVQGKPDPEVKWYKNGvpiDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGE 84
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7952-8041 4.07e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 47.78  E-value: 4.07e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLL--KDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNP 8029
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQIspKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  8030 LGTASSSAKLIL 8041
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
14207-14292 4.09e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.57  E-value: 4.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14207 KLLAGLTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIE-NVPKKSTVTITDSKRSDTGTYIIEAVNVCGRAT 14285
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569 14286 AVVEVNV 14292
Cdd:cd20973      82 CSAELTV 88
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
24827-24911 4.09e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 47.21  E-value: 4.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24827 KLPFNTYsVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEetatSTILHIKESSKDDFGKYSVTATNNAGT-- 24904
Cdd:cd05728       4 KVISDTE-ADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE----AGDLRITKLSLSDSGMYQCVAENKHGTiy 78

                    ....*..
gi 1958765569 24905 ATENLSV 24911
Cdd:cd05728      79 ASAELAV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
26325-26386 4.12e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.94  E-value: 4.12e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 26325 IAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMA 26386
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
23052-23152 4.13e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 47.64  E-value: 4.13e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23052 PPRISMDPkykDTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAK 23131
Cdd:cd05762       1 PPQIIQFP---EDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVE 77
                            90       100
                    ....*....|....*....|.
gi 1958765569 23132 NVAGEKSVTVNVKVLDRPGPP 23152
Cdd:cd05762      78 NKLGSRQAQVNLTVVDKPDPP 98
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33891-33984 4.19e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 47.56  E-value: 4.19e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPsDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHieNtddlTTLIIMDVQK-QDGGLYTLSL 33969
Cdd:cd20958       1 PPFIRPMG-NLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFP--N----GTLVIENVQRsSDEGEYTCTA 73
                            90
                    ....*....|....*.
gi 1958765569 33970 GNEFG-SDSATVNINI 33984
Cdd:cd20958      74 RNQQGqSASRSVFVKV 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
22374-22461 4.20e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 47.73  E-value: 4.20e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22374 LDADLRKVVtIRACCTLRLFVPIKGRPAPEVKWAREhGESLD-----KASIESTSSYTLLVVGNVNRFDSGKYILTVENS 22448
Cdd:cd20974       3 FTQPLQSVV-VLEGSTATFEAHVSGKPVPEVSWFRD-GQVIStstlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 22449 SGSKSAFVNVRVL 22461
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5137-5226 4.21e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.80  E-value: 4.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5137 FTEKLEPSQLLKKGDAtQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVES---TAVLRLTDVAIEDSGEYMCEAQNE 5213
Cdd:cd20951       3 FIIRLQSHTVWEKSDA-KLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESeygVHVLHIRRVTVEDSAVYSAVAKNI 81
                            90
                    ....*....|...
gi 1958765569  5214 AGSDHCTSIVIVK 5226
Cdd:cd20951      82 HGEASSSASVVVE 94
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8892-8989 4.21e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 47.64  E-value: 4.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8892 PPSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPI 8971
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*...
gi 1958765569  8972 GSASSSAKLILTEGKNPP 8989
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPP 98
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
20509-20584 4.23e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 47.56  E-value: 4.23e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 20509 NSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVEStavNTTLVVYDCQK-SDAGKYTITLKNVAG-TKEGTLSIKV 20584
Cdd:cd20958      15 GQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFP---NGTLVIENVQRsSDEGEYTCTARNQQGqSASRSVFVKV 89
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
32191-32292 4.25e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 47.74  E-value: 4.25e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32191 TDAMRLLERPPEFTLplynktaYVGENVRFGVTITVHPEPRVTWYKSGQKIKpgdDDKKYTFESDKGLYQLTINSVTTDD 32270
Cdd:cd05747       1 TLPATILTKPRSLTV-------SEGESARFSCDVDGEPAPTVTWMREGQIIV---SSQRHQITSTEYKSTFEISKVQMSD 70
                            90       100
                    ....*....|....*....|..
gi 1958765569 32271 DAEYAVVARNKHGEDSCKAKLT 32292
Cdd:cd05747      71 EGNYTVVVENSEGKQEAQFTLT 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
8518-8607 4.28e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 47.45  E-value: 4.28e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRK--LKETNGLSGSSVVMECKVFGSPPISVLW-LHDGNAISSGRkyqTTLTDNTcALTVNMLEDADAGDYTCIATN 8594
Cdd:cd04969       1 PDFELNpvKKKILAAKGGDVIIECKPKASPKPTISWsKGTELLTNSSR---ICILPDG-SLKIKNVTKSDEGKYTCFAVN 76
                            90
                    ....*....|...
gi 1958765569  8595 VAGSDECSAPLTV 8607
Cdd:cd04969      77 FFGKANSTGSLSV 89
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5056-5131 4.30e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.51  E-value: 4.30e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5056 GSAVCLKSAFQGSTP-LTIRWFKGDKELVSGGS--CYITKEASESSLELYAVKTTDSGTYTCKVSNVAGSVECSANLFV 5131
Cdd:cd05750      14 GSKLVLKCEATSENPsPRYRWFKDGKELNRKRPknIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
33245-33315 4.33e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.57  E-value: 4.33e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 33245 AKLTCAVESSALcaKEVAWYKDGKKLKENGHFQFHYSADGTYELKIHNLSESDCGEYVCEVSGEGGTSKTS 33315
Cdd:cd20973      15 ARFDCKVEGYPD--PEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33700-33787 4.39e-05

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 47.64  E-value: 4.39e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33700 FISQPRSQNINEGQNVLFSCEISGEPSPEIEWFK---NNL--PISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKN 33774
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKegsQNLlfPYQPPQPSSRFSVSPTGDLTITNVQRSDVGYYICQALN 81
                            90
                    ....*....|...
gi 1958765569 33775 FRGQCSATASLTV 33787
Cdd:cd05726      82 VAGSILAKAQLEV 94
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8893-8980 4.40e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.49  E-value: 4.40e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTsFLDN--IATLNIFKTDRSLAGQYSCTVTNP 8970
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM-LVREngRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|
gi 1958765569  8971 IGSASSSAKL 8980
Cdd:cd05744      80 AGENSFNAEL 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8048-8137 4.45e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 47.73  E-value: 4.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8048 PFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIR----PGgnYKMTLVENTATLTVLKVAKGDAGQYTCYAS 8123
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIStstlPG--VQISFSDGRAKLSIPAVTKANSGRYSLTAT 78
                            90
                    ....*....|....
gi 1958765569  8124 NVAGKDSCSAQLGV 8137
Cdd:cd20974      79 NGSGQATSTAELLV 92
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33079-33155 4.54e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 47.40  E-value: 4.54e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33079 PRSITVHEGESARFSCDTD-GEPVPTVTWLRGGQ--VVSTSARHQVTTAKykstFEISSVQASDEGNYSVVVENTDGKQE 33155
Cdd:cd05724       4 PSDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQplNLDNERVRIVDDGN----LLIAEARKSDEGTYKCVATNMVGERE 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
29976-30041 4.55e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.94  E-value: 4.55e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 29976 LRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTESY--SLLIVDKVNRYDAGKYTIEAENQSGKKSAT 30041
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELgnGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7483-7570 4.55e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.39  E-value: 4.55e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7483 IVEKPEP-MTVTTGNPFTLECVVAGTPELSAKWLKDGRELsSGSRHHITFVRNlaSLKIPSAEMNDKGLYSFEVENSVGK 7561
Cdd:cd20978       3 FIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDG--TLTIINVQPEDTGYYGCVATNEIGD 79

                    ....*....
gi 1958765569  7562 SSCTVSVHV 7570
Cdd:cd20978      80 IYTETLLHV 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7010-7099 4.55e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 47.24  E-value: 4.55e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7010 PPSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENlQMSFVDNVATLKILQTDLSHSGQYSCSASNPL 7089
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|
gi 1958765569  7090 GTASSTARLT 7099
Cdd:cd20976      80 GQVSCSAWVT 89
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
5883-5963 4.56e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 47.62  E-value: 4.56e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5883 PPSF-IKKIE-NVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHiSFEDSVATLQVRSVDNGHSGRYTCQAKN 5960
Cdd:cd05730       1 PPTIrARQSEvNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKY-SFNEDGSEMTILDVDKLDEAEYTCIAEN 79

                    ...
gi 1958765569  5961 ESG 5963
Cdd:cd05730      80 KAG 82
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
27790-27874 4.56e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 47.62  E-value: 4.56e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27790 RTSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSlLVIPQVTRNDTGKYILTIENGVGQpKSST 27869
Cdd:cd05730      10 EVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDGSE-MTILDVDKLDEAEYTCIAENKAGE-QEAE 87

                    ....*
gi 1958765569 27870 VSVKV 27874
Cdd:cd05730      88 IHLKV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
32897-32975 4.60e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 47.20  E-value: 4.60e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 32897 VPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNYKGEASDYATLDV 32975
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7107-7196 4.62e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.40  E-value: 4.62e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILK-VGKGDSGQYTCQATNDV 7185
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLIIEpVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  7186 GKDMCSAQLSV 7196
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7011-7099 4.67e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 47.18  E-value: 4.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSaPIH-VCWYRDGVLLRDDENlQMSFVDnvATLKILQTDLSH-SGQYSCSASNP 7088
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGY-PISsITWEKDGRRLPLNHR-QRVFPN--GTLVIENVQRSSdEGEYTCTARNQ 76
                            90
                    ....*....|..
gi 1958765569  7089 LG-TASSTARLT 7099
Cdd:cd20958      77 QGqSASRSVFVK 88
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
14-97 4.67e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 47.40  E-value: 4.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    14 SVVVLEGSAATFEAHIS-GSPVPEVSWFRDGQVISTSTlPGVQIsFSDGraRLMIPAVTKANSGRYSLRATNGSGQATS- 91
Cdd:cd05724       6 DTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDN-ERVRI-VDDG--NLLIAEARKSDEGTYKCVATNMVGERESr 81

                    ....*.
gi 1958765569    92 TAELLV 97
Cdd:cd05724      82 AARLSV 87
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
1044-1122 4.71e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 47.59  E-value: 4.71e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1044 PVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYnKQTGECRLVISMTFADDAGEYTIVIRNKHG-ETS 1122
Cdd:cd05737       8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKV-EAGRTVYFTINGVSSEDSGKYGLVVKNKYGsETS 86
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
6074-6152 4.72e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 47.33  E-value: 4.72e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6074 SFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAG 6152
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS 79
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5140-5225 4.88e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.51  E-value: 4.88e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5140 KLEP--SQLLKKGDATQLVCKVTG-TPPIKITWFANDREL-RESSKH-KMSFVESTAVLRLTDVAIEDSGEYMCEAQNEA 5214
Cdd:cd05750       2 KLKEmkSQTVQEGSKLVLKCEATSeNPSPRYRWFKDGKELnRKRPKNiKIRNKKKNSELQINKAKLEDSGEYTCVVENIL 81
                            90
                    ....*....|.
gi 1958765569  5215 GSDHCTSIVIV 5225
Cdd:cd05750      82 GKDTVTGNVTV 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
111-193 4.93e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 47.00  E-value: 4.93e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   111 QSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSlDFQISQEgdlYSLLIAEAYPEDSGTYSVNATNSVGRATSTAD 190
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDD---HSLKIRKVTAGDMGSYTCVAENMVGKIEASAT 80

                    ...
gi 1958765569   191 LLV 193
Cdd:cd05725      81 LTV 83
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
21602-21657 4.93e-05

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 47.24  E-value: 4.93e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 21602 LGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINecvRSDSGAYPLTAKNTVG 21657
Cdd:cd20968      24 MGNPKPSVSWIKGDDLIKENNRIAVLESGSLRIHNVQ---KEDAGQYRCVAKNSLG 76
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
1260-1337 5.00e-05

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 47.19  E-value: 5.00e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1260 EGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMdflqDGRASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYV 1337
Cdd:cd05723      11 ESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKI----VKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8706-8791 5.02e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 47.24  E-value: 5.02e-05
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gi 1958765569  8706 FVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVT---ASQRCNITTTEksaiLEILSSTVEDSGQYNCYIENAS 8782
Cdd:cd20976       4 FSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQyaaDRSTCEAGVGE----LHIQDVLPEDHGTYTCLAKNAA 79

                    ....*....
gi 1958765569  8783 GKDSCSAQI 8791
Cdd:cd20976      80 GQVSCSAWV 88
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
3481-3553 5.02e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 47.62  E-value: 5.02e-05
                            10        20        30        40        50        60        70
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gi 1958765569  3481 SVTVV----GCPKPKIQWFFNGMLLTpSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYGRAVCSAHLKVSPK 3553
Cdd:cd05730      20 SVTLAcdadGFPEPTMTWTKDGEPIE-SGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFAK 95
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
6365-6433 5.03e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 47.02  E-value: 5.03e-05
                            10        20        30        40        50        60
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gi 1958765569  6365 LKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKkykIASKNFHASIHILNVDSTDIGEYHCKAQNEVGS 6433
Cdd:cd05731       8 LRGGVLLLECIAEGLPTPDIRWIKLGGELPKGR---TKFENFNKTLKIENVSEADSGEYQCTASNTMGS 73
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
32306-32396 5.04e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.40  E-value: 5.04e-05
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gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSL-GPHIEIVHEGlDYYALHIRDTLPEDTGYYRVTATNT 32384
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPdSAHKMLVREN-GVHSLIIEPVTSRDAGIYTCIATNR 79
                            90
                    ....*....|..
gi 1958765569 32385 AGSTSCQAHLQV 32396
Cdd:cd20990      80 AGQNSFNLELVV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6446-6536 5.05e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.49  E-value: 5.05e-05
                            10        20        30        40        50        60        70        80
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gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDG 6525
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
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gi 1958765569  6526 GVRENMASLTV 6536
Cdd:cd05744      81 GENSFNAELVV 91
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33083-33153 5.05e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 47.55  E-value: 5.05e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33083 TVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSAR----HQVTTAKY-KSTFEISSVQASDEGNYSVVVENTDGK 33153
Cdd:cd20956      12 TLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRfrvgDYVTSDGDvVSYVNISSVRVEDGGEYTCTATNDVGS 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
26709-26786 5.06e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.11  E-value: 5.06e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 26709 TVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTFVVKV 26786
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5807-5880 5.07e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 47.14  E-value: 5.07e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5807 DVELECEVMGTTPFEVTWLKNNKEI-RSGKKYTMSEKMsvfyLHITKCAPSDVGEYQCIIANEGGSCACTARVAL 5880
Cdd:cd20957      18 TAVFNCSVTGNPIHTVLWMKDGKPLgHSSRVQILSEDV----LVIPSVKREDKGMYQCFVRNDGDSAQATAELKL 88
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
33704-33787 5.08e-05

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 47.26  E-value: 5.08e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33704 PRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQCSATA 33783
Cdd:cd05736       7 PEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDIS 86

                    ....
gi 1958765569 33784 SLTV 33787
Cdd:cd05736      87 SLFV 90
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
7293-7376 5.12e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 47.16  E-value: 5.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVK-DRKQvrSSKKFKVTSknfDTSLHIFNLEAPDIGEYHCKATNE 7371
Cdd:cd04968       1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKvDGSP--SSQWEITTS---EPVLEIPNVQFEDEGTYECEAENS 75

                    ....*
gi 1958765569  7372 VGSDT 7376
Cdd:cd04968      76 RGKDT 80
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
32093-32170 5.12e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.18  E-value: 5.12e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 32093 EGGYVKYVCKIENYDQStQVTWYFGVRQLENSEKYEITY-EDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 32170
Cdd:cd20973      11 EGSAARFDCKVEGYPDP-EVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7113-7200 5.12e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 47.64  E-value: 5.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7113 PVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSA 7192
Cdd:cd05762       8 PEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQV 87

                    ....*...
gi 1958765569  7193 QLSVKEPP 7200
Cdd:cd05762      88 NLTVVDKP 95
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
27797-27854 5.12e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 47.14  E-value: 5.12e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 27797 AGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSsslLVIPQVTRNDTGKY 27854
Cdd:cd20957      15 FGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDV---LVIPSVKREDKGMY 69
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
8998-9078 5.17e-05

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 46.85  E-value: 5.17e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8998 VDAVVGESADLECHVTGTQPiKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCyainEVGKDSCTAQLN 9077
Cdd:cd20967       7 VQVSKGHKIRLTVELADPDA-EVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC----VAGGEKCSFELF 81

                    .
gi 1958765569  9078 I 9078
Cdd:cd20967      82 V 82
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7308-7381 5.18e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.12  E-value: 5.18e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  7308 GSDVILQCE-ISGTPPFEVVWVKDRKQV--RSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCACTV 7381
Cdd:cd05750      14 GSKLVLKCEaTSENPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
21971-22050 5.19e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.79  E-value: 5.19e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21971 PRIMVdvkFKDTITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATN 22050
Cdd:pfam13927     2 PVITV---SPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
1052-1119 5.20e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 47.54  E-value: 5.20e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  1052 GGSVVFECQIGGNPKPHVYWKKSGVPLTTGYR---YKVSYNKQTgecrLVISMTFADDAGEYTIVIRNKHG 1119
Cdd:cd05857      19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKVRNQHWS----LIMESVVPSDKGNYTCVVENEYG 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
18032-18111 5.21e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 47.35  E-value: 5.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18032 LVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLT 18111
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTLT 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
1516-1609 5.22e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.00  E-value: 5.22e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEK-LKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDiivPHKYPRIRIEGTKGeaALKIDSTISQDSAWYTATAIN 1594
Cdd:cd20978       1 PKFIQKpEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGK---PLQGPMERATVEDG--TLTIINVQPEDTGYYGCVATN 75
                            90
                    ....*....|....*
gi 1958765569  1595 KAGrdTTRCKVNIEV 1609
Cdd:cd20978      76 EIG--DIYTETLLHV 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
32214-32286 5.22e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.81  E-value: 5.22e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 32214 VGENVRFGVTITVHPEPRVTWYKSGQKIKpgdDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARNKHGEDS 32286
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLK---ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
22626-22935 5.22e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 52.64  E-value: 5.22e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22626 GEEYSFRVSAQNEKGISDPRQLSVPVIAKDL-VIPPAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWH--KDDVPLKQ 22702
Cdd:COG4733     411 GRRIGGRVSSVDGRVVTLDRPVTMEAGDRYLrVRLPDGTSVARTVQSVAGRTLTVSTAYSETPEAGAVWAfgPDELETQL 490
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22703 TTRVNAESTENNSlltikeacredvghYTVKLT--NSAGEATETLNVIVLDKPGPPTGPVKMDEVTAD--------SVTL 22772
Cdd:COG4733     491 FRVVSIEENEDGT--------------YTITAVqhAPEKYAAIDAGAFDDVPPQWPPVNVTTSESLSVvaqgtavtTLTV 556
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22773 SWEPPKYDggssiNNYIVEKRDtSTTAWQIVsATVARTTIKASRLKTGcEYQFRIAAENRYGKSTyLNSEPVIAQYPFKV 22852
Cdd:COG4733     557 SWDAPAGA-----VAYEVEWRR-DDGNWVSV-PRTSGTSFEVPGIYAG-DYEVRVRAINALGVSS-AWAASSETTVTGKT 627
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22853 PGPPGTPFVTLASKD-SMEVQWHEPVsdgGSRVIGYHLERKERNSILWVKLNKTPIPQTKFKTTGLEEGIEYEFRVSAEN 22931
Cdd:COG4733     628 APPPAPTGLTATGGLgGITLSWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVD 704

                    ....
gi 1958765569 22932 IVGI 22935
Cdd:COG4733     705 RSGN 708
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
2584-2653 5.23e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.12  E-value: 5.23e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2584 KPLTDQTVAESQEAVFECEVA--NPESEGEWLKDGKHLT--LSNNFRSESDGHKRRLVIAAAKLDDIGEYTYKV 2653
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEATseNPSPRYRWFKDGKELNrkRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVV 77
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8611-8700 5.24e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 47.40  E-value: 5.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARcNVSLQ---DSVAELELFDVDTSQSGDYTCIVSN 8687
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSD-HYTIQrdlDGTCSLHTTASTLDDDGNYTIMAAN 79
                            90
                    ....*....|...
gi 1958765569  8688 EAGRASCTTQLFV 8700
Cdd:cd05893      80 PQGRISCTGRLMV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
9292-9380 5.24e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.19  E-value: 5.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKW-TKGKwrQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHG 9370
Cdd:cd20972       4 FIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWfCEGK--ELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81
                            90
                    ....*....|
gi 1958765569  9371 EIESNVNLQV 9380
Cdd:cd20972      82 SDTTSAEIFV 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8518-8607 5.25e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.40  E-value: 5.25e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTC-ALTVNMLEDADAGDYTCIATNVA 8596
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVhSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  8597 GSDECSAPLTV 8607
Cdd:cd20990      81 GQNSFNLELVV 91
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
7487-7570 5.25e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 47.14  E-value: 5.25e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7487 PEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGS-RHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGKSSCT 7565
Cdd:cd05894       2 ENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS 81

                    ....*
gi 1958765569  7566 VSVHV 7570
Cdd:cd05894      82 LFVKV 86
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5042-5131 5.27e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.00  E-value: 5.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5042 PSFVTKPES-RDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELvSGGSCYITKEasESSLELYAVKTTDSGTYTCKVSNVA 5120
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVE--DGTLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  5121 GSVECSANLFV 5131
Cdd:cd20978      78 GDIYTETLLHV 88
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
9189-9272 5.33e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 47.02  E-value: 5.33e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9189 TPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIkPSDRcsFSFASGTAVLELKDTAKADSGDYVCKASNVAGSDTSKCK 9268
Cdd:cd05731       3 SSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGEL-PKGR--TKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTIS 79

                    ....
gi 1958765569  9269 VTIK 9272
Cdd:cd05731      80 VTVE 83
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
20217-20302 5.37e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 47.64  E-value: 5.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20217 LRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIVVKVL 20296
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*.
gi 1958765569 20297 DTPGPP 20302
Cdd:cd05762      93 DKPDPP 98
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
4588-4654 5.40e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 47.21  E-value: 5.40e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMS-FANSEAILDITDVKVDDSGTYSCEATNDAGS 4654
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTkVEEKGWSLIIERAIPRDKGKYTCIVENEYGS 86
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9672-9759 5.41e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.11  E-value: 5.41e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9672 FTKRIQNIVVSEHQSATFECEVSfddAI----VTWYKGPTELTE--SQKYNFRNDGRcHYMTIHNVTPDDEGVYSVIARL 9745
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVS---GLptpdLFWQLNGKPVRPdsAHKMLVRENGR-HSLIIEPVTKRDAGIYTCIARN 78
                            90
                    ....*....|....
gi 1958765569  9746 EpRGEARSTAELYL 9759
Cdd:cd05744      79 R-AGENSFNAELVV 91
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
17742-17818 5.41e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 47.21  E-value: 5.41e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17742 IKVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDVTPVGSK---LEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd05891      13 IMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKyasLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3021-3091 5.43e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.18  E-value: 5.43e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  3021 RKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQIVDRIKI-QKEKYVHRLLIPSARMSDAGKYTVVA 3091
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEgYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKA 73
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
6-97 5.43e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 47.08  E-value: 5.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLPGVQISfSDGRARLMIPAVTKANSGRYSLRATNG 85
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEA-EGGLCRLRILAAERGDAGFYTCKAVNE 79
                            90
                    ....*....|..
gi 1958765569    86 SGQATSTAELLV 97
Cdd:cd20975      80 YGARQCEARLEV 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
18445-18506 5.46e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 47.01  E-value: 5.46e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 18445 KGRPEPDITWSKEGKVLV-KDKRVDLIHDlprVELQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd05724      23 RGHPEPTVSWRKDGQPLNlDNERVRIVDD---GNLLIAEARKSDEGTYKCVATNMVGERESRA 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
29980-30046 5.48e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.00  E-value: 5.48e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 29980 VSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDkVNRYDAGKYTIEAENQSGKKSATVLVKV 30046
Cdd:cd20978      23 CQVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIIN-VQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8421-8519 5.48e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 47.64  E-value: 5.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8421 PATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*....
gi 1958765569  8501 GKDSCTVSIQVSDRIIPPS 8519
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPPA 99
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
7293-7376 5.49e-05

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 47.32  E-value: 5.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSknfdTSLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd05851       1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSG----AVLKIFNIQPEDEGTYECEAENIK 76

                    ....
gi 1958765569  7373 GSDT 7376
Cdd:cd05851      77 GKDK 80
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6259-6349 5.50e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 47.40  E-value: 5.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFVKKLEASKIVKaGDSARLECKITGSPEIRVVWYRNEHELT-ASDKYQMTF-IDSVAVMQMNSLGTEDSGDFICEAQN 6336
Cdd:cd05893       1 PFFEMKLKHYKIFE-GMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRdLDGTCSLHTTASTLDDDGNYTIMAAN 79
                            90
                    ....*....|...
gi 1958765569  6337 PAGSTSCSTKVIV 6349
Cdd:cd05893      80 PQGRISCTGRLMV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
18431-18506 5.50e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.19  E-value: 5.50e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 18431 TVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd20972      12 EVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSA 87
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
7214-7271 5.51e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 47.20  E-value: 5.51e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7214 QGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSF-VNSVALLTINEASVEDTGDY 7271
Cdd:cd05737      15 EGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVeAGRTVYFTINGVSSEDSGKY 73
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5252-5311 5.55e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.19  E-value: 5.55e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5252 VAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLV-SLQILKFVASDAGEYQCRVTNEVGSST 5311
Cdd:pfam00047    21 STGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQsSLLISNVTKEDAGTYTCVVNNPGGSAT 81
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
104-193 5.56e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 47.40  E-value: 5.56e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLD-FQISQEGD-LYSLLIAEAYPEDSGTYSVNATNS 181
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDhYTIQRDLDgTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569   182 VGRATSTADLLV 193
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
1261-1337 5.57e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 47.17  E-value: 5.57e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1261 GMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQM-DFL-QDGR--ASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLY 1336
Cdd:cd20956      16 GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgDYVtSDGDvvSYVNISSVRVEDGGEYTCTATNDVGSVSHSARIN 95

                    .
gi 1958765569  1337 V 1337
Cdd:cd20956      96 V 96
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
5971-6066 5.58e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.11  E-value: 5.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5971 LLVQEPAqiiEKAKSVDVTekdpVTLECVVAGTPELKVKWLKDGKQIvPSRYFSMSFENNvASFRIQSVMKQDSGQYTFK 6050
Cdd:cd20952       1 IILQGPQ---NQTVAVGGT----VVLNCQATGEPVPTISWLKDGVPL-LGKDERITTLEN-GSLQIKGAEKSDTGEYTCV 71
                            90
                    ....*....|....*.
gi 1958765569  6051 VENDFGSSSCDAYLRV 6066
Cdd:cd20952      72 ALNLSGEATWSAVLDV 87
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
9085-9175 5.60e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.12  E-value: 5.60e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLSETIEETEGNSFKLEGrVAGSQPITIAWYKNNVEIHPTSNCEITFKNN--ALLLQVKKASMADAGLYTCKATN 9162
Cdd:cd05750       1 PKLKEMKSQTVQEGSKLVLKCEA-TSENPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVEN 79
                            90
                    ....*....|...
gi 1958765569  9163 DAGSALCTSSIVI 9175
Cdd:cd05750      80 ILGKDTVTGNVTV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
5511-5591 5.60e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 47.16  E-value: 5.60e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5511 PSFT--KKLRKMDSIK--GSFIDLECIVAGSHPISIQWFKDDQ-----EISASDKYKFSfhdntafLEISQLEGTDSGTY 5581
Cdd:cd05856       1 PRFTqpAKMRRRVIARpvGSSVRLKCVASGNPRPDITWLKDNKpltppEIGENKKKKWT-------LSLKNLKPEDSGKY 73
                            90
                    ....*....|
gi 1958765569  5582 TCSATNKAGH 5591
Cdd:cd05856      74 TCHVSNRAGE 83
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7107-7196 5.65e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 47.24  E-value: 5.65e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7107 PFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYtITCVGNTPHLRILKVGKGDSGQYTCQATNDVG 7186
Cdd:cd20976       2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADR-STCEAGVGELHIQDVLPEDHGTYTCLAKNAAG 80
                            90
                    ....*....|
gi 1958765569  7187 KDMCSAQLSV 7196
Cdd:cd20976      81 QVSCSAWVTV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
6733-6816 5.66e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.19  E-value: 5.66e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6733 KEPEPLEILPGKNITFT-SVIRGTPPFKVGWFRGARELVKGDRCNIYF-EDTVAELELFNIDVSQSGEYTCVVSNNAGQA 6810
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTcSASTGSPGPDVTWSKEGGTLIESLKVKHDNgRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                    ....*.
gi 1958765569  6811 SCTTRL 6816
Cdd:pfam00047    81 TLSTSL 86
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
33079-33162 5.68e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 47.21  E-value: 5.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33079 PRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVT--TAKYKStFEISSVQASDEGNYSVVVENTDGKQEA 33156
Cdd:cd05891       8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKleQGKYAS-LTIKGVTSEDSGKYSINVKNKYGGETV 86

                    ....*.
gi 1958765569 33157 QFTLTV 33162
Cdd:cd05891      87 DVTVSV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
33892-33985 5.86e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.03  E-value: 5.86e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGN 33971
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569 33972 EFGSDSATVNINIR 33985
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
9673-9757 5.93e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.18  E-value: 5.93e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9673 TKRIQNIVVSEHQSATFECEVS-FDDAIVTWYKGPTELTESQKYNFRND--GRCHyMTIHNVTPDDEGVYSVIArLEPRG 9749
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEgYPDPEVKWMKDDNPIVESRRFQIDQDedGLCS-LIISDVCGDDSGKYTCKA-VNSLG 78

                    ....*...
gi 1958765569  9750 EARSTAEL 9757
Cdd:cd20973      79 EATCSAEL 86
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
21991-22053 5.93e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.55  E-value: 5.93e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 21991 FKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGG 22053
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2588-2664 5.97e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.73  E-value: 5.97e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2588 DQTVAESQEAVFECEV-ANPESEGEWLKDG-KHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYT----YKVATSKTSAK 2661
Cdd:smart00410     3 SVTVKEGESVTLSCEAsGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTcaatNSSGSASSGTT 82

                     ...
gi 1958765569   2662 LKV 2664
Cdd:smart00410    83 LTV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
14200-14292 5.98e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.03  E-value: 5.98e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14200 PEIFldVKLLAgLTVKAGTKIELPATVTGKPEPKITWTKADTLLRP---DQRITIENVPKKSTVTITDSKRSDTGTYIIE 14276
Cdd:cd20951       1 PEFI--IRLQS-HTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAV 77
                            90
                    ....*....|....*.
gi 1958765569 14277 AVNVCGRATAVVEVNV 14292
Cdd:cd20951      78 AKNIHGEASSSASVVV 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5992-6066 5.98e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.81  E-value: 5.98e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5992 DPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRV 6066
Cdd:cd05748       8 ESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
13517-13598 6.02e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 46.76  E-value: 6.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13517 SDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTKT----VDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKAEG 13592
Cdd:cd05894       1 AENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgrvrVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHA 80

                    ....*.
gi 1958765569 13593 FINLQV 13598
Cdd:cd05894      81 SLFVKV 86
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
8242-8323 6.04e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 47.16  E-value: 6.04e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8242 FPVET--LKGADVHLECELQGTPPFQVSWYKDKRELRSgKKYKIMSENLLtsiHILNVDTADIGEYQCKATNDVGSDTCV 8319
Cdd:cd04968       7 FPADTyaLKGQTVTLECFALGNPVPQIKWRKVDGSPSS-QWEITTSEPVL---EIPNVQFEDEGTYECEAENSRGKDTVQ 82

                    ....
gi 1958765569  8320 GSVT 8323
Cdd:cd04968      83 GRII 86
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8811-8886 6.04e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 46.47  E-value: 6.04e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8811 GDSASLQCQLAGTPEIGVSWYKGDTKLrptTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGEVSSSTFLTV 8886
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQL---SVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7390-7477 6.06e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 46.62  E-value: 6.06e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7390 VKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDKGEV------IRESENVRISFVDniatlqlgspeASHSGKYVCQIK 7463
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELpkgryeILDDHSLKIRKVT-----------AGDMGSYTCVAE 69
                            90
                    ....*....|....
gi 1958765569  7464 NDAGMRECSALLTV 7477
Cdd:cd05725      70 NMVGKIEASATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
20506-20571 6.07e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.79  E-value: 6.07e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 20506 AKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKN 20571
Cdd:pfam13927    13 VREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
18215-18398 6.08e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 52.64  E-value: 6.08e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18215 PPSPPGKPVVTD---------ITENAATVSWTLPKSDggspiTGYYVERREITGKWVRVNKTPiaDLKFRVTGLYEGNtY 18285
Cdd:COG4733     528 PPQWPPVNVTTSeslsvvaqgTAVTTLTVSWDAPAGA-----VAYEVEWRRDDGNWVSVPRTS--GTSFEVPGIYAGD-Y 599
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18286 EFRVFAENLAGLSNPSPSSDPI----KACRPIKPPGPPINPKLkdktkESADLVWTKPLsdgGSPILGYVVECQKPGTTQ 18361
Cdd:COG4733     600 EVRVRAINALGVSSAWAASSETtvtgKTAPPPAPTGLTATGGL-----GGITLSWSFPV---DADTLRTEIRYSTTGDWA 671
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958765569 18362 wDRINKDELIRQCAFRVPGLIEGNEYRFRIRAANIVG 18398
Cdd:COG4733     672 -SATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
13511-13598 6.10e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.00  E-value: 6.10e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13511 PPKIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTKTVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKA 13590
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDI 80

                    ....*...
gi 1958765569 13591 EGFINLQV 13598
Cdd:cd20978      81 YTETLLHV 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4303-4381 6.10e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.00  E-value: 6.10e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4303 VALGHLAKFTCEIQGAPNVRFQWFKAGREIyesdkcSIRSSNYI---SSLEILRTQVVDCGEYTCKASNEYGSVSCTATL 4379
Cdd:cd20978      13 VKGGQDVTLPCQVTGVPQPKITWLHNGKPL------QGPMERATvedGTLTIINVQPEDTGYYGCVATNEIGDIYTETLL 86

                    ..
gi 1958765569  4380 TV 4381
Cdd:cd20978      87 HV 88
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
33072-33153 6.13e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.19  E-value: 6.13e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33072 AARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTD 33151
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ..
gi 1958765569 33152 GK 33153
Cdd:cd20972      81 GS 82
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
106-193 6.15e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.11  E-value: 6.15e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   106 FSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIqSSLDFQISQEgDLYSLLIAEAYPEDSGTYSVNATNSVGRA 185
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPL-LGKDERITTL-ENGSLQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569   186 TSTADLLV 193
Cdd:cd20952      80 TWSAVLDV 87
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
6548-6629 6.18e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 46.63  E-value: 6.18e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6548 SMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSqkhKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVV 6627
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKG---RTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISV 80

                    ..
gi 1958765569  6628 DV 6629
Cdd:cd05731      81 TV 82
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
14904-15229 6.18e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 52.25  E-value: 6.18e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14904 ETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKE----------VKASDRLTMKndhISAHLEVP-KSVHADAGVYTIT 14972
Cdd:COG4733     451 VARTVQSVAGRTLTVSTAYSETPEAGAVWAFGPDEletqlfrvvsIEENEDGTYT---ITAVQHAPeKYAAIDAGAFDDV 527
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14973 L-ENKLGSATASINVKVIglpgpckdikASDITKSSCKLTWEPPEFDggspiLHYVLE-RREAGRRTYIPVMSGENklsw 15050
Cdd:COG4733     528 PpQWPPVNVTTSESLSVV----------AQGTAVTTLTVSWDAPAGA-----VAYEVEwRRDDGNWVSVPRTSGTS---- 588
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15051 TVKDLIPNGEYFFRVKAVNKIGggeyielknpvIAQDPKQPPDPPVDVEVHNPTAKA----------MTITWKPPLYDGG 15120
Cdd:COG4733     589 FEVPGIYAGDYEVRVRAINALG-----------VSSAWAASSETTVTGKTAPPPAPTgltatgglggITLSWSFPVDADT 657
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15121 SKImgyiiEKLAKGEDRWK--RCNEHLVPVLTYTAKGLEEGKEYQFRVRAENAAGI--GEPSRATPPTKAVDPIDAPKVI 15196
Cdd:COG4733     658 LRT-----EIRYSTTGDWAsaTVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNvsAWWVSGQASADAAGILDAITGQ 732
                           330       340       350
                    ....*....|....*....|....*....|...
gi 1958765569 15197 LRTSLEVKRGDEIALDATISGSPYPTITWIKDE 15229
Cdd:COG4733     733 ILETELGQELDAIIQNATVAEVVAATVTDVTAQ 765
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
6915-6994 6.19e-05

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 47.16  E-value: 6.19e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFK---GDTKLRSTPE--YRTYFTNNVATLVFNKVGINDSGEYTCVA 6989
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKqvpGKENLIMRPNhvRGNVVVTNIGQLVIYNAQPQDAGLYTCTA 80

                    ....*
gi 1958765569  6990 ENSIG 6994
Cdd:cd05765      81 RNSGG 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
29970-30041 6.25e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.19  E-value: 6.25e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 29970 IRAGASLRLMVSVSGRPSPVITWSKKGIDLANR---AIIDNTESYSLLIVDKVNRyDAGKYTIEAENQSGKKSAT 30041
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSpdiQIHQEGDLHSLIIAEAFEE-DTGRYSCLATNSVGSDTTS 86
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
914-981 6.34e-05

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 46.71  E-value: 6.34e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   914 GESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTV 981
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMV 68
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6165-6246 6.39e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 47.17  E-value: 6.39e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6165 PPSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKC----FIGLEGS-TSFLNLYSVDASKTGQYTCQ 6239
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFrvgdYVTSDGDvVSYVNISSVRVEDGGEYTCT 80

                    ....*..
gi 1958765569  6240 VTNDVGS 6246
Cdd:cd20956      81 ATNDVGS 87
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
5994-6064 6.39e-05

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 46.41  E-value: 6.39e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5994 VTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVAsfrIQSVMKQDSGQYTFKVENDFGSSSCDAYL 6064
Cdd:cd05746       1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEGYLA---IRDVGVADQGRYECVARNTIGYASVSMVL 68
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
9293-9378 6.40e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.97  E-value: 6.40e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9293 VSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKgKWRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGEI 9372
Cdd:cd05747       7 LTKPRSLTVSEGESARFSCDVDGEPAPTVTWMR-EGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQ 85

                    ....*.
gi 1958765569  9373 ESNVNL 9378
Cdd:cd05747      86 EAQFTL 91
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
4770-4841 6.41e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 47.23  E-value: 6.41e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  4770 TALAGQTVTLQAAVRG-SEPIsVMWMKGQEVIkEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEAGSQ 4841
Cdd:cd05730      14 TANLGQSVTLACDADGfPEPT-MTWTKDGEPI-ESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQ 84
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
7860-7943 6.46e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 46.72  E-value: 6.46e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7860 EPLEHVEAAiGEPTTLQCKVDGTPEIRISWYKE-HTKLRSAPAYKMQfknNVASLVINKVDHSDVGEYTCKAENSVGAVA 7938
Cdd:cd20952       5 GPQNQTVAV-GGTVVLNCQATGEPVPTISWLKDgVPLLGKDERITTL---ENGSLQIKGAEKSDTGEYTCVALNLSGEAT 80

                    ....*
gi 1958765569  7939 SSAVL 7943
Cdd:cd20952      81 WSAVL 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8053-8128 6.46e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.97  E-value: 6.46e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8053 KPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGK 8128
Cdd:cd05747       9 KPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5229-5318 6.47e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 46.86  E-value: 6.47e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTfIQDQLVSLQILKFVASDAGEYQCRVTNEVG 5308
Cdd:cd20976       2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRST-CEAGVGELHIQDVLPEDHGTYTCLAKNAAG 80
                            90
                    ....*....|
gi 1958765569  5309 SSTCSARVTL 5318
Cdd:cd20976      81 QVSCSAWVTV 90
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
33416-33505 6.50e-05

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 47.16  E-value: 6.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDgkaiaqsskyklSNDKEEFILE-----------------ILKT 33478
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQ------------VPGKENLIMRpnhvrgnvvvtnigqlvIYNA 68
                            90       100
                    ....*....|....*....|....*..
gi 1958765569 33479 ETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd05765      69 QPQDAGLYTCTARNSGGLLRANFPLSV 95
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
7111-7186 6.53e-05

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 47.31  E-value: 6.53e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7111 IKPVSIDVIAGESADFECHVTGAQPMRVTWSK-------DNKEIRPGGNYTITCVGNtphLRILKVGKGDSGQYTCQATN 7183
Cdd:cd20954       6 VEPVDANVAAGQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYDPNVRILPNGT---LVFGHVQKENEGHYLCEAKN 82

                    ...
gi 1958765569  7184 DVG 7186
Cdd:cd20954      83 GIG 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6821-6902 6.59e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.97  E-value: 6.59e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6821 PATFVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEA 6900
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  6901 GR 6902
Cdd:cd05747      83 GK 84
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
24136-24227 6.63e-05

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 47.00  E-value: 6.63e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24136 RISMDPKFRDTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIeESARCEIKNTDFK-ALLIVKDAIRIDGGQYILRASN 24214
Cdd:cd20969       1 RAAIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHL-VSAKSNGRLTVFPdGTLEVRYAQVQDNGTYLCIAAN 79
                            90
                    ....*....|...
gi 1958765569 24215 VAGSKSFPVNVKV 24227
Cdd:cd20969      80 AGGNDSMPAHLHV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
5696-5777 6.65e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.97  E-value: 6.65e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5696 PPQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARND 5775
Cdd:cd05747       3 PATILTKPRSLTV-SEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENS 81

                    ..
gi 1958765569  5776 AG 5777
Cdd:cd05747      82 EG 83
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
18027-18112 6.71e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 46.83  E-value: 6.71e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18027 KLIEGL----VVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDS--FSSvLTIKNCLRKDTGEYQLTVSNA 18100
Cdd:cd05891       2 KVIGGLpdvvTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgkYAS-LTIKGVTSEDSGKYSINVKNK 80
                            90
                    ....*....|..
gi 1958765569 18101 AGTKTVAVHLTV 18112
Cdd:cd05891      81 YGGETVDVTVSV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8621-8687 6.74e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 46.80  E-value: 6.74e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8621 DVLTGSNVTFT-SIVKGTPPFTVSWFKGSSELVPGARCNVS-LQDSVAELELFDVDTSQSGDYTCIVSN 8687
Cdd:pfam00047     7 TVLEGDSATLTcSASTGSPGPDVTWSKEGGTLIESLKVKHDnGRTTQSSLLISNVTKEDAGTYTCVVNN 75
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
4588-4663 6.87e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.12  E-value: 6.87e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4588 GESARLHCKLKG-SPVIQVTWFKNNKELSESNTVRMSFANSE--AILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVI 4663
Cdd:cd05750      14 GSKLVLKCEATSeNPSPRYRWFKDGKELNRKRPKNIKIRNKKknSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
19411-19500 6.90e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.02  E-value: 6.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19411 PPKILMPEQITIKAGKKLRVEAHVYGKPNPICKWK-KGEDDVVTSSHLAIHKADSSSVLIIKDVTRKDSGYYSLTAENSS 19489
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQlDGKPIRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569 19490 GTDTQKIKVTV 19500
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
23747-23822 6.90e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 47.17  E-value: 6.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23747 AFSSYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVID--SLDLTTLS---IKETHKDDGGHYGITVANVVG 23821
Cdd:cd20956       7 TFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDyvTSDGDVVSyvnISSVRVEDGGEYTCTATNDVG 86

                    .
gi 1958765569 23822 Q 23822
Cdd:cd20956      87 S 87
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
8993-9085 6.96e-05

Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 409440  Cd Length: 102  Bit Score: 47.34  E-value: 6.96e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8993 IPLAP--VDAVVGESADLECHVTG--TQPIKVTWAKDNREI---RSGGNYQ-ISYLENSAHLTIVKVDKGDSGQYTCYAI 9064
Cdd:cd05854       5 ITLAPssADINQGENLTLQCHASHdpTMDLTFTWSLDDFPIdldKPNGHYRrMEVKETIGDLVIVNAQLSHAGTYTCTAQ 84
                            90       100
                    ....*....|....*....|.
gi 1958765569  9065 NEVGKDSCTAQLNIKerlTPP 9085
Cdd:cd05854      85 TVVDSASASATLVVR---GPP 102
PRK10819 PRK10819
transport protein TonB; Provisional
10937-11017 6.96e-05

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 50.45  E-value: 6.96e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10937 SMVPPKRPEAPPA--------KVPEASKEVVPE-------------KKVSVAPKKKPEaPAVKVPEAPKKVV-------- 10987
Cdd:PRK10819     51 TMVAPADLEPPQAvqpppepvVEPEPEPEPIPEppkeapvvipkpePKPKPKPKPKPK-PVKKVEEQPKREVkpveprpa 129
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 1958765569 10988 -------PEKKVPVAAPKKPEAPAAEVPEVPKA---AVPQ 11017
Cdd:PRK10819    130 spfentaPARPTSSTATAAASKPVTSVSSGPRAlsrNQPQ 169
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
4676-4746 6.96e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.82  E-value: 6.96e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  4676 AHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRL-FTQKTFVFLEITSFNSADIGDYECVVANEVG 4746
Cdd:cd05737      11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLkVEAGRTVYFTINGVSSEDSGKYGLVVKNKYG 82
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
28877-28955 6.99e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.97  E-value: 6.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28877 QTHIVRAGASIRLFIAYQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFT 28954
Cdd:cd05747      11 RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIvsSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFT 90

                    .
gi 1958765569 28955 V 28955
Cdd:cd05747      91 L 91
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
9085-9171 7.05e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 47.07  E-value: 7.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLSETiEETEGNSFKLEGRVAGSQPITIAWYKNNVEI-HPTSNCEITFKNNA-LLLQVKKASMADAGLYTCKATN 9162
Cdd:cd05892       1 PMFIQKPQNK-KVLEGDPVRLECQISAIPPPQIFWKKNNEMLqYNTDRISLYQDNCGrICLLIQNANKKDAGWYTVSAVN 79

                    ....*....
gi 1958765569  9163 DAGSALCTS 9171
Cdd:cd05892      80 EAGVVSCNA 88
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
1517-1597 7.05e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 46.84  E-value: 7.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1517 AFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRiRIEGTKGEAALKIDSTISQDSAWYTATAINKA 1596
Cdd:cd05763       1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARER-RMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSA 79

                    .
gi 1958765569  1597 G 1597
Cdd:cd05763      80 G 80
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
26706-26784 7.08e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 46.80  E-value: 7.08e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26706 KTLTVKAGSSFTMTVPFR-GRPIPNVSWSKPDTDLRTRAYI---DSTDSRTSLTIENANRNDSGKYTLTIQNVLSAASMT 26781
Cdd:pfam00047     4 PTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVkhdNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLS 83

                    ...
gi 1958765569 26782 FVV 26784
Cdd:pfam00047    84 TSL 86
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
8707-8793 7.10e-05

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 46.91  E-value: 7.10e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8707 VKRLNDYSIEKGKPLILE-GTFSGTPPISVTWKKNGVNVTASQR---CNITTTEKSAILEILSSTVEDSGQYNCYIENAS 8782
Cdd:cd05895       3 LKEMKSQEVAAGSKLVLRcETSSEYPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSSKL 82
                            90
                    ....*....|.
gi 1958765569  8783 GKDSCSAQILI 8793
Cdd:cd05895      83 GNDSASANVTI 93
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
6453-6536 7.11e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 46.76  E-value: 7.11e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6453 NSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDGGvrENMA 6532
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVG--EDHA 80

                    ....
gi 1958765569  6533 SLTV 6536
Cdd:cd05894      81 SLFV 84
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
9699-9757 7.12e-05

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 46.02  E-value: 7.12e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9699 IVTWYKGPTELTESQKYNFRNDGrchYMTIHNVTPDDEGVYSVIARlEPRGEARSTAEL 9757
Cdd:cd05746      14 TITWNKDGVQVTESGKFHISPEG---YLAIRDVGVADQGRYECVAR-NTIGYASVSMVL 68
I-set pfam07679
Immunoglobulin I-set domain;
13425-13507 7.12e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 46.87  E-value: 7.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13425 EIIRPPQDILEAPGADVIFLAELNKDKV-EVQWLRNNMIVVQGDKHQMMSEGKIHRLQICDIKPRDQGEYRFIAKDK--- 13500
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSage 81

                    ....*...
gi 1958765569 13501 -EARAKLE 13507
Cdd:pfam07679    82 aEASAELT 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
20901-20981 7.19e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 46.72  E-value: 7.19e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20901 TVKAGDSIVLSAiSILGKPLPKSSWSKAGKDIRPSDiAQITSTPTSSmLTVKYATRKDAGEYTITATNPFGTKEEHVKVS 20980
Cdd:cd20952      10 TVAVGGTVVLNC-QATGEPVPTISWLKDGVPLLGKD-ERITTLENGS-LQIKGAEKSDTGEYTCVALNLSGEATWSAVLD 86

                    .
gi 1958765569 20981 V 20981
Cdd:cd20952      87 V 87
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
30660-30728 7.19e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.97  E-value: 7.19e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 30660 VRQGGVIRLTIPIKGKPFPICKWTKEGQDV--SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKK 30728
Cdd:cd05747      15 VSEGESARFSCDVDGEPAPTVTWMREGQIIvsSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQ 85
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
4588-4663 7.21e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.82  E-value: 7.21e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANseaiLDITDVKVDDSGTYSCEATNDAGSDSCSTEVVI 4663
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
33423-33505 7.31e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 46.83  E-value: 7.31e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33423 RDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLS-NDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSC 33501
Cdd:cd05729      12 REHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTkVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTY 91

                    ....
gi 1958765569 33502 KLTI 33505
Cdd:cd05729      92 DVDV 95
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7299-7374 7.36e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 46.62  E-value: 7.36e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7299 KPPPVGALKGSDVILQCEISGTPPFEVVWVKD-------RKQVRSskkfkvtsknfDTSLHIFNLEAPDIGEYHCKATNE 7371
Cdd:cd05725       3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEdgelpkgRYEILD-----------DHSLKIRKVTAGDMGSYTCVAENM 71

                    ...
gi 1958765569  7372 VGS 7374
Cdd:cd05725      72 VGK 74
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
7952-8035 7.39e-05

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 47.16  E-value: 7.39e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSfvHHVAT-------LQIL--QTDQSHVGQY 8022
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRS--HRIVLpsgslffLRVVhgRKGRSDEGVY 78
                            90
                    ....*....|...
gi 1958765569  8023 NCSASNPLGTASS 8035
Cdd:cd07693      79 VCVAHNSLGEAVS 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33609-33689 7.41e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.73  E-value: 7.41e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  33609 STQMNITSGQRVTLKANIAGATD--VKWVLNGTE-LSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCIGKTSQGVVKCQ 33685
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPpeVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                     ....
gi 1958765569  33686 FDLT 33689
Cdd:smart00410    81 TTLT 84
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
24147-24217 7.46e-05

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 46.67  E-value: 7.46e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 24147 IVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARcEIKNTDFKALLIVKDAIRIDGGQYILRASNVAG 24217
Cdd:cd04978       9 LVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPE-DMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
22660-22739 7.50e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 46.69  E-value: 7.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22660 PAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENN-SLLTIKEACREDVGHYTVKLTNSA 22738
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGlCRLRILAAERGDAGFYTCKAVNEY 80

                    .
gi 1958765569 22739 G 22739
Cdd:cd20975      81 G 81
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
899-990 7.50e-05

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 46.94  E-value: 7.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQItfqSGiARLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd05851       1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISM---SG-AVLKIFNIQPEDEGTYECEAENIK 76
                            90
                    ....*....|..
gi 1958765569   979 GTVSTSCYLAVQ 990
Cdd:cd05851      77 GKDKHQARVYVQ 88
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
24824-24913 7.53e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.02  E-value: 7.53e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTT--RVNVEETATSTILhIKESSKDDFGKYSVTATNN 24901
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSahKMLVRENGVHSLI-IEPVTSRDAGIYTCIATNR 79
                            90
                    ....*....|..
gi 1958765569 24902 AGTATENLSVIV 24913
Cdd:cd20990      80 AGQNSFNLELVV 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
1252-1337 7.58e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 46.74  E-value: 7.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1252 RIKNYRILEGMGVTFHCK-MSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRAS-LRIPVVLPEDEGIYTAFASNIKGNA 1329
Cdd:cd05750       5 EMKSQTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSeLQINKAKLEDSGEYTCVVENILGKD 84

                    ....*...
gi 1958765569  1330 ICSGKLYV 1337
Cdd:cd05750      85 TVTGNVTV 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7583-7666 7.62e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 46.68  E-value: 7.62e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7583 LKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCqpSFADNvCTLTLSSLEPSDTGAYTCVAANVAGQDESSA 7662
Cdd:cd04969       9 KKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRI--CILPD-GSLKIKNVTKSDEGKYTCFAVNFFGKANSTG 85

                    ....
gi 1958765569  7663 LLTV 7666
Cdd:cd04969      86 SLSV 89
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
23742-23829 7.68e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.82  E-value: 7.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23742 PDVrpafssYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINV-IDSLDLTTLSIKETHKDDGGHYGITVANVV 23820
Cdd:cd05737       8 PDV------VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLkVEAGRTVYFTINGVSSEDSGKYGLVVKNKY 81

                    ....*....
gi 1958765569 23821 GQKTAAIEI 23829
Cdd:cd05737      82 GSETSDVTV 90
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33891-33984 7.69e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 46.78  E-value: 7.69e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQE--QQGRFHIENTDDLTTLIIMDVQKQDGGLYTLS 33968
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPrfRVGDYVTSDGDVVSYVNISSVRVEDGGEYTCT 80
                            90
                    ....*....|....*.
gi 1958765569 33969 LGNEFGSDSATVNINI 33984
Cdd:cd20956      81 ATNDVGSVSHSARINV 96
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7294-7381 7.69e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 46.96  E-value: 7.69e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSK--KFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNE 7371
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|
gi 1958765569  7372 VGSDTCACTV 7381
Cdd:cd20974      81 SGQATSTAEL 90
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8062-8137 7.72e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 46.08  E-value: 7.72e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8062 GESGSFKCHVTGTAPIKITWAKdnreirpGGNY----KMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQLGV 8137
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTK-------GGSQlsvdRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
33080-33162 7.78e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 46.68  E-value: 7.78e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33080 RSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTakyKSTFEISSVQASDEGNYSVVVENTDGKQEAQFT 33159
Cdd:cd04969      10 KKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILP---DGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGS 86

                    ...
gi 1958765569 33160 LTV 33162
Cdd:cd04969      87 LSV 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
24149-24220 7.82e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 46.81  E-value: 7.82e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 24149 VNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKS 24220
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDT 84
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
31144-31229 7.85e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 46.68  E-value: 7.85e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31144 YPLKEKYYGAVGSTLRLHVMYIGRPVPAMTWYHGQKLLQNSESITIenTEHYThLVMKNVQrKTHAGKYKVQLSNVFGTV 31223
Cdd:cd04969       6 NPVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICI--LPDGS-LKIKNVT-KSDEGKYTCFAVNFFGKA 81

                    ....*...
gi 1958765569 31224 D--AILDV 31229
Cdd:cd04969      82 NstGSLSV 89
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
23460-23542 7.91e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.82  E-value: 7.91e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23460 LRKVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIR--DAAIIDV-TSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSA 23536
Cdd:cd05737       7 LPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAflDHCNLKVeAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETS 86

                    ....*.
gi 1958765569 23537 FVTVRV 23542
Cdd:cd05737      87 DVTVSV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
19811-19897 7.92e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 46.56  E-value: 7.92e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19811 VEMKSLLTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKS 19890
Cdd:cd20949       3 TENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82

                    ....*..
gi 1958765569 19891 ATIKLKV 19897
Cdd:cd20949      83 DMQERTV 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
29167-29249 7.92e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 46.96  E-value: 7.92e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29167 QLITCKAGSTFTIDVPISGRPAPKVTWKLEE--MRLKETDRMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFT 29244
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*
gi 1958765569 29245 ITVVV 29249
Cdd:cd20974      88 AELLV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5721-5787 7.95e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.43  E-value: 7.95e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5721 VTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd05748      16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
31045-31135 7.95e-05

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 46.55  E-value: 7.95e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31045 PGVRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSdgrtHTLTVMTEEQEDEGVYTCVATNEVG 31124
Cdd:cd05851       2 ADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSG----AVLKIFNIQPEDEGTYECEAENIKG 77
                            90
                    ....*....|.
gi 1958765569 31125 EVETSSKLLLQ 31135
Cdd:cd05851      78 KDKHQARVYVQ 88
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
8893-8978 7.97e-05

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 46.69  E-value: 7.97e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDNIATLNIFK--TDRSLAGQYSCTVTNP 8970
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQLIIasVTDDDATVYQVRATNQ 81

                    ....*...
gi 1958765569  8971 IGSASSSA 8978
Cdd:cd20971      82 GGSVSGTA 89
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
5416-5504 7.99e-05

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 47.16  E-value: 7.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5416 TITEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQEL---TLGPKYKISVTDTVSI--LKIISTEK--KDSGEYTFE 5488
Cdd:cd07693       2 RIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLetdKDDPRSHRIVLPSGSLffLRVVHGRKgrSDEGVYVCV 81
                            90
                    ....*....|....*..
gi 1958765569  5489 VQNDVGRS-SCKASINV 5504
Cdd:cd07693      82 AHNSLGEAvSRNASLEV 98
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4227-4281 8.03e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.17  E-value: 8.03e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  4227 EVNWYFKGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNGKAMTS 4281
Cdd:cd00096      14 TITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
24838-24913 8.04e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 46.63  E-value: 8.04e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 24838 GEDLKIEIPVIGRPRPKISWVKDGEPL--RQTTRVNVEETatstiLHIKESSKDDFGKYSVTATNNAGTATENLSVIV 24913
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIKLGGELpkGRTKFENFNKT-----LKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
18034-18112 8.06e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 46.81  E-value: 8.06e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 18034 VKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLTV 18112
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
4393-4476 8.10e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 46.77  E-value: 8.10e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4393 PKSLTTFVGKAAKFLCTVSGTPVIETIWQK-DGtalSPSPDCRITDADNkhSLELSNLTVQDRGVYSCKASNKFGADICQ 4471
Cdd:cd04968       8 PADTYALKGQTVTLECFALGNPVPQIKWRKvDG---SPSSQWEITTSEP--VLEIPNVQFEDEGTYECEAENSRGKDTVQ 82

                    ....*
gi 1958765569  4472 AELTI 4476
Cdd:cd04968      83 GRIIV 87
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
11643-11714 8.12e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 46.42  E-value: 8.12e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 11643 SVGSSAIFECLVSPST--AITTWMKDGSNIRESPKHrFIADGKDRK--LHIIDVQLSDAGEYTCVL--RLGNKEKTST 11714
Cdd:pfam00047     9 LEGDSATLTCSASTGSpgPDVTWSKEGGTLIESLKV-KHDNGRTTQssLLISNVTKEDAGTYTCVVnnPGGSATLSTS 85
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
7591-7656 8.15e-05

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 46.67  E-value: 8.15e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7591 GASVVLECRVSGSAPISVGWFLDGNEIISSPKcQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAG 7656
Cdd:cd04978      14 GETGELICEAEGNPQPTITWRLNGVPIEPAPE-DMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8331-8418 8.20e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 46.62  E-value: 8.20e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8331 VKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIVRESDNIWISHSenvatLHFSRAEPANAGKYTCQIKNDAGVQ 8410
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILDDHS-----LKIRKVTAGDMGSYTCVAENMVGKI 75

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gi 1958765569  8411 ECYATLSV 8418
Cdd:cd05725      76 EASATLTV 83
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
15922-15998 8.21e-05

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 46.77  E-value: 8.21e-05
                            10        20        30        40        50        60        70        80
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gi 1958765569 15922 VKAGEPVNIPADVTGLPMPKIEWSKN----EKVIEKPTDAL-NITKEEVSrseaktELSIPKAVREDKGTYTITASNRLG 15996
Cdd:cd05765      12 VKVGETASFHCDVTGRPQPEITWEKQvpgkENLIMRPNHVRgNVVVTNIG------QLVIYNAQPQDAGLYTCTARNSGG 85

                    ..
gi 1958765569 15997 SV 15998
Cdd:cd05765      86 LL 87
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
32316-32389 8.23e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 46.56  E-value: 8.23e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 32316 ECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDyYALHIRDTLPEDTGYYRVTATNTAGSTS 32389
Cdd:cd20949      10 TVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILA-DGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
23750-23825 8.25e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.58  E-value: 8.25e-05
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gi 1958765569 23750 SYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTA 23825
Cdd:cd05747      12 SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEA 87
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
4963-5032 8.30e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.82  E-value: 8.30e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  4963 GGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEG-TASLEISRVDMNDAGNFTCRATNSVGSKDS 5032
Cdd:cd05737      16 GKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGrTVYFTINGVSSEDSGKYGLVVKNKYGSETS 86
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7293-7374 8.31e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 46.78  E-value: 8.31e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFK----VTSKNFDTS-LHIFNLEAPDIGEYHCK 7367
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRvgdyVTSDGDVVSyVNISSVRVEDGGEYTCT 80

                    ....*..
gi 1958765569  7368 ATNEVGS 7374
Cdd:cd20956      81 ATNDVGS 87
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
20508-20574 8.32e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 46.69  E-value: 8.32e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 20508 ENSNFRLKIPIKGKPAPSVSWKKGEDPLATDT-RVSV-ESTAVNTTLVVYDCQKSDAGKYTITLKNVAG 20574
Cdd:cd05892      14 EGDPVRLECQISAIPPPQIFWKKNNEMLQYNTdRISLyQDNCGRICLLIQNANKKDAGWYTVSAVNEAG 82
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7855-7945 8.33e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 46.68  E-value: 8.33e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7855 PPYFIEPLEHVE-AAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPayKMQFKNNvASLVINKVDHSDVGEYTCKAENS 7933
Cdd:cd04969       1 PDFELNPVKKKIlAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS--RICILPD-GSLKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569  7934 VGAVASSAVLVI 7945
Cdd:cd04969      78 FGKANSTGSLSV 89
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8611-8700 8.34e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.62  E-value: 8.34e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDP-MDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVpGARCNVSLQDSVaeLELFDVDTSQSGDYTCIVSNEA 8689
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ-GPMERATVEDGT--LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  8690 GRASCTTQLFV 8700
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
33229-33315 8.38e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 46.81  E-value: 8.38e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33229 PPKITQSLKAEASRDIAKLTCAVESSALCAKEVAWYKDGKKLKENGHFQFHYSADgTYELKIHNLSESDCGEYVCEVSGE 33308
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGD-LHSLIIAEAFEEDTGRYSCLATNS 79

                    ....*..
gi 1958765569 33309 GGTSKTS 33315
Cdd:cd20972      80 VGSDTTS 86
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
18719-18805 8.38e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.82  E-value: 8.38e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18719 LSGVLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTSAESSkFSLTKAKRSDGGKYVVTATNPAGSFV 18798
Cdd:cd05737       7 LPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVY-FTINGVSSEDSGKYGLVVKNKYGSET 85

                    ....*..
gi 1958765569 18799 AYATVNV 18805
Cdd:cd05737      86 SDVTVSV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
2038-2128 8.40e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 46.69  E-value: 8.40e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERS-DRIYWYwpEDN---VCeLVIRDVTAEDSASIMVKA 2113
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNtDRISLY--QDNcgrIC-LLIQNANKKDAGWYTVSA 77
                            90
                    ....*....|....*
gi 1958765569  2114 INIAGETSSHAFLLV 2128
Cdd:cd05892      78 VNEAGVVSCNARLDV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
33700-33787 8.44e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 46.78  E-value: 8.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33700 FISQP---RSQNINE--GQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRnmYTLEIRNASVSDSGKYTVKAKN 33774
Cdd:cd05856       2 RFTQPakmRRRVIARpvGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKK--WTLSLKNLKPEDSGKYTCHVSN 79
                            90
                    ....*....|...
gi 1958765569 33775 FRGQCSATASLTV 33787
Cdd:cd05856      80 RAGEINATYKVDV 92
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
31059-31132 8.46e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 46.83  E-value: 8.46e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTH-TLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGSINHTYDV 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
29972-30045 8.50e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 46.64  E-value: 8.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29972 AGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDN----TESY-SLLIVDKVNRYDAGKYTIEAENQSG--KKSATVLV 30044
Cdd:cd20951      14 EKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKykieSEYGvHVLHIRRVTVEDSAVYSAVAKNIHGeaSSSASVVV 93

                    .
gi 1958765569 30045 K 30045
Cdd:cd20951      94 E 94
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
8703-8793 8.50e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 46.39  E-value: 8.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8703 PAIFVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKngVNVTASQRCNITTTEksAILEILSSTVEDSGQYNCYIENAS 8782
Cdd:cd04968       1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRK--VDGSPSSQWEITTSE--PVLEIPNVQFEDEGTYECEAENSR 76
                            90
                    ....*....|.
gi 1958765569  8783 GKDSCSAQILI 8793
Cdd:cd04968      77 GKDTVQGRIIV 87
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
1264-1328 8.64e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 46.77  E-value: 8.64e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  1264 VTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGN 1328
Cdd:cd05857      22 VKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGS 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4854-4929 8.64e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.40  E-value: 8.64e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4854 KIIERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISN 4929
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10810-11303 8.73e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 51.69  E-value: 8.73e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10810 AKVPEIPKKPEEKVSVPVPKKEKAPPAKV-------PEVPKKPVPEEKapvpvpkkvePPPAKVPEVPKKPVPEKK---V 10879
Cdd:NF033839    123 SQLQKLMMESQSKVDEAVSKFEKDSSSSSssgsstkPETPQPENPEHQ----------KPTTPAPDTKPSPQPEGKkpsV 192
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10880 PAPTPKKVEAPPAKAPEVPPKEVTPEKKVPVVPPKKPEAPPPKVPEPPKEVVPEKKVSMVPPKRPEAPPAKVPEASKEVV 10959
Cdd:NF033839    193 PDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVV 272
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10960 PEKKVSVAP-------KKKPEAPAVKVPEAPKKVVPEKKVPVAAPKKPEAPAAEVPEVPKAAVPQKKIPEavppkpespp 11032
Cdd:NF033839    273 TKFKKGLTQdtpkepgNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPE---------- 342
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11033 pevyeepaeeivpeeppeevveepepapppkvtvppkkpvpekkappavvkkpepppakapeVPKEapPEKKVPSVVPKk 11112
Cdd:NF033839    343 --------------------------------------------------------------VKPQ--LETPKPEVKPQ- 357
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11113 PEAPPAKVPEVPKEVVPEkkvaVPKKPEVPPAKVPEVPKKPVVEEKPViEEKPAIPVAEKVESPPTEVYEEPEevaaqee 11192
Cdd:NF033839    358 PEKPKPEVKPQPEKPKPE----VKPQPETPKPEVKPQPEKPKPEVKPQ-PEKPKPEVKPQPEKPKPEVKPQPE------- 425
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11193 epapvveeeeyeappppapeIPVPQVPEEPKKVVPEkkypvikkpeppppkvpevsKKPAPMKKVPVVKKPEPPEAEvpe 11272
Cdd:NF033839    426 --------------------KPKPEVKPQPEKPKPE--------------------VKPQPEKPKPEVKPQPETPKP--- 462
                           490       500       510
                    ....*....|....*....|....*....|.
gi 1958765569 11273 vpkklapvKKEPVPVTKKPEVLPEkvPEAPK 11303
Cdd:NF033839    463 --------EVKPQPEKPKPEVKPQ--PEKPK 483
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
25229-25300 8.75e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.58  E-value: 8.75e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 25229 IIVRAGETFVLEADIRGKPIPDIVWSKDGNELeETAARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGG 25300
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQII-VSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
4582-4664 8.78e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 46.25  E-value: 8.78e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4582 SYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESntvRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEV 4661
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKG---RTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISV 80

                    ...
gi 1958765569  4662 VIK 4664
Cdd:cd05731      81 TVE 83
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8996-9076 8.80e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 46.63  E-value: 8.80e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8996 APVDAVV--GESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAH-LTIVKVDKGDSGQYTCYAINEVGKDSC 9072
Cdd:cd20990       6 APGDLTVqeGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHsLIIEPVTSRDAGIYTCIATNRAGQNSF 85

                    ....
gi 1958765569  9073 TAQL 9076
Cdd:cd20990      86 NLEL 89
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
24141-24227 8.88e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 46.83  E-value: 8.88e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24141 PKFRDT-------IVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEI-KNTDFKALLIVKDAIRIDGGQYILRA 24212
Cdd:cd05729       1 PRFTDTekmeereHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGtKVEEKGWSLIIERAIPRDKGKYTCIV 80
                            90
                    ....*....|....*
gi 1958765569 24213 SNVAGSKSFPVNVKV 24227
Cdd:cd05729      81 ENEYGSINHTYDVDV 95
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8425-8511 8.96e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 46.23  E-value: 8.96e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8425 VEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTgDSKYKISFFNKvsgLKIISVAPGDSGVYSFEVQNPVGKDS 8504
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELP-KGRYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  8505 CTVSIQV 8511
Cdd:cd05725      77 ASATLTV 83
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
28884-28957 9.04e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 46.78  E-value: 9.04e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 28884 GASIRLFIAYQGRPTPTAVWSKPDSNLSIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFTVKV 28957
Cdd:cd05856      19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
24824-24906 9.05e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 46.63  E-value: 9.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLR-QTTRVNVEETATSTI-LHIKESSKDDFGKYSVTATNN 24901
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDLDGTCsLHTTASTLDDDGNYTIMAANP 80

                    ....*
gi 1958765569 24902 AGTAT 24906
Cdd:cd05893      81 QGRIS 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
33898-33984 9.17e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 46.69  E-value: 9.17e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENTDDLTtLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:cd05892       7 PQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRIC-LLIQNANKKDAGWYTVSAVNEAGVVS 85

                    ....*..
gi 1958765569 33978 ATVNINI 33984
Cdd:cd05892      86 CNARLDV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2756-2836 9.25e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.02  E-value: 9.25e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2756 KIIKKPKDVTALENATVAFEVSVSHDTVP-VKWFHKNVEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTavvgqleCK 2834
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGSPPPtITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYT-------CV 75

                    ..
gi 1958765569  2835 AK 2836
Cdd:pfam13927    76 AS 77
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
2038-2128 9.26e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 46.58  E-value: 9.26e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNG--VKIERSDRIYWYWPEDNvCELVIRDVTAEDSASIMVKAIN 2115
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGR-AKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|...
gi 1958765569  2116 IAGETSSHAFLLV 2128
Cdd:cd20974      80 GSGQATSTAELLV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4864-4943 9.26e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 46.58  E-value: 9.26e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4864 VTAGDPATLEYTVSGTPELKPKWYKDGR--PLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFT 4941
Cdd:cd20974      12 VLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELL 91

                    ..
gi 1958765569  4942 VL 4943
Cdd:cd20974      92 VL 93
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
5150-5215 9.29e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 46.85  E-value: 9.29e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5150 GDATQLVCKVTGTPPIKITWFANDRELrESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAG 5215
Cdd:cd05730      18 GQSVTLACDADGFPEPTMTWTKDGEPI-ESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAG 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8622-8701 9.29e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.04  E-value: 9.29e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8622 VLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAGRASCTtqLFVK 8701
Cdd:cd05748       4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSAT--INVK 81
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
31557-31620 9.31e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.78  E-value: 9.31e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31557 VSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFG 31620
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISN-VTLEDSGTYTCVASNSAG 63
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8248-8315 9.33e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 46.23  E-value: 9.33e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8248 KGADVHLECELQGTPPFQVSWYKDKRELRSGKKYkimsenlltsiHILNVDTADIGEYQCKATNDVGS 8315
Cdd:pfam13895    13 EGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF-----------FTLSVSAEDSGTYTCVARNGRGG 69
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
19814-19888 9.33e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 46.44  E-value: 9.33e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 19814 KSLLTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRnlcTLELFSVNRKDSGDYTITAENSSGS 19888
Cdd:cd05876       2 SSSLVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNK---TLQLLNVGESDDGEYVCLAENSLGS 73
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
14212-14286 9.36e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.58  E-value: 9.36e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 14212 LTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATA 14286
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEA 87
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
28485-28560 9.41e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 46.73  E-value: 9.41e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 28485 GDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGsTSLFVRDATRDHRGVYTVEAKN-VSGSTKAEITVKV 28560
Cdd:cd20970      17 GENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENG-TTLTIRNIRRSDMGIYLCIASNgVPGSVEKRITLQV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7762-7852 9.42e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 46.42  E-value: 9.42e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7762 PATFVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEA 7841
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                            90
                    ....*....|.
gi 1958765569  7842 GQDICEALVSV 7852
Cdd:cd20972      81 GSDTTSAEIFV 91
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
8811-8887 9.52e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 46.44  E-value: 9.52e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8811 GDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMhfkNNVATLVFTQVDSNDSGEYICRAENSVGEVSSSTFLTVQ 8887
Cdd:cd05876      10 GQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQ---NHNKTLQLLNVGESDDGEYVCLAENSLGSARHAYYVTVE 83
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
6551-6629 9.53e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 46.77  E-value: 9.53e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6551 VTVGETCSLECKVAGTPELSVEWYKDGKLLtsSQKHK---FSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVV 6627
Cdd:cd05857      16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEF--KQEHRiggYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHL 93

                    ..
gi 1958765569  6628 DV 6629
Cdd:cd05857      94 DV 95
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8798-8886 9.57e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.04  E-value: 9.57e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8798 YFVKQLEPLKVTVGdsaslqcqLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGE 8877
Cdd:cd05748       2 IVVRAGESLRLDIP--------IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGE 73

                    ....*....
gi 1958765569  8878 VSSSTFLTV 8886
Cdd:cd05748      74 KSATINVKV 82
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
6073-6152 9.58e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 46.39  E-value: 9.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTK----KLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLevSNLELEDTANYTCKVS 6148
Cdd:cd05856       1 PRFTQpakmRRRVIARPVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSL--KNLKPEDSGKYTCHVS 78

                    ....
gi 1958765569  6149 NVAG 6152
Cdd:cd05856      79 NRAG 82
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
4952-5040 9.59e-05

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 46.47  E-value: 9.59e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4952 TKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRyqIAFVEgTASLEISRVDMNDAGNFTCRATNSVGSKD 5031
Cdd:cd20968       3 TRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNR--IAVLE-SGSLRIHNVQKEDAGQYRCVAKNSLGIAY 79

                    ....*....
gi 1958765569  5032 SRGALIVQE 5040
Cdd:cd20968      80 SKPVTIEVE 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
23742-23822 9.61e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 46.41  E-value: 9.61e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23742 PDVRPaFSSYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSldlTTLSIKETHKD-DGGHYGITVANVV 23820
Cdd:cd20958       2 PFIRP-MGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPN---GTLVIENVQRSsDEGEYTCTARNQQ 77

                    ..
gi 1958765569 23821 GQ 23822
Cdd:cd20958      78 GQ 79
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
7307-7377 9.67e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 46.69  E-value: 9.67e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  7307 KGSDVILQCEISGTPPFEVVWVKDRKQVR-SSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTC 7377
Cdd:cd20975      14 EGQDVIMSIRVQGEPKPVVSWLRNRQPVRpDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQC 85
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7577-7666 9.69e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 46.63  E-value: 9.69e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIisSPKCQ----PSFADNVCTLTLSSLEPSDTGAYTCVAA 7652
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQI--SPKSDhytiQRDLDGTCSLHTTASTLDDDGNYTIMAA 78
                            90
                    ....*....|....
gi 1958765569  7653 NVAGQDESSALLTV 7666
Cdd:cd05893      79 NPQGRISCTGRLMV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
11732-11800 9.72e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.02  E-value: 9.72e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11732 EEVTVVKGQPLYLSCEL--NKERDVVWRKDGKIVVEKPGRIVPGVIGLMRaLTINDADDTDAGTYTVTVEN 11800
Cdd:pfam13927     9 SSVTVREGETVTLTCEAtgSPPPTITWYKNGEPISSGSTRSRSLSGSNST-LTISNVTRSDAGTYTCVASN 78
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
29349-29538 9.82e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 51.87  E-value: 9.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29349 PFVPPSAPTRPEVYYV----SANAMSIRWEEPyhdGGSkiVGYWVEKKeRNTILWVKENKVPclECNYKVTGLVEGlEYQ 29424
Cdd:COG4733     530 QWPPVNVTTSESLSVVaqgtAVTTLTVSWDAP---AGA--VAYEVEWR-RDDGNWVSVPRTS--GTSFEVPGIYAG-DYE 600
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29425 FRTYALNAAGVSKASEASRPIMAQNPVDPPGRP---EVTDVTRStVSLVWSAPMYDGgskVVGYIIERKPVSEVGDGRWL 29501
Cdd:COG4733     601 VRVRAINALGVSSAWAASSETTVTGKTAPPPAPtglTATGGLGG-ITLSWSFPVDAD---TLRTEIRYSTTGDWASATVA 676
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958765569 29502 KCNYTIvsdNFFTVTALSEGDTYEFRVLAKNAAGIIS 29538
Cdd:COG4733     677 QALYPG---NTYTLAGLKAGQTYYYRARAVDRSGNVS 710
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
7590-7657 9.87e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 46.39  E-value: 9.87e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7590 LGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSfaDNVCTLTLSSLEPSDTGAYTCVAANVAGQ 7657
Cdd:cd05856      18 VGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENK--KKKWTLSLKNLKPEDSGKYTCHVSNRAGE 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12976-13046 9.93e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 46.64  E-value: 9.93e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12976 VFTKNLANLEVSEGDTIKLVCEVS-KPGAEVTWYKgDEEVIET----GRFEILTDGRKRILIIQNAQLEDAGSYNC 13046
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYK-NGVPIDPssipGKYKIESEYGVHVLHIRRVTVEDSAVYSA 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7676-7759 9.93e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 9.93e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   7676 PDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSREL----------ESGEACTISLEDfVTELelleveplQSGDYSCLVT 7745
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaesgrfsvsRSGSTSTLTISN-VTPE--------DSGTYTCAAT 71
                             90
                     ....*....|....
gi 1958765569   7746 NDAGSASCTTHLFV 7759
Cdd:smart00410    72 NSSGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12725-12782 9.97e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.78  E-value: 9.97e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12725 ATFDCELSYEDIP-VEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAK 12782
Cdd:cd00096       1 VTLTCSASGNPPPtITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
9589-9652 9.99e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 46.63  E-value: 9.99e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  9589 DVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKPQGRVKTEV-EHKVHKLTIADVRAEDQGRYTC 9652
Cdd:cd20990       9 DLTVQEGKLCRMDCKVSgLPTPDLSWQLDGKPIRPDSAHKMLVrENGVHSLIIEPVTSRDAGIYTC 74
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
15920-16006 1.01e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 46.30  E-value: 1.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15920 IKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKPTDALNITKEEVSRseakTELSIPKAVREDKGTYTITASNRLGSVF 15999
Cdd:cd05892      10 KKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGR----ICLLIQNANKKDAGWYTVSAVNEAGVVS 85

                    ....*..
gi 1958765569 16000 RNVHVEV 16006
Cdd:cd05892      86 CNARLDV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
29169-29249 1.01e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 1.01e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  29169 ITCKAGSTFTIDVPISGRPAPKVTWKLEEMR-LKETDRMSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITV 29247
Cdd:smart00410     4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                     ..
gi 1958765569  29248 VV 29249
Cdd:smart00410    84 TV 85
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
33091-33161 1.01e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 45.64  E-value: 1.01e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 33091 RFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKStfeISSVQASDEGNYSVVVENTDGKQEAQFTLT 33161
Cdd:cd05746       2 QIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEGYLA---IRDVGVADQGRYECVARNTIGYASVSMVLS 69
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
3600-3667 1.01e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 46.31  E-value: 1.01e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  3600 VHGEPAPTVLWFKEDMPLYTNVCYTIIHNPDGSGTFIVNDPQRGDSGLYICKAENLWGTSTCTAELLV 3667
Cdd:cd20975      24 VQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQCEARLEV 91
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
19818-19897 1.02e-04

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 46.39  E-value: 1.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19818 TVKAGTNVCLDATVFGKPMPTVSWKKDStpiKQTEGVKM--------AMKRNLCTLELFSVNRKDSGDYTITAENSSGSK 19889
Cdd:cd05765      11 TVKVGETASFHCDVTGRPQPEITWEKQV---PGKENLIMrpnhvrgnVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGLL 87

                    ....*...
gi 1958765569 19890 SATIKLKV 19897
Cdd:cd05765      88 RANFPLSV 95
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4588-4660 1.02e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 46.72  E-value: 1.02e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  4588 GESARLHCKL-KGSPVIQVTWFKNNKELSESNTVRMSFANSE-AILDITDVKVDDSGTYSCEATNDAGSDSCSTE 4660
Cdd:cd20959      17 GMRAQLHCGVpGGDLPLNIRWTLDGQPISDDLGITVSRLGRRsSILSIDSLEASHAGNYTCHARNSAGSASYTAP 91
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6632-6725 1.02e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 46.72  E-value: 1.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6632 RMVPPSFTRRLKDIGGVLGTSCVLEckvAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCT-LQLNSLDSSDMGSYTCVA 6710
Cdd:cd20959       3 RIIPFAFGEGAAQVGMRAQLHCGVP---GGDLPLNIRWTLDGQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCHA 79
                            90
                    ....*....|....*
gi 1958765569  6711 ANVAGSDECRALLTV 6725
Cdd:cd20959      80 RNSAGSASYTAPLTV 94
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6455-6536 1.02e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.04  E-value: 1.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6455 LTVVAGEPAELQASIEGAPPISVHWLKEkEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDGGVREnmASL 6534
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKD-GQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS--ATI 78

                    ..
gi 1958765569  6535 TV 6536
Cdd:cd05748      79 NV 80
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
33892-33984 1.02e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 46.31  E-value: 1.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITWScgGRRIQSQEQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGN 33971
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWL--RNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVN 78
                            90
                    ....*....|...
gi 1958765569 33972 EFGSDSATVNINI 33984
Cdd:cd20975      79 EYGARQCEARLEV 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
6360-6435 1.03e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 1.03e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6360 PVVETLKNTEV------SLECE-LSGTPPFEVVWYKDKRQL--RSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNE 6430
Cdd:cd05750       1 PKLKEMKSQTVqegsklVLKCEaTSENPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENI 80

                    ....*
gi 1958765569  6431 VGSDT 6435
Cdd:cd05750      81 LGKDT 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
6087-6162 1.03e-04

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 46.08  E-value: 1.03e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6087 GSSIHMECKVSGSlPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKvsnvAGDNACSGILTV 6162
Cdd:cd20967      12 GHKIRLTVELADP-DAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV----AGGEKCSFELFV 82
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7952-8041 1.03e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 46.58  E-value: 1.03e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQL--LKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNP 8029
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVisTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  8030 LGTASSSAKLIL 8041
Cdd:cd20974      81 SGQATSTAELLV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
28081-28152 1.03e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.23  E-value: 1.03e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 28081 PGAQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLkESEYVRFSKTENkiTLSIKNVKKENGGKYTVILDN 28152
Cdd:cd20978       7 PEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDG--TLTIINVQPEDTGYYGCVATN 75
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
5712-5787 1.04e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 46.63  E-value: 1.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5712 GQSTTFECQVTGTPEIRVSWYLDGNEITDLR-RYGISF-VDGLATFQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd05893      15 GMPVTFTCRVAGNPKPKIYWFKDGKQISPKSdHYTIQRdLDGTCSLHTTASTLDDDGNYTIMAANPQGRISCTGRLMV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
1258-1327 1.04e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.43  E-value: 1.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1258 ILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05737      13 IMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNKYG 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
17329-17407 1.04e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.02  E-value: 1.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 17329 PPTLDLDFRDkLTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVEN 17407
Cdd:pfam13927     1 KPVITVSPSS-VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5322-5411 1.04e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.23  E-value: 1.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5322 PSFIKKIET-TSSLRGGTAAFQATLKGSLPITVTWLKDNDEITeDDNIRMTFENNvaSLYLSGIEVKHDGKYVCQAKNDA 5400
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ-GPMERATVEDG--TLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  5401 GIQRCSALLSV 5411
Cdd:cd20978      78 GDIYTETLLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2422-2479 1.05e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.78  E-value: 1.05e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  2422 AVLECKVSVPDVTSVKWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYKLMV 2479
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVA 58
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
31461-31531 1.05e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 46.38  E-value: 1.05e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31461 CKVTGHPKPIVKWYRQGKEIIAD----GLKYRVQEFkggyhQLIIASVTDDDATVYQVRATNQGGSVSGTASLEV 31531
Cdd:cd05857      26 CPAAGNPTPTMRWLKNGKEFKQEhrigGYKVRNQHW-----SLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 95
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
13511-13596 1.05e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.58  E-value: 1.05e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13511 PPKIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTKT---VDTTAEQTSFRILEAKKEDKGRYKIVLQNKH 13587
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQrhqITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ....*....
gi 1958765569 13588 GKAEGFINL 13596
Cdd:cd05747      83 GKQEAQFTL 91
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
1038-1127 1.06e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 46.30  E-value: 1.06e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQK--LVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQtgecrLVISMTFADDAGEYTIVIR 1115
Cdd:cd04969       1 PDFELNPVKKKilAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGS-----LKIKNVTKSDEGKYTCFAV 75
                            90
                    ....*....|..
gi 1958765569  1116 NKHGETSASASL 1127
Cdd:cd04969      76 NFFGKANSTGSL 87
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6267-6338 1.07e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 46.37  E-value: 1.07e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  6267 ASKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDsvaVMQMNSLGTEDSGDFICEAQNPA 6338
Cdd:cd20957       9 PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDG 77
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
31457-31531 1.07e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 46.37  E-value: 1.07e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31457 ATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEfkggyHQLIIASVTDDDATVYQVRATNQGGSVSGTASLEV 31531
Cdd:cd20957      19 AVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSE-----DVLVIPSVKREDKGMYQCFVRNDGDSAQATAELKL 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4949-5036 1.07e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 46.37  E-value: 1.07e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSV-VGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEgtaSLEISRVDMNDAGNFTCRATNSV 5027
Cdd:cd20957       1 PLSATIDPPVQTVdFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDG 77

                    ....*....
gi 1958765569  5028 GSKDSRGAL 5036
Cdd:cd20957      78 DSAQATAEL 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
19818-19897 1.07e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 46.42  E-value: 1.07e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19818 TVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLKV 19897
Cdd:cd20972      12 EVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
6545-6621 1.08e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 1.08e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6545 KAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLL-TSSQKHKFSFYNkiSSLKILSVEKEDAGTYTFQVQNNVGKS 6621
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIiEFNTRYIVRENG--TTLTIRNIRRSDMGIYLCIASNGVPGS 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8433-8511 1.09e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 46.41  E-value: 1.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8433 VTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNK-VSGLKIISVAPGDSGVYSFEVQNPVGKDSCTVSIQV 8511
Cdd:cd20973       9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
9292-9380 1.09e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 46.46  E-value: 1.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGE 9371
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81

                    ....*....
gi 1958765569  9372 IESNVNLQV 9380
Cdd:cd05763      82 ISANATLTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
16840-17014 1.10e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 51.48  E-value: 1.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16840 VTRNSMTVNWEEPEydggsPVTGYWLEMKDTtSKRWKRVNRdpikamTLGVSYKVTGLIEGsDYQFRVYAINAAGV--GP 16917
Cdd:COG4733     549 TAVTTLTVSWDAPA-----GAVAYEVEWRRD-DGNWVSVPR------TSGTSFEVPGIYAG-DYEVRVRAINALGVssAW 615
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16918 ASLPSDPVTARdpvappGPPFPKVTDWTKSS----VDLEWSPPLkdgGSKITGYIVEYKEEGKEEWEKGKDKEVRGTKLV 16993
Cdd:COG4733     616 AASSETTVTGK------TAPPPAPTGLTATGglggITLSWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYT 686
                           170       180
                    ....*....|....*....|.
gi 1958765569 16994 VTGLKEGAFYKFRVRAVNIAG 17014
Cdd:COG4733     687 LAGLKAGQTYYYRARAVDRSG 707
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5229-5308 1.10e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.23  E-value: 1.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEF-KSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLrSGRKYKTFIQDQlvSLQILKFVASDAGEYQCRVTNEV 5307
Cdd:cd20978       1 PKFIQKPeKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDG--TLTIINVQPEDTGYYGCVATNEI 77

                    .
gi 1958765569  5308 G 5308
Cdd:cd20978      78 G 78
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1811-1879 1.10e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 46.24  E-value: 1.10e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  1811 RVLEGETARFRCRVTGYPQPKVNWYLNGQLIR-KSKRFRVR--YDGIHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd05893      11 KIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQrdLDGTCSLHTTASTLDDDGNYTIMAANPQG 82
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
7581-7666 1.10e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 46.23  E-value: 1.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7581 RKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQDES 7660
Cdd:cd20969       7 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSM 86

                    ....*.
gi 1958765569  7661 SALLTV 7666
Cdd:cd20969      87 PAHLHV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7482-7563 1.10e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 46.17  E-value: 1.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7482 RIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGK 7561
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                    ..
gi 1958765569  7562 SS 7563
Cdd:cd20949      81 AS 82
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
28085-28163 1.10e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 46.37  E-value: 1.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28085 ISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESE-YVRFSKTENKITLSIKNVKKENGGKYTVILDNAVCRNSFPITI 28163
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
7119-7198 1.11e-04

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409398  Cd Length: 101  Bit Score: 46.71  E-value: 1.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7119 IAGESADFECHVTGAQPMRVTWSKDNKEIRPGGN--YTITC------VGNTphLRILKVGKGDSGQYTCQATNDVGKDMC 7190
Cdd:cd05735      16 TKGQKKEMSCTAHGEKPIIVRWEKEDTIINPSEMsrYLVTTkevgdeVIST--LQILPTVREDSGFFSCHAINSYGEDRG 93

                    ....*...
gi 1958765569  7191 SAQLSVKE 7198
Cdd:cd05735      94 IIQLTVQE 101
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
16-91 1.11e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 45.85  E-value: 1.11e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569    16 VVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTlpgvqisfsdgraRLMIPAVTKANSGRYSLRATNGSGQATS 91
Cdd:pfam13895    10 VVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSP-------------NFFTLSVSAEDSGTYTCVARNGRGGKVS 72
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
31455-31531 1.11e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 46.29  E-value: 1.11e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31455 SNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEFKGgyhQLIIASVTDDDATVYQVRATNQGGSVSGTASLEV 31531
Cdd:cd04978      15 ETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGR---TLIFSNLQPNDTAVYQCNASNVHGYLLANAFLHV 88
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
6087-6162 1.12e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 1.12e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6087 GSSIHMECKVSGSLP-INAQWFKDGKEI--STSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAGDNACSGILTV 6162
Cdd:cd05750      14 GSKLVLKCEATSENPsPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
27382-27474 1.12e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 1.12e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27382 PVIDLPLEYTEVVKyRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNA--LVCVENSTDLAsilIKDANRLNSGSYELKL 27459
Cdd:cd20970       1 PVISTPQPSFTVTA-REGENATFMCRAEGSPEPEISWTRNGNLIIEFNtrYIVRENGTTLT---IRNIRRSDMGIYLCIA 76
                            90
                    ....*....|....*.
gi 1958765569 27460 RN-AMGSASATIRVQI 27474
Cdd:cd20970      77 SNgVPGSVEKRITLQV 92
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
1050-1127 1.12e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 46.02  E-value: 1.12e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  1050 VEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNkqtGEcrLVIS-MTFADDAGEYTIVIRNKHGEtSASASL 1127
Cdd:cd20958      13 VAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPN---GT--LVIEnVQRSSDEGEYTCTARNQQGQ-SASRSV 85
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
6650-6725 1.13e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 46.17  E-value: 1.13e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6650 GTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTV 6725
Cdd:cd20949      14 GQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQERTV 89
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
33437-33505 1.13e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 45.99  E-value: 1.13e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33437 IKVTGEPQPTVTWTKDGKAIAQSS-KYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd05894      17 VPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
6352-6435 1.13e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 46.39  E-value: 1.13e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6352 PPVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASknfhASIHILNVDSTDIGEYHCKAQNEV 6431
Cdd:cd04968       1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPSSQWEITTSE----PVLEIPNVQFEDEGTYECEAENSR 76

                    ....
gi 1958765569  6432 GSDT 6435
Cdd:cd04968      77 GKDT 80
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
25629-25708 1.14e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 46.46  E-value: 1.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25629 VTLRASATLRLFVTIKGRPEPEVKWEKAEGI----LTERaQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVN 25704
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGGTdfpaARER-RMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANAT 87

                    ....
gi 1958765569 25705 VRVL 25708
Cdd:cd05763      88 LTVL 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5041-5131 1.15e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.49  E-value: 1.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5041 PPSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVA 5120
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|.
gi 1958765569  5121 GSVECSANLFV 5131
Cdd:cd05762      81 GSRQAQVNLTV 91
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
21592-21658 1.15e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.19  E-value: 1.15e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 21592 GDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGE 21658
Cdd:cd05747      18 GESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
9308-9380 1.15e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.04  E-value: 1.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9308 TFIAKVG----------GDPIPNVKWTKGKwRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGEIESNVN 9377
Cdd:cd05748       1 TIVVRAGeslrldipikGRPTPTVTWSKDG-QPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    ...
gi 1958765569  9378 LQV 9380
Cdd:cd05748      80 VKV 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4962-5030 1.15e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.04  E-value: 1.15e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4962 VGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSK 5030
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEK 74
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
31457-31531 1.16e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 46.24  E-value: 1.16e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31457 ATLVCKV-TGHPKPIVKWYRQGKEIIADGLkyRVQEFKGGyhQLIIASVTDDDATVYQVRATNQGGS-VSGTASLEV 31531
Cdd:cd05724      15 AVLECSPpRGHPEPTVSWRKDGQPLNLDNE--RVRIVDDG--NLLIAEARKSDEGTYKCVATNMVGErESRAARLSV 87
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5891-5963 1.16e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 46.33  E-value: 1.16e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5891 ENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVAT-LQVRSVDNGHSGRYTCQAKNESG 5963
Cdd:cd20959      11 EGAAQVGMRAQLHCGVPGGDLPLNIRWTLDGQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCHARNSAG 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12547-12601 1.17e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.78  E-value: 1.17e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12547 VVLQCEISKADAP-VKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTC 12601
Cdd:cd00096       1 VTLTCSASGNPPPtITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTC 56
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
6650-6725 1.17e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 46.23  E-value: 1.17e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6650 GTSCVLECKVAGSSPISIAWFHEKTKIVSGAK--YQTTFSDNvcTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTV 6725
Cdd:cd20969      17 GHTVQFVCRADGDPPPAILWLSPRKHLVSAKSngRLTVFPDG--TLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
28477-28558 1.17e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 46.33  E-value: 1.17e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28477 FDGLVIKSGDSLRIKALVQGRPVPRVTWFKDG--VEIERRMNMeITDVLGSTSLFVRDATRDHRGVYTVEAKNVSG--ST 28552
Cdd:cd05744       7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGkpVRPDSAHKM-LVRENGRHSLIIEPVTKRDAGIYTCIARNRAGenSF 85

                    ....*.
gi 1958765569 28553 KAEITV 28558
Cdd:cd05744      86 NAELVV 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
7295-7376 1.17e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.95  E-value: 1.17e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7295 VFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNfdTSLHIFNLEAPDIGEYHCKATNEVGS 7374
Cdd:cd20952       1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLEN--GSLQIKGAEKSDTGEYTCVALNLSGE 78

                    ..
gi 1958765569  7375 DT 7376
Cdd:cd20952      79 AT 80
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
8430-8511 1.18e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 45.86  E-value: 1.18e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8430 SIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDsKYKISFFNKVsgLKIISVAPGDSGVYSFEVQNPVGKDSCTVSI 8509
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKG-RTKFENFNKT--LKIENVSEADSGEYQCTASNTMGSARHTISV 80

                    ..
gi 1958765569  8510 QV 8511
Cdd:cd05731      81 TV 82
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
15-91 1.18e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.43  E-value: 1.18e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569    15 VVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTlpGVQISFSDGR-ARLMIPAVTKANSGRYSLRATNGSGQATS 91
Cdd:cd05737      11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLD--HCNLKVEAGRtVYFTINGVSSEDSGKYGLVVKNKYGSETS 86
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5703-5778 1.18e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 46.24  E-value: 1.18e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5703 PSPVLVLRnGQSTTFECQV-TGTPEIRVSWYLDGNEItDLRRYGISFVDGlATFQISNARVENSGTYVCEARNDAGT 5778
Cdd:cd05724       4 PSDTQVAV-GEMAVLECSPpRGHPEPTVSWRKDGQPL-NLDNERVRIVDD-GNLLIAEARKSDEGTYKCVATNMVGE 77
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
4391-4466 1.20e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 46.03  E-value: 1.20e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4391 SRPKSLTTFVGKAAKFLCTVS-GTPVIETIWQKDGTALSPSPDCRITDADN-KHSLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNNPGG 78
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
1518-1597 1.21e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.05  E-value: 1.21e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1518 FVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIvpHKYPRIRIEGTKgeaaLKIDSTISQDSAWYTATAINKAG 1597
Cdd:cd05728       2 WLKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPL--ASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHG 75
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
13511-13585 1.22e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.63  E-value: 1.22e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 13511 PPKIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPL---STKTVDTTAEQTSFRILEAKKEDKGRYKIVLQN 13585
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPIssgSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5143-5221 1.22e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 45.99  E-value: 1.22e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5143 PSQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVEstaVLRLTDVAIEDSGEYMCEAQNEAGSDHCTS 5221
Cdd:cd20957       9 PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQATA 84
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
9293-9380 1.23e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 1.23e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9293 VSEPQS---IRVVEKTTATFIAKVGGDPIPNVKWTKGKWR--QLNQGGRIlihqKGDESKLEIRDTTKTDSGLYRCVAFN 9367
Cdd:cd20970       3 ISTPQPsftVTAREGENATFMCRAEGSPEPEISWTRNGNLiiEFNTRYIV----RENGTTLTIRNIRRSDMGIYLCIASN 78
                            90
                    ....*....|....
gi 1958765569  9368 K-HGEIESNVNLQV 9380
Cdd:cd20970      79 GvPGSVEKRITLQV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8235-8314 1.23e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.23  E-value: 1.23e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGA-DVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTsihILNVDTADIGEYQCKATNDV 8313
Cdd:cd20978       1 PKFIQKPEKNVVVKGGqDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGTLT---IINVQPEDTGYYGCVATNEI 77

                    .
gi 1958765569  8314 G 8314
Cdd:cd20978      78 G 78
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
9583-9665 1.24e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.05  E-value: 1.24e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9583 WERHLQDVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKPQGRVktEVEHKvhKLTIADVRAEDQGRYTC----KHEDL 9657
Cdd:cd05728       2 WLKVISDTEADIGSSLRWECKASgNPRPAYRWLKNGQPLASENRI--EVEAG--DLRITKLSLSDSGMYQCvaenKHGTI 77

                    ....*...
gi 1958765569  9658 ETSAELRI 9665
Cdd:cd05728      78 YASAELAV 85
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
8265-8317 1.24e-04

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 46.18  E-value: 1.24e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8265 QVSWYKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDT 8317
Cdd:cd20927      31 QVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDS 83
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
7214-7280 1.24e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 46.06  E-value: 1.24e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7214 QGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNS-VALLTINEASVEDTGDYICEAHNGVG 7280
Cdd:cd05891      15 EGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGkYASLTIKGVTSEDSGKYSINVKNKYG 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5414-5504 1.24e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.23  E-value: 1.24e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5414 PATITEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTlGPKYKISVTDtvSILKIISTEKKDSGEYTFEVQNDV 5493
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ-GPMERATVED--GTLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  5494 GRSSCKASINV 5504
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
4759-4842 1.25e-04

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 46.17  E-value: 1.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4759 PPTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFssgvAVLTISDVQIGLGGKYTCLAENEA 4838
Cdd:cd05851       1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSG----AVLKIFNIQPEDEGTYECEAENIK 76

                    ....
gi 1958765569  4839 GSQT 4842
Cdd:cd05851      77 GKDK 80
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
17742-17816 1.25e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 46.03  E-value: 1.25e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 17742 IKVGDTLRLSAIIK-GVPFPKVTWKKEDREAPTKAQIDVTPVG---SKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKV 17816
Cdd:pfam00047     8 VLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRttqSSLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
33416-33499 1.25e-04

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 46.39  E-value: 1.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33416 PVIVTGLRDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAI-----AQSSKYKLSNDKEEFILEIL--KTETSDGGLYSC 33488
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLetdkdDPRSHRIVLPSGSLFFLRVVhgRKGRSDEGVYVC 80
                            90
                    ....*....|.
gi 1958765569 33489 TVANSAGSVSS 33499
Cdd:cd07693      81 VAHNSLGEAVS 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5518-5591 1.25e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.85  E-value: 1.25e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5518 RKMDSIKGSFIDLECIVAGSHPI-SIQWFKDDQEISASDKYKFSFHDNTafLEISQLEGTDSGTYTCSATNKAGH 5591
Cdd:cd05724       5 SDTQVAVGEMAVLECSPPRGHPEpTVSWRKDGQPLNLDNERVRIVDDGN--LLIAEARKSDEGTYKCVATNMVGE 77
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
18728-18803 1.25e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.85  E-value: 1.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18728 GDTIRLEAGV-RGKPFPEVAWTKDKDATDLTrSPRVKIdtsAESSKFSLTKAKRSDGGKYVVTATNPAG---SFVAYATV 18803
Cdd:cd05724      12 GEMAVLECSPpRGHPEPTVSWRKDGQPLNLD-NERVRI---VDDGNLLIAEARKSDEGTYKCVATNMVGereSRAARLSV 87
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
7293-7375 1.25e-04

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 46.15  E-value: 1.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVK-------DRKQVRSSKKFKVTSKNfdtSLHIFNLEAPDIGEYH 7365
Cdd:cd20954       1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYDPNVRILPNG---TLVFGHVQKENEGHYL 77
                            90
                    ....*....|
gi 1958765569  7366 CKATNEVGSD 7375
Cdd:cd20954      78 CEAKNGIGSG 87
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
4968-5040 1.26e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 46.10  E-value: 1.26e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  4968 LDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSRGALIVQE 5040
Cdd:cd05736      20 LRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7307-7374 1.26e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 45.70  E-value: 1.26e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7307 KGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNfdtSLHIFNLEAPDIGEYHCKATNEVGS 7374
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSG---TLRISRVALHDQGQYECQAVNIVGS 65
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7771-7839 1.27e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.63  E-value: 1.27e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7771 DTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIEN 7839
Cdd:pfam13927    10 SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
4483-4569 1.27e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 1.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4483 IKELEPVQSAINKKIHLECQ-VDEDRKVSITWSKDGQKLPAGKDYKIYFED--KIASLEIPLAKLKDSGTYSCTASNEAG 4559
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNkkKNSELQINKAKLEDSGEYTCVVENILG 82
                            90
                    ....*....|
gi 1958765569  4560 SSSSSATVAV 4569
Cdd:cd05750      83 KDTVTGNVTV 92
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
7208-7291 1.27e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 45.86  E-value: 1.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7208 TSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHeswKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVGHASCSTA 7287
Cdd:cd05731       3 SSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGELP---KGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTIS 79

                    ....
gi 1958765569  7288 LKVK 7291
Cdd:cd05731      80 VTVE 83
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5041-5131 1.28e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 46.40  E-value: 1.28e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5041 PPSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSC----YITKEAS-ESSLELYAVKTTDSGTYTCK 5115
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFrvgdYVTSDGDvVSYVNISSVRVEDGGEYTCT 80
                            90
                    ....*....|....*.
gi 1958765569  5116 VSNVAGSVECSANLFV 5131
Cdd:cd20956      81 ATNDVGSVSHSARINV 96
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
4306-4381 1.29e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 1.29e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4306 GHLAKFTCEIQGAPNVRFQWFKAGREIYESDK-CSIRSSNyiSSLEILRTQVVDCGEYTCKASNE-YGSVSCTATLTV 4381
Cdd:cd20970      17 GENATFMCRAEGSPEPEISWTRNGNLIIEFNTrYIVRENG--TTLTIRNIRRSDMGIYLCIASNGvPGSVEKRITLQV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
5147-5217 1.29e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.04  E-value: 1.29e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  5147 LKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVE-STAVLRLTDVAIEDSGEYMCEAQNEAGSD 5217
Cdd:cd05737      13 IMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGSE 84
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
18424-18511 1.29e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 46.07  E-value: 1.29e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18424 VTCRDvITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRV-ELQIKEAVRADHGKYIISAKNSSGHA 18502
Cdd:cd05763       4 KTPHD-ITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARERRMHVMPEDdVFFIVDVKIEDTGVYSCTAQNSAGSI 82

                    ....*....
gi 1958765569 18503 QGSAIVNVL 18511
Cdd:cd05763      83 SANATLTVL 91
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
6539-6620 1.29e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 46.00  E-value: 1.29e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6539 PAVIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYK-DGKLLTSSQKHKFSfynkiSSLKILSVEKEDAGTYTFQVQNN 6617
Cdd:cd04968       1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKvDGSPSSQWEITTSE-----PVLEIPNVQFEDEGTYECEAENS 75

                    ...
gi 1958765569  6618 VGK 6620
Cdd:cd04968      76 RGK 78
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
19816-19897 1.30e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 46.06  E-value: 1.30e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19816 LLTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKR-NLCTLELFSVNRKDSGDYTITAENSSGSKSATIK 19894
Cdd:cd05891      10 VVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVT 89

                    ...
gi 1958765569 19895 LKV 19897
Cdd:cd05891      90 VSV 92
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8629-8700 1.30e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 46.33  E-value: 1.30e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8629 TFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFD-VDTSQSGDYTCIVSNEAGRASCTTQLFV 8700
Cdd:cd20959      22 LHCGVPGGDLPLNIRWTLDGQPISDDLGITVSRLGRRSSILSIDsLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
907-989 1.31e-04

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 46.49  E-value: 1.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   907 KNVTVVEGESVTLECHISGYPSPKVTWYREDYQI--------ESSIDFQITfQSGiaRLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd05726       7 RDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNllfpyqppQPSSRFSVS-PTG--DLTITNVQRSDVGYYICQALNVA 83
                            90
                    ....*....|.
gi 1958765569   979 GTVSTSCYLAV 989
Cdd:cd05726      84 GSILAKAQLEV 94
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
10807-11021 1.31e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 51.39  E-value: 1.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10807 APPAKVPEIPKKPEEKVSVPvPKKEKAPPAKVPEVPKKPVPEEKAPVPVPKKVEPPPAKVPEVPkkPVPEKKVPAPTPKK 10886
Cdd:PRK07003    400 TAVTGAAGAALAPKAAAAAA-ATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSR--CDERDAQPPADSGS 476
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10887 VEAPPAKAPEVPPKEVTPEKKVPVVPPKKPEAPPPKVPEPPKEVVPEKKVSMVPPKRPEAPPAKVP-------EASKEVV 10959
Cdd:PRK07003    477 ASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPaaraggaAAALDVL 556
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 10960 PEK--KVSVAPKKKPEA---PAVKVPEAPKKVVPEKKVPVAAPKKPE----------APAAEVPEVPKAAVPQKKIP 11021
Cdd:PRK07003    557 RNAgmRVSSDRGARAAAaakPAAAPAAAPKPAAPRVAVQVPTPRARAatgdappngaARAEQAAESRGAPPPWEDIP 633
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7484-7570 1.32e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 45.85  E-value: 1.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7484 VEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGsRHHItfvRNLASLKIPSAEMNDKGLYSFEVENSVGKSS 7563
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEI---LDDHSLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  7564 CTVSVHV 7570
Cdd:cd05725      77 ASATLTV 83
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
5229-5316 1.33e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 46.30  E-value: 1.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQL--VSLQILKFVASDAGEYQCRVTNE 5306
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCgrICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|
gi 1958765569  5307 VGSSTCSARV 5316
Cdd:cd05892      81 AGVVSCNARL 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
20887-20976 1.33e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.19  E-value: 1.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20887 APTIVLDPTikdGLTVKAGDSIVLSAiSILGKPLPKSSWSKAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITA 20966
Cdd:cd05747       3 PATILTKPR---SLTVSEGESARFSC-DVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVV 78
                            90
                    ....*....|
gi 1958765569 20967 TNPFGTKEEH 20976
Cdd:cd05747      79 ENSEGKQEAQ 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8532-8607 1.34e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 45.85  E-value: 1.34e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8532 GSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTcaltvnmledaDAGDYTCIATNVAGSdECSAPLTV 8607
Cdd:pfam13895    14 GEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTLSVSAE-----------DSGTYTCVARNGRGG-KVSNPVEL 77
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
27806-27874 1.34e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.85  E-value: 1.34e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27806 PFKGRPPPTVTWRKDEKNLG-SDARYSIQNTDSsslLVIPQVTRNDTGKYILTIENGVGQPKSSTVSVKV 27874
Cdd:cd05724      21 PPRGHPEPTVSWRKDGQPLNlDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGERESRAARLSV 87
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
6353-6444 1.35e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 46.10  E-value: 1.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6353 PVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQL--RSSKKYKIASKNfhASIHILNVDSTDIGEYHCKAQNE 6430
Cdd:cd05736       1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDInpKLSKQLTLIANG--SELHISNVRYEDTGAYTCIAKNE 78
                            90
                    ....*....|....
gi 1958765569  6431 VGSDTCICAIKLKE 6444
Cdd:cd05736      79 GGVDEDISSLFVED 92
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
31461-31531 1.35e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.05  E-value: 1.35e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31461 CKVTGHPKPIVKWYRQGKEIIADGlkyRVQEFKGgyhQLIIASVTDDDATVYQVRATNQGGSVSGTASLEV 31531
Cdd:cd05728      21 CKASGNPRPAYRWLKNGQPLASEN---RIEVEAG---DLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
31049-31132 1.35e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.05  E-value: 1.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31049 KEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKEL-VQSRKYKMSSDGRTHTLTVmteeqEDEGVYTCVATNEVGEVE 31127
Cdd:cd05728       4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLaSENRIEVEAGDLRITKLSL-----SDSGMYQCVAENKHGTIY 78

                    ....*
gi 1958765569 31128 TSSKL 31132
Cdd:cd05728      79 ASAEL 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12903-12960 1.35e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.40  E-value: 1.35e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12903 ARFECEIS-KENVKVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEVR 12960
Cdd:cd00096       1 VTLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
9189-9266 1.36e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 46.03  E-value: 1.36e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9189 TPVTASEGDFLQLSCHV-QGSEPIRIQWLRAGREIKPSDRCSFSFAS-GTAVLELKDTAKADSGDYVCKASNVAGSDTSK 9266
Cdd:pfam00047     4 PTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRtTQSSLLISNVTKEDAGTYTCVVNNPGGSATLS 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
17060-17121 1.36e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.40  E-value: 1.36e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 17060 VSGKPPPTVTWNMNERALPQEA--TIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTII 17121
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLPPSSrdSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
18712-18805 1.37e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 46.03  E-value: 1.37e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18712 KPVLDLklsgvlTVKAGDTIRLEAGVRGKPFPEVAWTKDKDAtdLTRSPRVKIDTSAESS-KFSLTKAKRSDGGKYVVTA 18790
Cdd:cd20973       2 QTLRDK------EVVEGSAARFDCKVEGYPDPEVKWMKDDNP--IVESRRFQIDQDEDGLcSLIISDVCGDDSGKYTCKA 73
                            90
                    ....*....|....*
gi 1958765569 18791 TNPAGSFVAYATVNV 18805
Cdd:cd20973      74 VNSLGEATCSAELTV 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
18027-18112 1.37e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 46.03  E-value: 1.37e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18027 KLIEGLVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDS-FSSVLTIKNCLRKDTGEYQLTVSNAAGTKT 18105
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEdGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569 18106 VAVHLTV 18112
Cdd:cd20973      82 CSAELTV 88
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
32326-32396 1.40e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 46.07  E-value: 1.40e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 32326 EIRVSGIPAPTLKWEKDGQ---PLSLGPHIEIVHEGLDYYalhIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:cd05763      20 ECAATGHPTPQIAWQKDGGtdfPAARERRMHVMPEDDVFF---IVDVKIEDTGVYSCTAQNSAGSISANATLTV 90
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
8810-8886 1.40e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 46.08  E-value: 1.40e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8810 VGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTcKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGEVSSSTFLTV 8886
Cdd:cd05730      17 LGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
25229-25297 1.41e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.63  E-value: 1.41e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 25229 IIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKSTLQkTTLTVKDCIRTDGGQYTLKLSN 25297
Cdd:pfam13927    11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSN-STLTISNVTRSDAGTYTCVASN 78
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
32314-32396 1.42e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.96  E-value: 1.42e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32314 NAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEglDYYALHIRDTLPEDTGYYRVTATNTA-GSTSCQA 32392
Cdd:cd20970      11 TVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRE--NGTTLTIRNIRRSDMGIYLCIASNGVpGSVEKRI 88

                    ....
gi 1958765569 32393 HLQV 32396
Cdd:cd20970      89 TLQV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
17046-17125 1.42e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 46.19  E-value: 1.42e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17046 IVVHAGGVIRIIAYVSGKPPPTVTWNMNERA-----LPQeATIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTI 17120
Cdd:cd20974      10 VVVLEGSTATFEAHVSGKPVPEVSWFRDGQViststLPG-VQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTA 88

                    ....*
gi 1958765569 17121 IVDVL 17125
Cdd:cd20974      89 ELLVL 93
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
23732-23829 1.44e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 45.99  E-value: 1.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23732 PITAKdlvIEPDVRpafssySVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSldlTTLSIKETHKDDGGH 23811
Cdd:cd20957       1 PLSAT---IDPPVQ------TVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSE---DVLVIPSVKREDKGM 68
                            90
                    ....*....|....*...
gi 1958765569 23812 YGITVANVVGQKTAAIEI 23829
Cdd:cd20957      69 YQCFVRNDGDSAQATAEL 86
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
32201-32293 1.45e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 45.92  E-value: 1.45e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPgDDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQY-NTDRISLYQDNCGRICLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:cd05892      80 EAGVVSCNARLDV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13159-13241 1.45e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.96  E-value: 1.45e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13159 KDTKVKEQQEAVFNCEVN-TEGAKAKWFRND-EAIFDSSKYIILQKDLVYTLRIRDARLDDQANFSVSLTNHRGeNVKSA 13236
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SASSG 80

                     ....*
gi 1958765569  13237 ANLIV 13241
Cdd:smart00410    81 TTLTV 85
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
5136-5216 1.46e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 46.00  E-value: 1.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5136 TFTEKLEPS-QLLKKGDATQLVCKVTGTPPIKITWFANDRELREssKHKM---SFVESTAVLRLTDVAIEDSGEYMCEAQ 5211
Cdd:cd05857       4 TNPEKMEKKlHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQ--EHRIggyKVRNQHWSLIMESVVPSDKGNYTCVVE 81

                    ....*
gi 1958765569  5212 NEAGS 5216
Cdd:cd05857      82 NEYGS 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
29569-29636 1.47e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.63  E-value: 1.47e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 29569 VTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKN 29636
Cdd:pfam13927    11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
33893-33984 1.48e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 46.19  E-value: 1.48e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33893 KIEALPS--DISIAEGKVLTvaCAFTGEPT-PEITW-SCGGRRIQSQEQQGRFhIENTDDLTTLIIMDVQKQDGGLYTLS 33968
Cdd:cd05865       2 QVDIVPSqgEISVGESKFFL--CQVAGEAKdKDISWfSPNGEKLTPNQQRISV-VRNDDYSSTLTIYNANIDDAGIYKCV 78
                            90
                    ....*....|....*..
gi 1958765569 33969 LGNEFGSDS-ATVNINI 33984
Cdd:cd05865      79 VSNEDEGESeATVNVKI 95
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
8796-8886 1.49e-04

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 46.15  E-value: 1.49e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8796 PPYFVkqLEPLKVTV--GDSASLQCQLAGTPEIGVSWYKG---------DTKLRPTTtckmHFKNNvATLVFTQVDSNDS 8864
Cdd:cd20954       1 PPRWI--VEPVDANVaaGQDVMLHCQADGFPTPTVTWKKAtgstpgeykDLLYDPNV----RILPN-GTLVFGHVQKENE 73
                            90       100
                    ....*....|....*....|...
gi 1958765569  8865 GEYICRAENSVGE-VSSSTFLTV 8886
Cdd:cd20954      74 GHYLCEAKNGIGSgLSKVIFLKV 96
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
9292-9380 1.51e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.78  E-value: 1.51e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVAFNKHGE 9371
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNG-QPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                    ....*....
gi 1958765569  9372 IESNVNLQV 9380
Cdd:cd20949      81 ASDMQERTV 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2582-2650 1.51e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.63  E-value: 1.51e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2582 ISKPLTDQTVAESQEAVFECEV-ANPESEGEWLKDGKHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYT 2650
Cdd:pfam13927     4 ITVSPSSVTVREGETVTLTCEAtGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYT 73
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
4291-4381 1.52e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 45.46  E-value: 1.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4291 APVIkrRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIyesdkcsirSSNYISSleILRTQVVDCGEYTCKASNEY 4370
Cdd:pfam13895     1 KPVL--TPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAI---------SSSPNFF--TLSVSAEDSGTYTCVARNGR 67
                            90
                    ....*....|..
gi 1958765569  4371 GS-VSCTATLTV 4381
Cdd:pfam13895    68 GGkVSNPVELTV 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7951-8039 1.53e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 46.09  E-value: 1.53e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7951 PPSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNlQMSFVHHVATLQILQTDQSHVGQYNCSASNPL 8030
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79

                    ....*....
gi 1958765569  8031 GTASSSAKL 8039
Cdd:cd20976      80 GQVSCSAWV 88
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
6274-6351 1.53e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 46.10  E-value: 1.53e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6274 GDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTKVIVKE 6351
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7023-7094 1.55e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 45.46  E-value: 1.55e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  7023 TVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENlqmSFVDNVAtlkilqtdLSHSGQYSCSASNPLGTASS 7094
Cdd:pfam13895    12 TEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN---FFTLSVS--------AEDSGTYTCVARNGRGGKVS 72
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4854-4942 1.56e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.87  E-value: 1.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4854 KIIERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPL---VASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNE 4930
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNI 81
                            90
                    ....*....|..
gi 1958765569  4931 VGSSSCETTFTV 4942
Cdd:cd20951      82 HGEASSSASVVV 93
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
14213-14290 1.56e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.95  E-value: 1.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14213 TVKAGTKIELPATVTGKPEPKITWTK-ADTLLRPDQRITIENvpkKSTVTITDSKRSDTGTYIIEAVNVCGRAT--AVVE 14289
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKdGVPLLGKDERITTLE---NGSLQIKGAEKSDTGEYTCVALNLSGEATwsAVLD 86

                    .
gi 1958765569 14290 V 14290
Cdd:cd20952      87 V 87
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
9183-9271 1.56e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 45.84  E-value: 1.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9183 VFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREI---KPSDRCSFsFASGTavLELKDTAKADSGDYVCKASNV 9259
Cdd:cd20969       4 IRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLvsaKSNGRLTV-FPDGT--LEVRYAQVQDNGTYLCIAANA 80
                            90
                    ....*....|..
gi 1958765569  9260 AGSDTSKCKVTI 9271
Cdd:cd20969      81 GGNDSMPAHLHV 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
14921-14979 1.57e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 46.00  E-value: 1.57e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 14921 PFRAVPVPTVSWHKDGKEVKASDRL---TMKNDHISAHLEvpKSVHADAGVYTITLENKLGS 14979
Cdd:cd05857      27 PAAGNPTPTMRWLKNGKEFKQEHRIggyKVRNQHWSLIME--SVVPSDKGNYTCVVENEYGS 86
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9585-9652 1.57e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 45.64  E-value: 1.57e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  9585 RHLQDVTLKEGQTCTMTCQFSVPNVKS-EWFRNGRVLkPQGRvktevEHKVH---KLTIADV-RAEDQGRYTC 9652
Cdd:cd20958       5 RPMGNLTAVAGQTLRLHCPVAGYPISSiTWEKDGRRL-PLNH-----RQRVFpngTLVIENVqRSSDEGEYTC 71
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
18531-18823 1.57e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 51.10  E-value: 1.57e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18531 TISWENPLDNggseiTNFIVEYRKPNQKgWSIVASdVTKRLIKANLLANNEYYFRVCAENKVGVGPTIETKTPILAINPI 18610
Cdd:COG4733     555 TVSWDAPAGA-----VAYEVEWRRDDGN-WVSVPR-TSGTSFEVPGIYAGDYEVRVRAINALGVSSAWAASSETTVTGKT 627
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18611 DRPGEPENLHiADKGKTFVYLKWRRPDYDGgspnlSYHVERRLKGSADWE--RVHKGSIKETHYMVDKCVENQIYEFRVQ 18688
Cdd:COG4733     628 APPPAPTGLT-ATGGLGGITLSWSFPVDAD-----TLRTEIRYSTTGDWAsaTVAQALYPGNTYTLAGLKAGQTYYYRAR 701
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18689 TKNEGG-ESDW-VRTEEVVVKEDLQKPVLDLKLSGVLTVKAGDTIRLE--AGVRGKPFPEVAWTKDKDATDLTRSPRVKI 18764
Cdd:COG4733     702 AVDRSGnVSAWwVSGQASADAAGILDAITGQILETELGQELDAIIQNAtvAEVVAATVTDVTAQIDTAVLFAGVATAAAI 781
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 18765 DTSAESSKFSLTK---------AKRSDGGKYVVTATNPAGSFVAYATVNVLDKPGPVRNLKIADVSSD 18823
Cdd:COG4733     782 GAEARVAATVAESataaaatgtAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVYGD 849
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
33231-33308 1.58e-04

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 45.70  E-value: 1.58e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 33231 KITQSLKAEASRDIaKLTCAVessALCAKEVAWYKDGKKLKENGHFQFHySADGTYELKIHNLSESDCGEYVCEVSGE 33308
Cdd:cd20967       2 KAQPAVQVSKGHKI-RLTVEL---ADPDAEVKWYKDGQELQSSSKVIFE-SIGAKRTLTVQQASLADAGEYQCVAGGE 74
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
6538-6629 1.58e-04

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 46.39  E-value: 1.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6538 EPAVIVEKAGSMTVTVGETCSLECKVAGTP--ELSVEWYKDGKL--LTSSQKHKFSFYNK--ISSLKILSVEKEDAGTYT 6611
Cdd:cd04970       1 DATRITLAPSNADITVGENATLQCHASHDPtlDLTFTWSFNGVPidLEKIEGHYRRRYGKdsNGDLEIVNAQLKHAGRYT 80
                            90
                    ....*....|....*...
gi 1958765569  6612 FQVQNNVGKSSCTAVVDV 6629
Cdd:cd04970      81 CTAQTVVDSDSASATLVV 98
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
899-980 1.58e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 45.70  E-value: 1.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTlvsglkNVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQItFQSGiaRLMIREAFAEDSGRFTCSAVNEA 978
Cdd:cd20968       5 PPT------NVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAV-LESG--SLRIHNVQKEDAGQYRCVAKNSL 75

                    ..
gi 1958765569   979 GT 980
Cdd:cd20968      76 GI 77
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
19818-19897 1.58e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.96  E-value: 1.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19818 TVKAGTNVCLDATVFGKPMPTVSWKKDSTPIkQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAEN-SSGSKSATIKLK 19896
Cdd:cd20970      13 TAREGENATFMCRAEGSPEPEISWTRNGNLI-IEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNgVPGSVEKRITLQ 91

                    .
gi 1958765569 19897 V 19897
Cdd:cd20970      92 V 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
32215-32293 1.58e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 46.06  E-value: 1.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32215 GENVRFGVTITVHPEPRVTWYKSGQKIKPGDddkKYTFESDKGLY-QLTINSVTTDDDAEYAVVARNKHGEDSCKAKLTV 32293
Cdd:cd05891      16 GKTLNLTCTVFGNPDPEVIWFKNDQDIELSE---HYSVKLEQGKYaSLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
24833-24906 1.59e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.95  E-value: 1.59e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 24833 YSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLR-QTTRVNVEETATstiLHIKESSKDDFGKYSVTATNNAGTAT 24906
Cdd:cd20952       9 QTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLgKDERITTLENGS---LQIKGAEKSDTGEYTCVALNLSGEAT 80
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4386-4480 1.60e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.10  E-value: 1.60e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4386 PPTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKF 4465
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*
gi 1958765569  4466 GADICQAELTIIDKP 4480
Cdd:cd05762      81 GSRQAQVNLTVVDKP 95
PHA03247 PHA03247
large tegument protein UL36; Provisional
10807-11180 1.61e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.61e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10807 APPAKVPEIPKKPEEKVSVPVPKKEKAPPAKVPEVPKKPVPEEKAPVPVPKKVEPPPAKV--------PEVPKKPVPEKK 10878
Cdd:PHA03247   2612 APPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGraaqasspPQRPRRRAARPT 2691
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10879 V---------PAPTPKKVEAPPAKAPEVPPKEVTPEKKVPVVPPKKPEAPPPKVPEPPKEVVPEKKVSmvpPKRPEAPPA 10949
Cdd:PHA03247   2692 VgsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR---PPTTAGPPA 2768
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10950 KVPEASKEVVPEKKVSVAPKKKPEAPAVKVPEAPKKVVPEKKVPVAAPKKP--EAPAAEVPEVPKAAVPQKKIPEAVPPK 11027
Cdd:PHA03247   2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPpaASPAGPLPPPTSAQPTAPPPPPGPPPP 2848
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11028 PESPPPEVyeepaeeivpeeppeevveepepapppkvtVPPKKPVPEKKAPPAVVKKPEPPPAKAPEVPKEAPPEKKVPS 11107
Cdd:PHA03247   2849 SLPLGGSV------------------------------APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 11108 VVPKKPEAPP--AKVPEVPKEVVPEKKVAVPKKPEVPPAKvPEVPKKPVVEEKPVIEEKPAIPVAEKVESPPTEV 11180
Cdd:PHA03247   2899 ALPPDQPERPpqPQAPPPPQPQPQPPPPPQPQPPPPPPPR-PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRV 2972
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1516-1600 1.61e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 45.86  E-value: 1.61e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEgTKGEAALKIDSTISQDSAWYTATAINK 1595
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVR-ENGVHSLIIEPVTSRDAGIYTCIATNR 79

                    ....*
gi 1958765569  1596 AGRDT 1600
Cdd:cd20990      80 AGQNS 84
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8047-8141 1.62e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.10  E-value: 1.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8047 PPFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVA 8126
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*
gi 1958765569  8127 GKDSCSAQLGVQEPP 8141
Cdd:cd05762      81 GSRQAQVNLTVVDKP 95
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
7112-7187 1.62e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.81  E-value: 1.62e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7112 KPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGK 7187
Cdd:cd05747       9 KPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
18724-18805 1.62e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.57  E-value: 1.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18724 TVKAGDTIRLEAGVRGKPFPEVAWTKDKdATDLTRSPRVKIdtsAESSKFSLTKAKRSDGGKYVVTATNPAGSFVAYATV 18803
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKDG-VPLLGKDERITT---LENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVL 85

                    ..
gi 1958765569 18804 NV 18805
Cdd:cd20952      86 DV 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6738-6818 1.62e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 45.64  E-value: 1.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6738 LEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNI-YFEDTVAELELFNIDVSQSGEYTCVVSNNAGQASCTTRL 6816
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569  6817 FV 6818
Cdd:cd20973      87 TV 88
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
9201-9263 1.62e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 46.10  E-value: 1.62e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  9201 LSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSD 9263
Cdd:cd05736      20 LRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVD 82
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
11643-11703 1.62e-04

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 45.70  E-value: 1.62e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11643 SVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCV 11703
Cdd:cd20967      10 SKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV 70
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
6272-6342 1.63e-04

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 45.92  E-value: 1.63e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6272 KAGDSARLECKITGSPEIRVVWYR-------NEHELTASDKYQMTFIDSVAVMQmnslgTEDSGDFICEAQNPAGSTS 6342
Cdd:cd20971      14 RYQSNATLVCKVTGHPKPIVKWYRqgkeiiaDGLKYRIQEFKGGYHQLIIASVT-----DDDATVYQVRATNQGGSVS 86
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
129-193 1.63e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.85  E-value: 1.63e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   129 GIPTPVVKFYRDGAEIQ-SSLDFQISQEGdlySLLIAEAYPEDSGTYSVNATNSVG-RATSTADLLV 193
Cdd:cd05724      24 GHPEPTVSWRKDGQPLNlDNERVRIVDDG---NLLIAEARKSDEGTYKCVATNMVGeRESRAARLSV 87
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
33891-33984 1.64e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 46.08  E-value: 1.64e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPSDISIAE--GKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFhienTDDLTTLIIMDVQKQDGGLYTLS 33968
Cdd:cd05730       1 PPTIRARQSEVNATAnlGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSF----NEDGSEMTILDVDKLDEAEYTCI 76
                            90
                    ....*....|....*.
gi 1958765569 33969 LGNEFGSDSATVNINI 33984
Cdd:cd05730      77 AENKAGEQEAEIHLKV 92
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
4604-4663 1.64e-04

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 45.80  E-value: 1.64e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4604 QVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVI 4663
Cdd:cd20927      31 QVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8988-9068 1.65e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 45.64  E-value: 1.65e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8988 PPFfdI-PLAPVDAVVGESADLECHVTGtQPIK-VTWAKDNREIRSGGNyQISYLENSahLTIVKVDKG-DSGQYTCYAI 9064
Cdd:cd20958       1 PPF--IrPMGNLTAVAGQTLRLHCPVAG-YPISsITWEKDGRRLPLNHR-QRVFPNGT--LVIENVQRSsDEGEYTCTAR 74

                    ....
gi 1958765569  9065 NEVG 9068
Cdd:cd20958      75 NQQG 78
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5603-5705 1.65e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.10  E-value: 1.65e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5603 PPYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSNDV 5682
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90       100
                    ....*....|....*....|...
gi 1958765569  5683 GTTSSKATIFVkeppqfIKKPSP 5705
Cdd:cd05762      81 GSRQAQVNLTV------VDKPDP 97
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
7113-7196 1.65e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.57  E-value: 1.65e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7113 PVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIrPGGNYTITCVGNTPhLRILKVGKGDSGQYTCQATNDVGKDMCSA 7192
Cdd:cd20952       6 PQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPL-LGKDERITTLENGS-LQIKGAEKSDTGEYTCVALNLSGEATWSA 83

                    ....
gi 1958765569  7193 QLSV 7196
Cdd:cd20952      84 VLDV 87
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
6929-6995 1.67e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 45.31  E-value: 1.67e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  6929 GDSVSLQCQVAGTPEITVSWFKGDTKLrstPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGT 6995
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQL---SVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGS 65
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
28893-28950 1.68e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.01  E-value: 1.68e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28893 YQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKS 28950
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLppSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
29958-30052 1.68e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.10  E-value: 1.68e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29958 LELADDLKktviIRAGASLRLMVSVSGRPSPVITWSK--KGIDLANRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQS 30035
Cdd:cd05762       5 IQFPEDMK----VRAGESVELFCKVTGTQPITCTWMKfrKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*..
gi 1958765569 30036 GKKSATVLVKVYDTPGP 30052
Cdd:cd05762      81 GSRQAQVNLTVVDKPDP 97
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7301-7372 1.69e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 45.60  E-value: 1.69e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  7301 PPVGALK-GSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNfdtSLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd20957       8 PPVQTVDfGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDG 77
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
6932-7001 1.69e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 45.25  E-value: 1.69e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6932 VSLQCQVAGTPEITVSWFKGDTKLrstPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIGTAASKTV 7001
Cdd:cd05746       1 VQIPCSAQGDPEPTITWNKDGVQV---TESGKFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMV 67
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
4970-5038 1.69e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 45.31  E-value: 1.69e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4970 CKIAGSLPMRVSWFKDGKEIAASDRYQiafVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSRGALIV 5038
Cdd:cd05745       9 CEAQGYPQPVIAWTKGGSQLSVDRRHL---VLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
17048-17130 1.70e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.10  E-value: 1.70e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17048 VHAGGVIRIIAYVSGKPPPTVTWnMNERALPQEA---TIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIVDV 17124
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTW-MKFRKQIQEGegiKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTV 91

                    ....*.
gi 1958765569 17125 LDVPGP 17130
Cdd:cd05762      92 VDKPDP 97
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
24846-24904 1.71e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.47  E-value: 1.71e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24846 PVIGRPRPKISWVKDGEPLR-QTTRVNVEETATstiLHIKESSKDDFGKYSVTATNNAGT 24904
Cdd:cd05724      21 PPRGHPEPTVSWRKDGQPLNlDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGE 77
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
4482-4569 1.72e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 45.91  E-value: 1.72e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4482 FIKELEPVqsAINKKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIyFEDkiASLEIPLAKLKDSGTYSCTASNEAGSS 4561
Cdd:cd04969       7 PVKKKILA--AKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICI-LPD--GSLKIKNVTKSDEGKYTCFAVNFFGKA 81

                    ....*...
gi 1958765569  4562 SSSATVAV 4569
Cdd:cd04969      82 NSTGSLSV 89
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
18431-18507 1.72e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.96  E-value: 1.72e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 18431 TVRVGQTIRILARVKGRPEPDITWSKEGKVLVK-DKRVDLIHDlpRVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:cd20970      13 TAREGENATFMCRAEGSPEPEISWTRNGNLIIEfNTRYIVREN--GTTLTIRNIRRSDMGIYLCIASNGVPGSVEKRI 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
1809-1890 1.73e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 45.64  E-value: 1.73e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1809 PVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDG---IHYLDivdcKSYDTGEVKVTAENPEGVTeHKV 1885
Cdd:cd20958       9 NLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNGtlvIENVQ----RSSDEGEYTCTARNQQGQS-ASR 83

                    ....*
gi 1958765569  1886 KLEIQ 1890
Cdd:cd20958      84 SVFVK 88
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
4301-4381 1.73e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 45.69  E-value: 1.73e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4301 LEVALGHLAKFTCEIQGAPNVRFQW-------FKAGREiyesdkcsiRSSNYISSLE---ILRTQVVDCGEYTCKASNEY 4370
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWqkdggtdFPAARE---------RRMHVMPEDDvffIVDVKIEDTGVYSCTAQNSA 79
                            90
                    ....*....|.
gi 1958765569  4371 GSVSCTATLTV 4381
Cdd:cd05763      80 GSISANATLTV 90
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
5719-5785 1.74e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 45.25  E-value: 1.74e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5719 CQVTGTPEIRVSWYLDGNEITDLRRYGISfVDGlaTFQISNARVENSGTYVCEARNDAGTASCSIEL 5785
Cdd:cd05746       5 CSAQGDPEPTITWNKDGVQVTESGKFHIS-PEG--YLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
1682-1754 1.74e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 45.67  E-value: 1.74e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  1682 FECRLTpiGDPTMVVEWLHDGKPLEAANRLRLIN-EFGYCSLDYEaaysrDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:cd05728      19 WECKAS--GNPRPAYRWLKNGQPLASENRIEVEAgDLRITKLSLS-----DSGMYQCVAENKHGTIYASAELAV 85
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
8421-8503 1.75e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 45.62  E-value: 1.75e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8421 PATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFK-DGKELtgdSKYKISFFNKVsgLKIISVAPGDSGVYSFEVQNP 8499
Cdd:cd04968       1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKvDGSPS---SQWEITTSEPV--LEIPNVQFEDEGTYECEAENS 75

                    ....
gi 1958765569  8500 VGKD 8503
Cdd:cd04968      76 RGKD 79
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
6460-6538 1.75e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 45.72  E-value: 1.75e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6460 GEPAELQASIEGAPPISVHWLKEKEEVVRESENvRISFVNNVATLQFAKAEPANAGKYICQVKNDGGVRENMASLTVLE 6538
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSK-QLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8517-8607 1.78e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 46.01  E-value: 1.78e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8517 PPSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAIS-SGR----KYQTTLTD-----NTCALTVNmledaDAG 8586
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPeSPRfrvgDYVTSDGDvvsyvNISSVRVE-----DGG 75
                            90       100
                    ....*....|....*....|.
gi 1958765569  8587 DYTCIATNVAGSDECSAPLTV 8607
Cdd:cd20956      76 EYTCTATNDVGSVSHSARINV 96
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
1044-1119 1.78e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 45.67  E-value: 1.78e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1044 PVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNkQTGECRLVISMTFADDAGEYTIVIRNKHG 1119
Cdd:cd05891       8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLE-QGKYASLTIKGVTSEDSGKYSINVKNKYG 82
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
31553-31637 1.78e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.10  E-value: 1.78e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31553 RGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNGvERKDAGFYVVCAKNRFGIDQKTVELDVAD 31632
Cdd:cd05762      15 AGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEG-QQEHCGCYTLEVENKLGSRQAQVNLTVVD 93

                    ....*
gi 1958765569 31633 VPDPP 31637
Cdd:cd05762      94 KPDPP 98
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
6543-6622 1.80e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.78  E-value: 1.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6543 VEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSS 6622
Cdd:cd20949       3 TENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7293-7387 1.80e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.10  E-value: 1.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*
gi 1958765569  7373 GSDTCACTVKFKEPP 7387
Cdd:cd05762      81 GSRQAQVNLTVVDKP 95
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8421-8511 1.81e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 45.70  E-value: 1.81e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8421 PATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKyKISFFNKVSGLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  8501 GKDSCTVSIQV 8511
Cdd:cd20976      80 GQVSCSAWVTV 90
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
12535-12614 1.81e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.58  E-value: 1.81e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12535 KLQDYTGVEKDEVVLQCE-ISKADAP-VKWFKDGKEIKPSKNAVIKADGKKR--MLILKKALKSDIGQYTCDC----GTD 12606
Cdd:cd05750       5 EMKSQTVQEGSKLVLKCEaTSENPSPrYRWFKDGKELNRKRPKNIKIRNKKKnsELQINKAKLEDSGEYTCVVenilGKD 84

                    ....*...
gi 1958765569 12607 QTSGKLDI 12614
Cdd:cd05750      85 TVTGNVTV 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7866-7945 1.81e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.58  E-value: 1.81e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7866 EAAIGEPTTLQCK-VDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVAS--LVINKVDHSDVGEYTCKAENSVGAVASSAV 7942
Cdd:cd05750      10 TVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNseLQINKAKLEDSGEYTCVVENILGKDTVTGN 89

                    ...
gi 1958765569  7943 LVI 7945
Cdd:cd05750      90 VTV 92
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7294-7373 1.81e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.58  E-value: 1.81e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFT--QKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRS-SKKFKVTSKNfdTSLHIFNLEAPDIGEYHCKATN 7370
Cdd:cd20970       1 PVIStpQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEfNTRYIVRENG--TTLTIRNIRRSDMGIYLCIASN 78

                    ...
gi 1958765569  7371 EVG 7373
Cdd:cd20970      79 GVP 81
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
14907-14988 1.82e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 45.67  E-value: 1.82e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14907 DIVVI-EGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHIS-AHLEVPKSVHADAGVYTITLENKLGSATASI 14984
Cdd:cd05891       9 DVVTImEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYGGETVDV 88

                    ....
gi 1958765569 14985 NVKV 14988
Cdd:cd05891      89 TVSV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
33704-33777 1.82e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 45.67  E-value: 1.82e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 33704 PRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMY-TLEIRNASVSDSGKYTVKAKNFRG 33777
Cdd:cd05891       8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYaSLTIKGVTSEDSGKYSINVKNKYG 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2931-3014 1.82e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.87  E-value: 1.82e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2931 ITSMLKDINAEEKDTITFEVTVnyEGI---SYKWLKNGVEIKSTD---RCQMRTKKLTHSLNIRNVHFGDAADYTFVA-- 3002
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEV--QGKpdpEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAkn 80
                            90
                    ....*....|....
gi 1958765569  3003 --GKATSTATLYVE 3014
Cdd:cd20951      81 ihGEASSSASVVVE 94
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9306-9380 1.82e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 45.60  E-value: 1.82e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  9306 TATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHqkgDESKLEIRDTTKTDSGLYRCVAFNKHGEIESNVNLQV 9380
Cdd:cd20957      18 TAVFNCSVTGNPIHTVLWMKDG-KPLGHSSRVQIL---SEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAELKL 88
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8530-8605 1.83e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.65  E-value: 1.83e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8530 LSGSSVVMECKV-FGSPPISVLWLHDGNAISSGRKYQTTLTDNTCA-LTVNMLEDADAGDYTCIATNVAGSDECSAPL 8605
Cdd:pfam00047     9 LEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSsLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
2586-2664 1.85e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 45.65  E-value: 1.85e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2586 LTDQTVAESQEAVFECEVA-NPESEGEWLKDGKHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEY----TYKVATSKTSA 2660
Cdd:cd20972       8 LRSQEVAEGSKVRLECRVTgNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYsclaTNSVGSDTTSA 87

                    ....
gi 1958765569  2661 KLKV 2664
Cdd:cd20972      88 EIFV 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4581-4663 1.85e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 45.86  E-value: 1.85e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4581 PSYLMLPGESA-------RLHCKLKGSPVIQVTWFKNNKELSESNTVRMSF-ANSEAILDITDVKVDDSGTYSCEATNDA 4652
Cdd:cd20990       1 PHFLQAPGDLTvqegklcRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVrENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  4653 GSDSCSTEVVI 4663
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1038-1128 1.85e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 45.86  E-value: 1.85e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYnKQTGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLV-RENGVHSLIIEPVTSRDAGIYTCIATNR 79
                            90
                    ....*....|.
gi 1958765569  1118 HGETSASASLL 1128
Cdd:cd20990      80 AGQNSFNLELV 90
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7401-7477 1.85e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 45.95  E-value: 1.85e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7401 GDPVELQAVVE-GFQPISVVWLKDkGEVIRESENVRISFVDNIAT-LQLGSPEASHSGKYVCQIKNDAGMRECSALLTV 7477
Cdd:cd20959      17 GMRAQLHCGVPgGDLPLNIRWTLD-GQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
5909-5973 1.85e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 45.53  E-value: 1.85e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5909 GSPPISITWLKDDQILEENDNVHIsFEDsvATLQVRSVDNGHSGRYTCQAKNESGVERCYAFLLV 5973
Cdd:cd04969      28 ASPKPTISWSKGTELLTNSSRICI-LPD--GSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
31047-31132 1.87e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 45.84  E-value: 1.87e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31047 VRKEMAD-VTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSR---KYKMSSDGrthTLTVMTEEQEDEGVYTCVATNE 31122
Cdd:cd20969       4 IRDRKAQqVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKsngRLTVFPDG---TLEVRYAQVQDNGTYLCIAANA 80
                            90
                    ....*....|
gi 1958765569 31123 VGEVETSSKL 31132
Cdd:cd20969      81 GGNDSMPAHL 90
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
5149-5225 1.88e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 45.31  E-value: 1.88e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5149 KGDATQLVCKVTGTPPIKITWFANDRELRESSKHkmsFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTSIVIV 5225
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRH---LVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8993-9071 1.88e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.65  E-value: 1.88e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8993 IPLAPVDAVVGESADLECHV-TGTQPIKVTWAK-DNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKD 9070
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKeGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                    .
gi 1958765569  9071 S 9071
Cdd:pfam00047    81 T 81
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
23746-23829 1.90e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 45.70  E-value: 1.90e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23746 PAFSSY----SVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLdLTTLSIKETHKDDGGHYGITVANVVG 23821
Cdd:cd20976       2 PSFSSVpkdlEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAG-VGELHIQDVLPEDHGTYTCLAKNAAG 80

                    ....*...
gi 1958765569 23822 QKTAAIEI 23829
Cdd:cd20976      81 QVSCSAWV 88
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
33076-33143 1.90e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143278 [Multi-domain]  Cd Length: 98  Bit Score: 45.74  E-value: 1.90e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 33076 LTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTS-------ARHQVTTAKYKSTFEISSVQASDEGNY 33143
Cdd:cd05870       5 IIQLKNETTVENGAATLSCKAEGEPIPEITWKRASDGHTFSegdkspdGRIEVKGQHGESSLHIKDVKLSDSGRY 79
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8427-8511 1.92e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 45.86  E-value: 1.92e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8427 KPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDS-KYKISF-FNKVSGLKIISVAPGDSGVYSFEVQNPVGKDS 8504
Cdd:cd05893       6 KLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSdHYTIQRdLDGTCSLHTTASTLDDDGNYTIMAANPQGRIS 85

                    ....*..
gi 1958765569  8505 CTVSIQV 8511
Cdd:cd05893      86 CTGRLMV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
21601-21667 1.92e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 45.66  E-value: 1.92e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 21601 VLGRPKPTVTWKKGDQILKQTQRVNVENTATSTI-LNINECVRSDSGAYPLTAKNTVG-EVGDViTIQV 21667
Cdd:cd05737      25 VWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVyFTINGVSSEDSGKYGLVVKNKYGsETSDV-TVSV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
4588-4656 1.92e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 45.66  E-value: 1.92e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSF-ANSEAILDITDVKVDDSGTYSCEATNDAGSDS 4656
Cdd:cd05737      16 GKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVeAGRTVYFTINGVSSEDSGKYGLVVKNKYGSET 85
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5993-6066 1.92e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 45.63  E-value: 1.92e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5993 PVTLECVVAGTPELKVKWLKDGKQIVPSRYFSM----SFENNVASF-RIQSVMKQDSGQYTFKVENDFGSSSCDAYLRV 6066
Cdd:cd20956      18 SVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgdyvTSDGDVVSYvNISSVRVEDGGEYTCTATNDVGSVSHSARINV 96
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
33698-33787 1.92e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 45.86  E-value: 1.92e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRN-MYTLEIRNASVSDSGKYTVKAKNFR 33776
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENgVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569 33777 GQCSATASLTV 33787
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
906-989 1.93e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 45.74  E-value: 1.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   906 LKNVTVVE-GESVTLECHISGYPSPKVTW---YREDYQIESSIDFQITFQSG--IARLMIREAFAEDSGRFTCSAVNEAG 979
Cdd:cd05869       8 VENQTAMElEEQITLTCEASGDPIPSITWrtsTRNISSEEKTLDGHIVVRSHarVSSLTLKYIQYTDAGEYLCTASNTIG 87
                            90
                    ....*....|
gi 1958765569   980 TVSTSCYLAV 989
Cdd:cd05869      88 QDSQSMYLEV 97
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
8239-8315 1.93e-04

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 45.27  E-value: 1.93e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8239 KKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENlltSIHILNVDTADIGEYQCKATNDVGS 8315
Cdd:cd05723       2 KKPSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEH---NLQVLGLVKSDEGFYQCIAENDVGN 75
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
12888-12957 1.94e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.78  E-value: 1.94e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 12888 FLRPLTDLQVKEKETARFECEISKENV-KVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSC 12957
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQpNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTC 72
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
17338-17420 1.95e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 45.60  E-value: 1.95e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17338 DKLTVRVGEAFALTGRYSGKPKPKVDWFK-DEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGRYCVVVENSTGSRKGFC 17416
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRgDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569 17417 QVNV 17420
Cdd:cd05894      83 FVKV 86
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
5041-5129 1.95e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.81  E-value: 1.95e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5041 PPSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVA 5120
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ....*....
gi 1958765569  5121 GSVECSANL 5129
Cdd:cd05747      83 GKQEAQFTL 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5611-5693 1.97e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.58  E-value: 1.97e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5611 QSQDVNPSTRVQLKALVGGTAP-MTIKWFKDNKELhpGAARS----VWKDDTSTILELFSAKAADSGTYICQLSNDVGTT 5685
Cdd:cd05750       7 KSQTVQEGSKLVLKCEATSENPsPRYRWFKDGKEL--NRKRPknikIRNKKKNSELQINKAKLEDSGEYTCVVENILGKD 84

                    ....*...
gi 1958765569  5686 SSKATIFV 5693
Cdd:cd05750      85 TVTGNVTV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
3208-3288 1.98e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 45.66  E-value: 1.98e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3208 VTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKF-LHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTSASL 3286
Cdd:cd05737      11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLkVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTV 90

                    ..
gi 1958765569  3287 SV 3288
Cdd:cd05737      91 SV 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
3462-3550 1.99e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.57  E-value: 1.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3462 VFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLtPSADYKFvFDGNNHSLIILFTRFQDEGEYTCMASNEYGR 3541
Cdd:cd20952       1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPL-LGKDERI-TTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78

                    ....*....
gi 1958765569  3542 AVCSAHLKV 3550
Cdd:cd20952      79 ATWSAVLDV 87
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6729-6818 2.00e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 45.86  E-value: 2.00e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6729 PSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELV-KGDRCNIYFE-DTVAELELFNIDVSQSGEYTCVVSNN 6806
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  6807 AGQASCTTRLFV 6818
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
31058-31124 2.02e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 45.80  E-value: 2.02e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 31058 LGEAAQLSCQIVGRPL-PDIKWYRFGKELVQSRKYKMS---SDGRTHTLTVMTEEQEDEGVYTCVATNEVG 31124
Cdd:cd05865      14 VGESKFFLCQVAGEAKdKDISWFSPNGEKLTPNQQRISvvrNDDYSSTLTIYNANIDDAGIYKCVVSNEDE 84
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8423-8498 2.04e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.40  E-value: 2.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8423 TIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQN 8498
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQ 76
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
5793-5863 2.04e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.40  E-value: 2.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5793 FIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCAPSDVGEYQC 5863
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTC 72
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
18033-18112 2.05e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.57  E-value: 2.05e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18033 VVKAGTTVRFPAIIRGVPVPTAKWATDG-TEITTDDHYTVETDSfssVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLT 18111
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKDGvPLLGKDERITTLENG---SLQIKGAEKSDTGEYTCVALNLSGEATWSAVLD 86

                    .
gi 1958765569 18112 V 18112
Cdd:cd20952      87 V 87
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4253-4286 2.06e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 45.46  E-value: 2.06e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1958765569  4253 TLVIESVKTEDEGEYVCEASNGNGKAMTSAKLTV 4286
Cdd:cd05725      50 SLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
5512-5600 2.06e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 45.69  E-value: 2.06e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5512 SFTKKLRKMDSIKGSFIDLECIVAGsHPI-SIQWFKDD-QEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKA 5589
Cdd:cd05763       1 SFTKTPHDITIRAGSTARLECAATG-HPTpQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSA 79
                            90
                    ....*....|.
gi 1958765569  5590 GHSQCSGHLTV 5600
Cdd:cd05763      80 GSISANATLTV 90
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
15916-16006 2.08e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.58  E-value: 2.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15916 RGDTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEkptdaLNITKEEVsrSEAKTELSIPKAVREDKGTYTITASNRL 15995
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLII-----EFNTRYIV--RENGTTLTIRNIRRSDMGIYLCIASNGV 80
                            90
                    ....*....|..
gi 1958765569 15996 -GSVFRNVHVEV 16006
Cdd:cd20970      81 pGSVEKRITLQV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
30660-30729 2.08e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 45.65  E-value: 2.08e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 30660 VRQGGVIRLTIPIKGKPFPICKWTKEGQDVSKRAMI---ATSETHTeLVIKEADRNDSGTYDLVLENKCGKKT 30729
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIqihQEGDLHS-LIIAEAFEEDTGRYSCLATNSVGSDT 84
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8997-9078 2.08e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.47  E-value: 2.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8997 PVD--AVVGESADLEC-----HVTGTqpikVTWAKDNREIRSGGNyQISYLENsAHLTIVKVDKGDSGQYTCYAINEVG- 9068
Cdd:cd05724       4 PSDtqVAVGEMAVLECspprgHPEPT----VSWRKDGQPLNLDNE-RVRIVDD-GNLLIAEARKSDEGTYKCVATNMVGe 77
                            90
                    ....*....|
gi 1958765569  9069 KDSCTAQLNI 9078
Cdd:cd05724      78 RESRAARLSV 87
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
9179-9273 2.09e-04

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409398  Cd Length: 101  Bit Score: 45.94  E-value: 2.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9179 KKPPVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFAS---GTAV---LELKDTAKADSGDY 9252
Cdd:cd05735       1 KIPAMITSYPNTTLATKGQKKEMSCTAHGEKPIIVRWEKEDTIINPSEMSRYLVTTkevGDEVistLQILPTVREDSGFF 80
                            90       100
                    ....*....|....*....|.
gi 1958765569  9253 VCKASNVAGSDTSKCKVTIKE 9273
Cdd:cd05735      81 SCHAINSYGEDRGIIQLTVQE 101
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
12093-12170 2.09e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.19  E-value: 2.09e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  12093 EDQTVKEGQTATFVCELS-HEKMHVVWFKNDVKLHTTR-TVLMSSEGKTYKLEIRETTLDDiS-----QIKAQVKNLSST 12165
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKLLAESgRFSVSRSGSTSTLTISNVTPED-SgtytcAATNSSGSASSG 80

                     ....*
gi 1958765569  12166 ANLKV 12170
Cdd:smart00410    81 TTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27812-28075 2.10e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.39  E-value: 2.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27812 PPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSSTVSVKVLDTPAACQKLQVKHVSL 27891
Cdd:COG3401      69 TGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLY 148
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27892 GTVTLLWDPPLIDGGSPIINYVIEKRDATKRTWSIVSHKcSGTSFKVMDLSEK--TPFFFRVLAENEIGIGEPCETTEPV 27969
Cdd:COG3401     149 GVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTV-TSTTLVDGGGDIEpgTTYYYRVAATDTGGESAPSNEVSVT 227
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27970 KAAEVPAPIRDLSMKDSTKTSVVLSWTKPDFDGgsiITDYLVERKGKGEQAWSHAGISKTCEIEIGQLKEQSVLEFRVSA 28049
Cdd:COG3401     228 TPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTA 304
                           250       260
                    ....*....|....*....|....*..
gi 1958765569 28050 RNEKG-QSDPVTIgpLTVKELVITPEV 28075
Cdd:COG3401     305 VDAAGnESAPSNV--VSVTTDLTPPAA 329
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
909-989 2.10e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 45.46  E-value: 2.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   909 VTVVEGESVTLECHISGYPSPKVTW-YREDYQIESSIDFQITFQSGiARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYL 987
Cdd:cd20969      12 VFVDEGHTVQFVCRADGDPPPAILWlSPRKHLVSAKSNGRLTVFPD-GTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHL 90

                    ..
gi 1958765569   988 AV 989
Cdd:cd20969      91 HV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5041-5131 2.11e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 45.70  E-value: 2.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5041 PPSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGScYITKEASESSLELYAVKTTDSGTYTCKVSNVA 5120
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  5121 GSVECSANLFV 5131
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5229-5310 2.12e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 45.25  E-value: 2.12e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKfvASDAGEYQCRVTNEVG 5308
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNGTLVIENVQR--SSDEGEYTCTARNQQG 78

                    ..
gi 1958765569  5309 SS 5310
Cdd:cd20958      79 QS 80
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
5880-5964 2.14e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 45.31  E-value: 2.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5880 LKEPPSfikkieNVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDnvHISFEDSvATLQVRSVDNGHSGRYTCQAK 5959
Cdd:cd20968       2 ITRPPT------NVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENN--RIAVLES-GSLRIHNVQKEDAGQYRCVAK 72

                    ....*
gi 1958765569  5960 NESGV 5964
Cdd:cd20968      73 NSLGI 77
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
9194-9271 2.14e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 45.75  E-value: 2.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9194 SEGDFLQLSCHVQGSEP-IRIQWLRAGREIKPSDR---CSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSDTSKCKV 9269
Cdd:cd05895      12 AAGSKLVLRCETSSEYPsLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSASANV 91

                    ..
gi 1958765569  9270 TI 9271
Cdd:cd05895      92 TI 93
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
15918-16013 2.14e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 45.72  E-value: 2.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15918 DTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKPTDAlnitkeEVSRSEAKTELSIPKAVREDKGTYTITASNRLGS 15997
Cdd:cd05762       9 EDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGI------KIENTENSSKLTITEGQQEHCGCYTLEVENKLGS 82
                            90
                    ....*....|....*.
gi 1958765569 15998 VFRNVHVEVYDRPSPP 16013
Cdd:cd05762      83 RQAQVNLTVVDKPDPP 98
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
12983-13060 2.15e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 2.15e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12983 NLEVSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSYNCRLPSSrtDGKVKVH 13060
Cdd:cd05747      12 SLTVSEGESARFSCDVDgEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENS--EGKQEAQ 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
12351-12426 2.15e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 2.15e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 12351 PLIFITPlSDVKVFEKDEAKFECEVSREPK-TFRWLKGTQEIAGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAE 12426
Cdd:pfam13927     2 PVITVSP-SSVTVREGETVTLTCEATGSPPpTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
6915-6995 2.18e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 45.67  E-value: 2.18e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFV-TE--LEPLEA-SVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVA-TLVFNKVGINDSGEYTCVA 6989
Cdd:cd05729       1 PRFTdTEkmEEREHAlPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIV 80

                    ....*.
gi 1958765569  6990 ENSIGT 6995
Cdd:cd05729      81 ENEYGS 86
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
9003-9078 2.18e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 44.93  E-value: 2.18e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  9003 GESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISyleNSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLNI 9078
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVL---SSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4499-4569 2.18e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 45.08  E-value: 2.18e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  4499 LECQVDEDRKVSITWSKDGQKLPAGKdYKIyFEDKiaSLEIPLAKLKDSGTYSCTASNEAGSSSSSATVAV 4569
Cdd:cd05725      17 FQCEVGGDPVPTVRWRKEDGELPKGR-YEI-LDDH--SLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5229-5316 2.19e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 45.42  E-value: 2.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDN--TTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTNE 5306
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|
gi 1958765569  5307 VGSSTCSARV 5316
Cdd:cd20974      81 SGQATSTAEL 90
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
16638-16725 2.19e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.40  E-value: 2.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16638 MEVEEGTDVNIVAKIKGVPFPTLTW-FKAPPKKPDSKepvvYDTHVNkqVVDDtcTLVIPQSRRSDTGLYSITAVNNLGT 16716
Cdd:cd20949       9 TTVKEGQSATILCEVKGEPQPNVTWhFNGQPISASVA----DMSKYR--ILAD--GLLINKVTQDDTGEYTCRAYQVNSI 80

                    ....*....
gi 1958765569 16717 ASKEMRLNV 16725
Cdd:cd20949      81 ASDMQERTV 89
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
8067-8135 2.19e-04

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 45.27  E-value: 2.19e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8067 FKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENtatLTVLKVAKGDAGQYTCYASNVAGKDSCSAQL 8135
Cdd:cd05723      17 FECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVGNAQASAQL 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
20202-20295 2.19e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 45.46  E-value: 2.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20202 PPEGELDAELRKTLILRagvtmrlyVPVKGRPPPKITWS---KPNVNLRERIGLDiKSTdfdtfLRCENVNKYDAGKYIL 20278
Cdd:cd20978       6 KPEKNVVVKGGQDVTLP--------CQVTGVPQPKITWLhngKPLQGPMERATVE-DGT-----LTIINVQPEDTGYYGC 71
                            90
                    ....*....|....*..
gi 1958765569 20279 TLENSCGKKEYTIVVKV 20295
Cdd:cd20978      72 VATNEIGDIYTETLLHV 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
4291-4381 2.19e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 45.32  E-value: 2.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4291 APVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREI-YESDKCSIRSSnyISSLEILRTQVVDCGEYTCKASNE 4369
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqYAADRSTCEAG--VGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569  4370 YGSVSCTATLTV 4381
Cdd:cd20976      79 AGQVSCSAWVTV 90
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5712-5787 2.20e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.58  E-value: 2.20e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5712 GQSTTFECQVTG-TPEIRVSWYLDGNEITDLRRYGISFVDGL--ATFQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd05750      14 GSKLVLKCEATSeNPSPRYRWFKDGKELNRKRPKNIKIRNKKknSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
1525-1607 2.20e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 45.66  E-value: 2.20e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1525 VNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGTKgEAALKIDSTISQDSAWYTATAINKAGRDTTRCK 1604
Cdd:cd05737      11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGR-TVYFTINGVSSEDSGKYGLVVKNKYGSETSDVT 89

                    ...
gi 1958765569  1605 VNI 1607
Cdd:cd05737      90 VSV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
24834-24903 2.21e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 2.21e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24834 SVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAG 24903
Cdd:cd05747      14 TVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4588-4653 2.21e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 2.21e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAG 4653
Cdd:cd05747      18 GESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
28876-28944 2.23e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 2.23e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 28876 KQTHIVRAGASIRLFIAYQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVEN 28944
Cdd:pfam13927     8 PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
1801-1889 2.24e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 45.32  E-value: 2.24e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSK-RFRVRYdGIHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd20976       2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAdRSTCEA-GVGELHIQDVLPEDHGTYTCLAKNAAG 80
                            90
                    ....*....|
gi 1958765569  1880 VTEHKVKLEI 1889
Cdd:cd20976      81 QVSCSAWVTV 90
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
5710-5777 2.24e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 45.72  E-value: 2.24e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5710 RNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDAG 5777
Cdd:cd05736      13 EPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
24824-24907 2.24e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.58  E-value: 2.24e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQA--GEDLKIEIPVIGRPRPKISWVKDGEpLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNN 24901
Cdd:cd20970       1 PVISTPQPSFTVTAreGENATFMCRAEGSPEPEISWTRNGN-LIIEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNG 79

                    ....*.
gi 1958765569 24902 AGTATE 24907
Cdd:cd20970      80 VPGSVE 85
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
18037-18112 2.25e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 44.93  E-value: 2.25e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 18037 GTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETdsfSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLTV 18112
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLS---SGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
21984-22053 2.25e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 45.65  E-value: 2.25e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21984 TLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGG 22053
Cdd:cd20972      12 EVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8907-8980 2.25e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 45.63  E-value: 2.25e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8907 GLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQ-----TSFLDNIATLNIFKTDRSLAGQYSCTVTNPIGSASSSAKL 8980
Cdd:cd20956      16 GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRvgdyvTSDGDVVSYVNISSVRVEDGGEYTCTATNDVGSVSHSARI 94
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9588-9665 2.26e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 45.22  E-value: 2.26e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9588 QDVTLKEGQTCTMTCQFSVPNVKS-EWFRNGRVLKPQGRVKTEVEHKVHkltIADVRAEDQGRYTC----KHEDLETSAE 9662
Cdd:cd20957       9 PVQTVDFGRTAVFNCSVTGNPIHTvLWMKDGKPLGHSSRVQILSEDVLV---IPSVKREDKGMYQCfvrnDGDSAQATAE 85

                    ...
gi 1958765569  9663 LRI 9665
Cdd:cd20957      86 LKL 88
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
32299-32396 2.27e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 45.67  E-value: 2.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32299 PTETTLRPMFKRLLANAEcheGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDYYALHIRDTLPEDTGYYR 32378
Cdd:cd05729       1 PRFTDTEKMEEREHALPA---ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYT 77
                            90
                    ....*....|....*...
gi 1958765569 32379 VTATNTAGSTSCQAHLQV 32396
Cdd:cd05729      78 CIVENEYGSINHTYDVDV 95
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8614-8700 2.27e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 45.08  E-value: 2.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8614 VQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELvPGARCNVsLQDSvaELELFDVDTSQSGDYTCIVSNEAGRAS 8693
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL-PKGRYEI-LDDH--SLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  8694 CTTQLFV 8700
Cdd:cd05725      77 ASATLTV 83
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
15925-16006 2.28e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 45.32  E-value: 2.28e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15925 GEPVNIPADVTGLPMPKIEWSKNEKVIEKPTDAlnitkeevSRSEAKT-ELSIPKAVREDKGTYTITASNRLGSVFRNVH 16003
Cdd:cd20976      16 GQDFVAQCSARGKPVPRITWIRNAQPLQYAADR--------STCEAGVgELHIQDVLPEDHGTYTCLAKNAAGQVSCSAW 87

                    ...
gi 1958765569 16004 VEV 16006
Cdd:cd20976      88 VTV 90
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6554-6625 2.29e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 45.47  E-value: 2.29e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6554 GETCSLECKVAGTPELSVEWYKDGKLLTSSQKHkFSFYNKIS---SLKILSVEKEDAGTYTFQVQNNVGKSSCTA 6625
Cdd:cd05893      15 GMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDH-YTIQRDLDgtcSLHTTASTLDDDGNYTIMAANPQGRISCTG 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
20887-20981 2.30e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 45.32  E-value: 2.30e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20887 APTIVLDPTikdGLTVKAGDSIVLSAiSILGKPLPKSSWSKAGKDIRpSDIAQITSTPTSSMLTVKYATRKDAGEYTITA 20966
Cdd:cd20976       1 APSFSSVPK---DLEAVEGQDFVAQC-SARGKPVPRITWIRNAQPLQ-YAADRSTCEAGVGELHIQDVLPEDHGTYTCLA 75
                            90
                    ....*....|....*
gi 1958765569 20967 TNPFGTKEEHVKVSV 20981
Cdd:cd20976      76 KNAAGQVSCSAWVTV 90
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
7855-7946 2.32e-04

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 45.38  E-value: 2.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7855 PPYFIEPLEHvEAAIGEPTTLQCKVDGTPEIRISWYK-------EHTKLRSAPAYKmQFKNnvASLVINKVDHSDVGEYT 7927
Cdd:cd20954       2 PRWIVEPVDA-NVAAGQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYDPNVR-ILPN--GTLVFGHVQKENEGHYL 77
                            90
                    ....*....|....*....
gi 1958765569  7928 CKAENSVGAvASSAVLVIK 7946
Cdd:cd20954      78 CEAKNGIGS-GLSKVIFLK 95
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6924-6996 2.33e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 45.26  E-value: 2.33e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  6924 LEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRT-YFTNNVATLVFNKVGINDSGEYTCVAENSIGTA 6996
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
5627-5694 2.33e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 45.80  E-value: 2.33e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  5627 VGGTAPMT-IKWFKDNKE-LHPGAAR--SVWKDDTSTILELFSAKAADSGTYICQLSNDVGtTSSKATIFVK 5694
Cdd:cd05865      24 VAGEAKDKdISWFSPNGEkLTPNQQRisVVRNDDYSSTLTIYNANIDDAGIYKCVVSNEDE-GESEATVNVK 94
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
6271-6342 2.34e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.40  E-value: 2.34e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  6271 VKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTS 6342
Cdd:cd20949      11 VKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4201-4286 2.35e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 45.46  E-value: 2.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4201 ILKPLVDTISEKGDTVHLTSSISN--AKEVNWYFKGDLVPpGAKFQCLKEENayTLVIESVKTEDEGEYVCEASNGNGKA 4278
Cdd:cd20978       4 IQKPEKNVVVKGGQDVTLPCQVTGvpQPKITWLHNGKPLQ-GPMERATVEDG--TLTIINVQPEDTGYYGCVATNEIGDI 80

                    ....*...
gi 1958765569  4279 MTSAKLTV 4286
Cdd:cd20978      81 YTETLLHV 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8901-8981 2.36e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 45.08  E-value: 2.36e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8901 DVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSpnvQTSFLDNiATLNIFKTDRSLAGQYSCTVTNPIGSASSSAKL 8980
Cdd:cd05725       6 NQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG---RYEILDD-HSLKIRKVTAGDMGSYTCVAENMVGKIEASATL 81

                    .
gi 1958765569  8981 I 8981
Cdd:cd05725      82 T 82
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
4387-4476 2.36e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 45.53  E-value: 2.36e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDcRIT---DADNKHSLELSNLTVQDRGVYSCKASN 4463
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTD-RISlyqDNCGRICLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569  4464 KFGADICQAELTI 4476
Cdd:cd05892      80 EAGVVSCNARLDV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
12977-13047 2.36e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.40  E-value: 2.36e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12977 FTKNLANLEVSEGDTIKLVCEV-SKPGAEVTWYKGDEE----VIETGRFEILTDGrkriLIIQNAQLEDAGSYNCR 13047
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVkGEPQPNVTWHFNGQPisasVADMSKYRILADG----LLINKVTQDDTGEYTCR 73
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8062-8138 2.37e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.49  E-value: 2.37e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8062 GESGSFKCHVTGTAPIKITWAKDNREIRP---GGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQLGVQ 8138
Cdd:cd20951      15 KSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVVE 94
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
908-989 2.37e-04

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 45.62  E-value: 2.37e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   908 NVTVVEGESVTLECHISGYPSPKVT--WYREDYQI---ESSIDFQITF-QSGIARLMIREAFAEDSGRFTCSAVNEAGTV 981
Cdd:cd04970      11 NADITVGENATLQCHASHDPTLDLTftWSFNGVPIdleKIEGHYRRRYgKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSD 90

                    ....*...
gi 1958765569   982 STSCYLAV 989
Cdd:cd04970      91 SASATLVV 98
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
33084-33162 2.38e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 45.61  E-value: 2.38e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33084 VHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSAR---HQVTTAKYKSTFEisSVQASDEGNYSVVVENTDGKQEAQFTL 33160
Cdd:cd05857      16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKVRNQHWSLIME--SVVPSDKGNYTCVVENEYGSINHTYHL 93

                    ..
gi 1958765569 33161 TV 33162
Cdd:cd05857      94 DV 95
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
32201-32294 2.39e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 45.42  E-value: 2.39e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIK----PGdddKKYTFESDKGlyQLTINSVTTDDDAEYAV 32276
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIStstlPG---VQISFSDGRA--KLSIPAVTKANSGRYSL 75
                            90
                    ....*....|....*...
gi 1958765569 32277 VARNKHGEDSCKAKLTVT 32294
Cdd:cd20974      76 TATNGSGQATSTAELLVL 93
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
28081-28152 2.39e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 45.42  E-value: 2.39e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 28081 PGAQISVRIGHNVHLELPYKGKPKPSISWLKDG--LPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDN 28152
Cdd:cd20974       6 PLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
5704-5788 2.41e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 45.09  E-value: 2.41e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5704 SPVLVLRnGQSTTFECQVTGTPEIRVSWYLDGNEITDLRrygISFVDGLATFQISNARVENSGTYVCEARNDAGTASCSI 5783
Cdd:cd05731       3 SSTMVLR-GGVLLLECIAEGLPTPDIRWIKLGGELPKGR---TKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTI 78

                    ....*
gi 1958765569  5784 ELKVK 5788
Cdd:cd05731      79 SVTVE 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
31154-31218 2.42e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.86  E-value: 2.42e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31154 VGSTLRLHVMYIGRPVPAMTWYHGQKLLQNSESITIENTEHYTHLVMKNVQRkTHAGKYKVQLSN 31218
Cdd:pfam13927    15 EGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTR-SDAGTYTCVASN 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
32892-32975 2.42e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 45.26  E-value: 2.42e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32892 MRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYT-NTSGVLTLEILDCQTEDSGTYRAVCTNYKGEASDY 32970
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                    ....*
gi 1958765569 32971 ATLDV 32975
Cdd:cd20973      84 AELTV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
32886-32976 2.43e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 45.42  E-value: 2.43e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32886 PRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNG--VELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNY 32963
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569 32964 KGEASDYATLDVT 32976
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5042-5132 2.44e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.49  E-value: 2.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5042 PSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKEL---VSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSN 5118
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  5119 VAGSVECSANLFVK 5132
Cdd:cd20951      81 IHGEASSSASVVVE 94
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
3464-3550 2.46e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 45.13  E-value: 2.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3464 IKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTP-SADYKFVFDGNnhslIILFTRFQ--DEGEYTCMASNEYG 3540
Cdd:cd04978       3 IIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPaPEDMRRTVDGR----TLIFSNLQpnDTAVYQCNASNVHG 78
                            90
                    ....*....|
gi 1958765569  3541 RAVCSAHLKV 3550
Cdd:cd04978      79 YLLANAFLHV 88
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
8997-9068 2.46e-04

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 45.38  E-value: 2.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8997 PVDAVV--GESADLECHVTGTQPIKVTWAK-------DNREIRSGGNYQIsyLENSAhLTIVKVDKGDSGQYTCYAINEV 9067
Cdd:cd20954       8 PVDANVaaGQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYDPNVRI--LPNGT-LVFGHVQKENEGHYLCEAKNGI 84

                    .
gi 1958765569  9068 G 9068
Cdd:cd20954      85 G 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
16639-16725 2.48e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 45.18  E-value: 2.48e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16639 EVEEGTDVNIVAKIKGVPFPTLTWFKappkkpdSKEPVVYDTHvNKQVVDDT--CTLVIPQSRRSDTGLYSITAVNNLGT 16716
Cdd:cd05744      11 EVQEGRLCRFDCKVSGLPTPDLFWQL-------NGKPVRPDSA-HKMLVRENgrHSLIIEPVTKRDAGIYTCIARNRAGE 82

                    ....*....
gi 1958765569 16717 ASKEMRLNV 16725
Cdd:cd05744      83 NSFNAELVV 91
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
1516-1598 2.50e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 45.47  E-value: 2.50e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1516 PAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGTKGEAALKIDSTISQDSAWYTATAINK 1595
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80

                    ...
gi 1958765569  1596 AGR 1598
Cdd:cd05893      81 QGR 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
9310-9380 2.51e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 45.14  E-value: 2.51e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9310 IAKVGGD----------PIPNVKWTKGKwRQLNQGGRILIHQKGDeskLEIRDTTKTDSGLYRCVAFNKHGEIESNVNLQ 9379
Cdd:cd04969      13 LAAKGGDviieckpkasPKPTISWSKGT-ELLTNSSRICILPDGS---LKIKNVTKSDEGKYTCFAVNFFGKANSTGSLS 88

                    .
gi 1958765569  9380 V 9380
Cdd:cd04969      89 V 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
17739-17818 2.51e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.18  E-value: 2.51e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17739 EQHIKVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQ-IDVTPVGSkLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVL 17817
Cdd:cd20952       8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDErITTLENGS-LQIKGAEKSDTGEYTCVALNLSGEATWSAVLD 86

                    .
gi 1958765569 17818 V 17818
Cdd:cd20952      87 V 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
1418-1507 2.51e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.18  E-value: 2.51e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1418 VFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHkVVIKEDGtqSLIIVPALPSDSGEWTVVAQNRAG 1497
Cdd:cd20952       1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDER-ITTLENG--SLQIKGAEKSDTGEYTCVALNLSG 77
                            90
                    ....*....|
gi 1958765569  1498 KSTISVTLTV 1507
Cdd:cd20952      78 EATWSAVLDV 87
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7771-7856 2.53e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 45.72  E-value: 2.53e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7771 DTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEAGQDICEALV 7850
Cdd:cd05762      10 DMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNL 89

                    ....*.
gi 1958765569  7851 SVLEPP 7856
Cdd:cd05762      90 TVVDKP 95
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7199-7290 2.56e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 45.56  E-value: 2.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7199 PPKFIKKLDTSKVAKQGESIQLECKIS-GSPEIKVVWFRNDSELHESWKYNMSFVNS-VALLTINEASVEDTGDYICEAH 7276
Cdd:cd20959       1 PPRIIPFAFGEGAAQVGMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRrSSILSIDSLEASHAGNYTCHAR 80
                            90
                    ....*....|....
gi 1958765569  7277 NGVGHASCSTALKV 7290
Cdd:cd20959      81 NSAGSASYTAPLTV 94
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
33079-33163 2.56e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 44.90  E-value: 2.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33079 PRSITVH-EGESARFSCDTDGEPVPTVTWLRGGQVVSTSarhQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGKQEAQ 33157
Cdd:cd05876       1 SSSSLVAlRGQSLVLECIAEGLPTPTVKWLRPSGPLPPD---RVKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSARHA 77

                    ....*.
gi 1958765569 33158 FTLTVQ 33163
Cdd:cd05876      78 YYVTVE 83
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
3208-3288 2.56e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 45.30  E-value: 2.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3208 VTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLI-EAFPEDAAVYTCEAKNDYGVATTSASL 3286
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARERRMHVMPEDDVFFIvDVKIEDTGVYSCTAQNSAGSISANATL 88

                    ..
gi 1958765569  3287 SV 3288
Cdd:cd05763      89 TV 90
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
6354-6435 2.58e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 45.27  E-value: 2.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6354 VFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKI-ASKNFHASIHILNVDSTDIGEYHCKAQNEVG 6432
Cdd:cd05737       3 VLGGLPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLkVEAGRTVYFTINGVSSEDSGKYGLVVKNKYG 82

                    ...
gi 1958765569  6433 SDT 6435
Cdd:cd05737      83 SET 85
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
1806-1879 2.58e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 45.29  E-value: 2.58e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1806 FPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIHY--LDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd05891       7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYasLTIKGVTSEDSGKYSINVKNKYG 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
24548-24623 2.58e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.49  E-value: 2.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24548 VRAGGSARIHIPFKGRPTPEITWSKE----EGEFTD-KVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSG--SKSAFV 24620
Cdd:cd20951      12 VWEKSDAKLRVEVQGKPDPEVKWYKNgvpiDPSSIPgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGeaSSSASV 91

                    ...
gi 1958765569 24621 TVK 24623
Cdd:cd20951      92 VVE 94
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
19813-19895 2.60e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.26  E-value: 2.60e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19813 MKSLLTVKAGTNVCLDATV-FGKPMPTVSWKK-DSTPIKQTEGVKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKS 19890
Cdd:pfam00047     2 APPTVTVLEGDSATLTCSAsTGSPGPDVTWSKeGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81

                    ....*
gi 1958765569 19891 ATIKL 19895
Cdd:pfam00047    82 LSTSL 86
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5042-5131 2.60e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 45.18  E-value: 2.60e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5042 PSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWfKGDKELVSGGSCY--ITKEASESSLELYAVKTTDSGTYTCKVSNV 5119
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFW-QLNGKPVRPDSAHkmLVRENGRHSLIIEPVTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569  5120 AGSVECSANLFV 5131
Cdd:cd05744      80 AGENSFNAELVV 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
4297-4381 2.61e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.18  E-value: 2.61e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4297 RIEPLE--VALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNyiSSLEILRTQVVDCGEYTCKASNEYGSVS 4374
Cdd:cd20952       3 LQGPQNqtVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLEN--GSLQIKGAEKSDTGEYTCVALNLSGEAT 80

                    ....*..
gi 1958765569  4375 CTATLTV 4381
Cdd:cd20952      81 WSAVLDV 87
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
8989-9078 2.64e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 45.15  E-value: 2.64e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENS-AHLTIVKVDKGDSGQYTCYAINEV 9067
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGlCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569  9068 GKDSCTAQLNI 9078
Cdd:cd20975      81 GARQCEARLEV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
16646-16718 2.66e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.63  E-value: 2.66e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 16646 VNIVAKIKGVPFPTLTWFKappkkpdSKEPVVYDTHVNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTAS 16718
Cdd:cd00096       1 VTLTCSASGNPPPTITWYK-------NGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7952-8039 2.66e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 45.14  E-value: 2.66e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7952 PSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNlQMSFVHH---VATLQILQTDQSHVGQYNCSASN 8028
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTD-RISLYQDncgRICLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|.
gi 1958765569  8029 PLGTASSSAKL 8039
Cdd:cd05892      80 EAGVVSCNARL 90
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
31554-31630 2.69e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 45.22  E-value: 2.69e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31554 GEVVSIKIPFSGKPDPVITWQKGQDLI-DNNGHYQVIVTRSFTSLVFpNGVERKDAGFYVVCAKNRFGIDQKTVELDV 31630
Cdd:cd05894      10 GNKLRLDVPISGEPAPTVTWSRGDKAFtATEGRVRVESYKDLSSFVI-EGAEREDEGVYTITVTNPVGEDHASLFVKV 86
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
1807-1879 2.69e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 45.30  E-value: 2.69e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQL---IRKSKRFRVRYDGIHYLdIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd05763       6 PHDITIRAGSTARLECAATGHPTPQIAWQKDGGTdfpAARERRMHVMPEDDVFF-IVDVKIEDTGVYSCTAQNSAG 80
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8071-8130 2.70e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.89  E-value: 2.70e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8071 VTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDS 8130
Cdd:cd05748      16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
2315-2386 2.70e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 45.27  E-value: 2.70e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  2315 PIAILQGLSDQKVCEGDIVQLEVKVSLENVEGV-WMKDGQEVQHSDRVHIVIDKQSHMLLIEDMTKEDAGNYS 2386
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVrWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYS 73
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4667-4746 2.71e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 45.25  E-value: 2.71e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4667 PSFIKTLEPAHIVRGANALLQCEVAGTgPFE-VSWFKDKKQIRSSKKYRLFTQKTFVFLEITSfnSADIGDYECVVANEV 4745
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGY-PISsITWEKDGRRLPLNHRQRVFPNGTLVIENVQR--SSDEGEYTCTARNQQ 77

                    .
gi 1958765569  4746 G 4746
Cdd:cd20958      78 G 78
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
911-990 2.74e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 44.90  E-value: 2.74e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   911 VVEGESVTLECHISGYPSPKVTWYREDYQIESSidfQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAVQ 990
Cdd:cd05876       7 ALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPD---RVKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSARHAYYVTVE 83
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
18905-19097 2.74e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 50.33  E-value: 2.74e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18905 YDRPGRPDPPEVTK----------VSKEEMTVVWNAPEYDggksiTGYYLEKKeKHAVRWVPVNKSaiPERRLKVQNLLP 18974
Cdd:COG4733     525 DDVPPQWPPVNVTTseslsvvaqgTAVTTLTVSWDAPAGA-----VAYEVEWR-RDDGNWVSVPRT--SGTSFEVPGIYA 596
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18975 GhEYQFRVKAENEVGIGEPSLPSRPVVAKDPIEPPGPPTNFKVVDTTkNSITLAWGKPVydgGAPIIGYvvEMRpkiadA 19054
Cdd:COG4733     597 G-DYEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTGLTATGGL-GGITLSWSFPV---DADTLRT--EIR-----Y 664
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....
gi 1958765569 19055 SPDEGWKRCNAAAQLVRM-EFTVTSLDENQEYEFRVCAQNQVGI 19097
Cdd:COG4733     665 STTGDWASATVAQALYPGnTYTLAGLKAGQTYYYRARAVDRSGN 708
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
11825-11889 2.75e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.19  E-value: 2.75e-04
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  11825 RDQHVKPKGTAVFTCHI-AKDTPNIKWFKGYDEiPLEPNDKTEILKEGNHLILKVKNAMPEDIDEY 11889
Cdd:smart00410     2 PSVTVKEGESVTLSCEAsGSPPPEVTWYKQGGK-LLAESGRFSVSRSGSTSTLTISNVTPEDSGTY 66
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5982-6066 2.75e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 2.75e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5982 KAKSVDVTEKdpVTLEC-VVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQ--SVMKQDSGQYTFKVENDFGSS 6058
Cdd:cd05750       7 KSQTVQEGSK--LVLKCeATSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSELQinKAKLEDSGEYTCVVENILGKD 84

                    ....*...
gi 1958765569  6059 SCDAYLRV 6066
Cdd:cd05750      85 TVTGNVTV 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
1047-1127 2.75e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 2.75e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1047 QKLVEGGSVVFECQ-IGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECRLVISMTFADDAGEYTIVIRNKHGETSASA 1125
Cdd:cd05750       9 QTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTG 88

                    ..
gi 1958765569  1126 SL 1127
Cdd:cd05750      89 NV 90
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
1519-1607 2.76e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 45.37  E-value: 2.76e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1519 VEKLKNVNIKEGSRLEMKVRATGN-PNPDIVWLKNSDIIVPHKYPR-IRIEGTKGEAALKIDSTISQDSAWYTATAINKA 1596
Cdd:cd05895       3 LKEMKSQEVAAGSKLVLRCETSSEyPSLRFKWFKNGKEINRKNKPEnIKIQKKKKKSELRINKASLADSGEYMCKVSSKL 82
                            90
                    ....*....|.
gi 1958765569  1597 GRDTTRCKVNI 1607
Cdd:cd05895      83 GNDSASANVTI 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4201-4286 2.76e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 45.18  E-value: 2.76e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4201 ILKPLVDTISEkGDTVHLTSSISN--AKEVNWYFKGDLVPPGAKFQCLKEENA-YTLVIESVKTEDEGEYVCEASNGNGK 4277
Cdd:cd05744       4 LQAPGDLEVQE-GRLCRFDCKVSGlpTPDLFWQLNGKPVRPDSAHKMLVRENGrHSLIIEPVTKRDAGIYTCIARNRAGE 82

                    ....*....
gi 1958765569  4278 AMTSAKLTV 4286
Cdd:cd05744      83 NSFNAELVV 91
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
1680-1745 2.76e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 45.13  E-value: 2.76e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1680 AHFECRLTpiGDPTMVVEWLHDGKPLEAANRLRLINEFGYcSLDYEAAYSRDSGVITCRATNKYGT 1745
Cdd:cd04978      17 GELICEAE--GNPQPTITWRLNGVPIEPAPEDMRRTVDGR-TLIFSNLQPNDTAVYQCNASNVHGY 79
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
20888-20974 2.77e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 45.14  E-value: 2.77e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20888 PTIVLDPTIKDGLTVKAGDsiVLSAISILGKPLPKSSWSKAGKDIRPSdiAQITSTPTSSmLTVKYATRKDAGEYTITAT 20967
Cdd:cd04969       1 PDFELNPVKKKILAAKGGD--VIIECKPKASPKPTISWSKGTELLTNS--SRICILPDGS-LKIKNVTKSDEGKYTCFAV 75

                    ....*..
gi 1958765569 20968 NPFGTKE 20974
Cdd:cd04969      76 NFFGKAN 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2411-2490 2.79e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 45.18  E-value: 2.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2411 LKDVNVIEGTKAVLECKVS---VPDVTsvkWYLNDEQIKPDDRVQSIVKGT-KQRLVINRTHASDEGPYKLMV----GRV 2482
Cdd:cd05744       7 PGDLEVQEGRLCRFDCKVSglpTPDLF---WQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIArnraGEN 83

                    ....*...
gi 1958765569  2483 ETSCNLSV 2490
Cdd:cd05744      84 SFNAELVV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
18737-18795 2.79e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.63  E-value: 2.79e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 18737 VRGKPFPEVAWTKDKdaTDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAG 18795
Cdd:cd00096       7 ASGNPPPTITWYKNG--KPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7483-7570 2.79e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.10  E-value: 2.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7483 IVEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGREL--SSGSRHHITFVR-NLASLKIPSAEMNDKGLYSFEVENSV 7559
Cdd:cd20951       3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKIESEyGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|.
gi 1958765569  7560 GKSSCTVSVHV 7570
Cdd:cd20951      83 GEASSSASVVV 93
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
13511-13598 2.80e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 45.31  E-value: 2.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13511 PP--KIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLstktvDTTAEQTSFR-------ILEAKKEDKGRYKI 13581
Cdd:cd05730       1 PPtiRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPI-----ESGEEKYSFNedgsemtILDVDKLDEAEYTC 75
                            90
                    ....*....|....*..
gi 1958765569 13582 VLQNKHGKAEGFINLQV 13598
Cdd:cd05730      76 IAENKAGEQEAEIHLKV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3044-3103 2.81e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.89  E-value: 2.81e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3044 PDITVQWMKDGQELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVAGGNMSTANLFVE 3103
Cdd:cd05748      20 PTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
6649-6727 2.83e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 45.33  E-value: 2.83e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6649 LGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTVQE 6727
Cdd:cd05736      14 PGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVED 92
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
4381-4468 2.83e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 45.33  E-value: 2.83e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4381 VTEAYPPTFLSRPkslttfvGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCK 4460
Cdd:cd05736       2 VIRVYPEFQAKEP-------GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCI 74

                    ....*...
gi 1958765569  4461 ASNKFGAD 4468
Cdd:cd05736      75 AKNEGGVD 82
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
3207-3288 2.83e-04

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 45.23  E-value: 2.83e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3207 PVTVQSGKPARFCAVIAGRPQPKISWYK----EEQLLSTGFKCK----FLHDGQeytLLLIEAFPEDAAVYTCEAKNDYG 3278
Cdd:cd05765       9 HQTVKVGETASFHCDVTGRPQPEITWEKqvpgKENLIMRPNHVRgnvvVTNIGQ---LVIYNAQPQDAGLYTCTARNSGG 85
                            90
                    ....*....|
gi 1958765569  3279 VATTSASLSV 3288
Cdd:cd05765      86 LLRANFPLSV 95
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
16638-16725 2.84e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 2.84e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16638 MEVEEGTDVNIVAKIKGVPFPTLTWFKappkkpDSKEPVVYDThvNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNL-GT 16716
Cdd:cd20970      12 VTAREGENATFMCRAEGSPEPEISWTR------NGNLIIEFNT--RYIVRENGTTLTIRNIRRSDMGIYLCIASNGVpGS 83

                    ....*....
gi 1958765569 16717 ASKEMRLNV 16725
Cdd:cd20970      84 VEKRITLQV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
27392-27474 2.86e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 2.86e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  27392 EVVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVC-VENSTDLASILIKDANRLNSGSYELKLRNAMGSASATI 27470
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFsVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                     ....
gi 1958765569  27471 RVQI 27474
Cdd:smart00410    82 TLTV 85
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
31049-31132 2.86e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 2.86e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31049 KEMADVTTKLGEAAQLSCQIVGR-PLPDIKWYRFGKELVQSR--KYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGE 31125
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEATSEnPSPRYRWFKDGKELNRKRpkNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGK 83

                    ....*..
gi 1958765569 31126 VETSSKL 31132
Cdd:cd05750      84 DTVTGNV 90
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
14217-14292 2.86e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 45.24  E-value: 2.86e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 14217 GTKIELPATVTGKPEPKITWTKADTLLRPDQriTIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVNV 14292
Cdd:cd05856      19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPE--IGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5510-5604 2.87e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 45.33  E-value: 2.87e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5510 PPSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKA 5589
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*
gi 1958765569  5590 GHSQCSGHLTVKEPP 5604
Cdd:cd05762      81 GSRQAQVNLTVVDKP 95
Titin_Z pfam09042
Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like ...
553-595 2.89e-04

Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. This interaction is essential for sarcomere assembly.


Pssm-ID: 462662  Cd Length: 43  Bit Score: 43.73  E-value: 2.89e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958765569   553 QETITKETRKTVVPKVIVATPKIKEQDVVSRSREAITTKRDQV 595
Cdd:pfam09042     1 QEKVREEDEKTAVSTVVVAVDKAKVLEPVSKSEEEIAAEQEQE 43
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7116-7197 2.89e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.89  E-value: 2.89e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7116 IDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDmcSAQLS 7195
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEK--SATIN 79

                    ..
gi 1958765569  7196 VK 7197
Cdd:cd05748      80 VK 81
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
21600-21658 2.90e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.63  E-value: 2.90e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 21600 PVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGE 21658
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
5148-5216 2.92e-04

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 45.15  E-value: 2.92e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5148 KKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAV-LRLTDVAIE-DSGEYMCEAQNEAGS 5216
Cdd:cd20971      14 RYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYhQLIIASVTDdDATVYQVRATNQGGS 84
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
12703-12781 2.96e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 45.21  E-value: 2.96e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12703 VKPRVIgllrPLKDVTVTAGETATFDCELSYEDIP-VEWYLKGKKLEPNDK-----VVTRSEGRVHTLTLRDVKLEDAGE 12776
Cdd:cd05732       1 VQPKIT----YLENQTAVELEQITLTCEAEGDPIPeITWRRATRGISFEEGdldgrIVVRGHARVSSLTLKDVQLTDAGR 76

                    ....*
gi 1958765569 12777 VQLTA 12781
Cdd:cd05732      77 YDCEA 81
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
5066-5131 2.96e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 45.14  E-value: 2.96e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5066 QGSTPLTIRWFKGDKELVSGGSCYITKEASessLELYAVKTTDSGTYTCKVSNVAGSVECSANLFV 5131
Cdd:cd04969      27 KASPKPTISWSKGTELLTNSSRICILPDGS---LKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
8717-8789 2.96e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 45.14  E-value: 2.96e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8717 KGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITtteKSAILEILSSTVEDSGQYNCYIENASGKDSCSA 8789
Cdd:cd04969      16 KGGDVIIECKPKASPKPTISWSKGTELLTNSSRICIL---PDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTG 85
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
33078-33157 2.98e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 45.07  E-value: 2.98e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33078 KPRSITVHEGESARFSCDTDGEPVPTVTWL-RGGQVVSTSA--RHQVTTAkykSTFEISSVQASDEGNYSVVVEN--TDG 33152
Cdd:cd20969       8 KAQQVFVDEGHTVQFVCRADGDPPPAILWLsPRKHLVSAKSngRLTVFPD---GTLEVRYAQVQDNGTYLCIAANagGND 84

                    ....*
gi 1958765569 33153 KQEAQ 33157
Cdd:cd20969      85 SMPAH 89
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
18428-18510 2.98e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 45.07  E-value: 2.98e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18428 DVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAI 18507
Cdd:cd20969      10 QQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAH 89

                    ...
gi 1958765569 18508 VNV 18510
Cdd:cd20969      90 LHV 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
24548-24631 2.99e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 45.33  E-value: 2.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24548 VRAGGSARIHIPFKGRPTPEITWSK-----EEGEFtdkVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTV 24622
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKfrkqiQEGEG---IKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNL 89

                    ....*....
gi 1958765569 24623 KVLDTPGPP 24631
Cdd:cd05762      90 TVVDKPDPP 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
10940-11457 2.99e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 2.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10940 PPkrPEAPPAKVPEASKEVVPEKKvsvaPKKKPEAPAVKVPEAPKKVVPEK---KVPVAAPKKPEAPAAEVPEVPKAAVP 11016
Cdd:PHA03247   2551 PP--PPLPPAAPPAAPDRSVPPPR----PAPRPSEPAVTSRARRPDAPPQSarpRAPVDDRGDPRGPAPPSPLPPDTHAP 2624
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11017 QKKIPEavppkpespppevyeepaeeivpeeppeevveepepapppkvtvpPKKPVPEKKAPPAVVKKPEPPPAKAPEVP 11096
Cdd:PHA03247   2625 DPPPPS---------------------------------------------PSPAANEPDPHPPPTVPPPERPRDDPAPG 2659
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11097 KEAPPEKKVPSVVPKKPEAPPA--KVPEVPKEVVPEKKVAVPKkpevPPAKVPEVPKKPVVEEKPVieekPAIPVAEKVE 11174
Cdd:PHA03247   2660 RVSRPRRARRLGRAAQASSPPQrpRRRAARPTVGSLTSLADPP----PPPPTPEPAPHALVSATPL----PPGPAAARQA 2731
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11175 SPPTEVYEEPEEVAAqeeepapvveeeeYEAPPPPAPEIPVPQVPEEPKKVVPEKkypvikkpeppppkvpEVSKKPAPM 11254
Cdd:PHA03247   2732 SPALPAAPAPPAVPA-------------GPATPGGPARPARPPTTAGPPAPAPPA----------------APAAGPPRR 2782
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11255 KKVPVVKKPEPPEAEvpevpkklAPVKKEPVPVtkkPEVLPEKVPEAPKKITPekresapvpeepeappapVEEIPEETi 11334
Cdd:PHA03247   2783 LTRPAVASLSESRES--------LPSPWDPADP---PAAVLAPAAALPPAASP------------------AGPLPPPT- 2832
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11335 yeeKATITIGRKETPPVEEREierfiqPEEPGMEPQpeeTPVQEPEPEKKVIEKPKLKPRPPIR-----APSPPKEDVKE 11409
Cdd:PHA03247   2833 ---SAQPTAPPPPPGPPPPSL------PLGGSVAPG---GDVRRRPPSRSPAAKPAAPARPPVRrlarpAVSRSTESFAL 2900
                           490       500       510       520
                    ....*....|....*....|....*....|....*....|....*...
gi 1958765569 11410 KIFQLKAVSKKKVPEKPEVVEKVEPTPLKVPTAEKKVRkllPEPKPQP 11457
Cdd:PHA03247   2901 PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR---PQPPLAP 2945
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
892-987 3.00e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.83  E-value: 3.00e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   892 PAEVPVTPPTLvsglknvTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSgiaRLMIREAFAEDSGRFT 971
Cdd:cd20957       1 PLSATIDPPVQ-------TVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQ 70
                            90
                    ....*....|....*.
gi 1958765569   972 CSAVNEAGTVSTSCYL 987
Cdd:cd20957      71 CFVRNDGDSAQATAEL 86
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
908-982 3.01e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 44.71  E-value: 3.01e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569   908 NVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSidfQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVS 982
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKG---RTKFENFNKTLKIENVSEADSGEYQCTASNTMGSAR 75
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
1419-1507 3.02e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 45.01  E-value: 3.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1419 FVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVND--YTHKVVIKEDGtqsLIIVPALPSDSGEWTVVAQNRA 1496
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASvaDMSKYRILADG---LLINKVTQDDTGEYTCRAYQVN 78
                            90
                    ....*....|.
gi 1958765569  1497 GKSTISVTLTV 1507
Cdd:cd20949      79 SIASDMQERTV 89
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
26699-26786 3.04e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 45.29  E-value: 3.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26699 DVDSEMRKTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRT---SLTIENANRNDSGKYTLTIQNVL 26775
Cdd:cd05729       5 DTEKMEEREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEkgwSLIIERAIPRDKGKYTCIVENEY 84
                            90
                    ....*....|.
gi 1958765569 26776 SAASMTFVVKV 26786
Cdd:cd05729      85 GSINHTYDVDV 95
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
8989-9074 3.04e-04

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 45.15  E-value: 3.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAK-------DNREIRSGGNYQISYLEnsahLTIVKVdKGDSGQYTC 9061
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRqgkeiiaDGLKYRIQEFKGGYHQL----IIASVT-DDDATVYQV 76
                            90
                    ....*....|...
gi 1958765569  9062 YAINEVGKDSCTA 9074
Cdd:cd20971      77 RATNQGGSVSGTA 89
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
17745-17816 3.04e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 44.71  E-value: 3.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 17745 GDTLRLSAIIKGVPFPKVTWKKEDREAPtKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGS--KTVSVKV 17816
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIKLGGELP-KGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSarHTISVTV 82
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
22682-22740 3.05e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.08  E-value: 3.05e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22682 PFIGRPTPTVTWHKDDVPLK-QTTRVNAESTENnslLTIKEACREDVGHYTVKLTNSAGE 22740
Cdd:cd05724      21 PPRGHPEPTVSWRKDGQPLNlDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGE 77
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
2846-2926 3.06e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 3.06e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2846 KTMRNIEVPETKAASFECEVSHFNvPSM---WLKNGVEI--EMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVC----G 2916
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEATSEN-PSPryrWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVenilG 82
                            90
                    ....*....|
gi 1958765569  2917 NDQVSATLTV 2926
Cdd:cd05750      83 KDTVTGNVTV 92
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
28485-28563 3.06e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 45.33  E-value: 3.06e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 28485 GDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEITVKVQDT 28563
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVEDS 93
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
3305-3391 3.08e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 45.04  E-value: 3.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3305 PAIVTPLQDAVTSEGRPARFQCQVSGTDL-KVSWYcRDKK-IKPSRF--FRMTQFEDTYQLEIAEAFPEDEGTYAFVANN 3380
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVpEVSWF-RDGQvISTSTLpgVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|.
gi 1958765569  3381 AVGQVSSTATL 3391
Cdd:cd20974      80 GSGQATSTAEL 90
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
23063-23145 3.08e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 45.29  E-value: 3.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23063 DTVVVQAGESFKIDADIYGKPIPTTQWVKGDQ--ELSSTARLEIKTTDFAtSLSVKDAVRVDSGNYILKAKNVAGEKSVT 23140
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQdiELSEHYSVKLEQGKYA-SLTIKGVTSEDSGKYSINVKNKYGGETVD 87

                    ....*
gi 1958765569 23141 VNVKV 23145
Cdd:cd05891      88 VTVSV 92
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4962-5029 3.08e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 45.18  E-value: 3.08e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4962 VGGACRLDCKIA-GSLPMRVSWFKDGKEIAASDRYQIAFVEG-TASLEISRVDMNDAGNFTCRATNSVGS 5029
Cdd:cd20959      16 VGMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRrSSILSIDSLEASHAGNYTCHARNSAGS 85
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
1801-1891 3.09e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 45.33  E-value: 3.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLI--RKSKRFRVRYDGIHyLDIVDCKSYDTGEVKVTAENPE 1878
Cdd:cd05736       1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDInpKLSKQLTLIANGSE-LHISNVRYEDTGAYTCIAKNEG 79
                            90
                    ....*....|...
gi 1958765569  1879 GVTEHKVKLEIQQ 1891
Cdd:cd05736      80 GVDEDISSLFVED 92
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7965-8041 3.09e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.83  E-value: 3.09e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  7965 LGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSfvhHVATLQILQTDQSHVGQYNCSASNPLGTASSSAKLIL 8041
Cdd:cd20957      15 FGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQIL---SEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAELKL 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
17048-17113 3.09e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.83  E-value: 3.09e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 17048 VHAGGVIRIIAYVSGKPPPTVTWNMNERALPQEATIETTAiSSSMVIKNCQRSHQGVYSLLAKNEG 17113
Cdd:cd20957      13 VDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILS-EDVLVIPSVKREDKGMYQCFVRNDG 77
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
1525-1605 3.10e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.89  E-value: 3.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1525 VNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHkyPRIRIEGTKGEAALKIDSTISQDSAWYTATAINKAGRDTTRCK 1604
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKET--GRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                    .
gi 1958765569  1605 V 1605
Cdd:cd05748      80 V 80
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
17727-17825 3.10e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 45.33  E-value: 3.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17727 PPELIldaNMAREQHIKVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDV--TPVGSKLEIRNAAHEDGGIYSLTVE 17804
Cdd:cd05762       1 PPQII---QFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIenTENSSKLTITEGQQEHCGCYTLEVE 77
                            90       100
                    ....*....|....*....|.
gi 1958765569 17805 NPAGSKTVSVKVLVLDKPGPP 17825
Cdd:cd05762      78 NKLGSRQAQVNLTVVDKPDPP 98
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
21786-22007 3.11e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.94  E-value: 3.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21786 SMTISWheplsDGGSPILGYHIERKeRNGILWQTVskALVPGNIFKSTGLTDGIaYEFRVIAENMAG-KSKPSKPSEPTF 21864
Cdd:COG4733     553 TLTVSW-----DAPAGAVAYEVEWR-RDDGNWVSV--PRTSGTSFEVPGIYAGD-YEVRVRAINALGvSSAWAASSETTV 623
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21865 ALDPIDPPgkpVPLNIT----RHTVALKWAKPEYTGgfkITSYVVekRDLPNGRWLKANFSNIL--ENEFTVSGLTEDAA 21938
Cdd:COG4733     624 TGKTAPPP---APTGLTatggLGGITLSWSFPVDAD---TLRTEI--RYSTTGDWASATVAQALypGNTYTLAGLKAGQT 695
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 21939 YEFRVIAKNAAGAISPPSEpsdAITCRDDLEAPRIMVDVKFKDTITLKAGEAFKLEADVSGRPPPTMEW 22007
Cdd:COG4733     696 YYYRARAVDRSGNVSAWWV---SGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTD 761
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5142-5225 3.13e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 44.69  E-value: 3.13e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5142 EPS-QLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHkmsfVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCT 5220
Cdd:cd05725       3 RPQnQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYE----ILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEAS 78

                    ....*
gi 1958765569  5221 SIVIV 5225
Cdd:cd05725      79 ATLTV 83
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
27392-27474 3.14e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 45.29  E-value: 3.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27392 EVVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNA--LVCVEnSTDLASILIKDANRLNSGSYELKLRNAMGSASAT 27469
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEhySVKLE-QGKYASLTIKGVTSEDSGKYSINVKNKYGGETVD 87

                    ....*
gi 1958765569 27470 IRVQI 27474
Cdd:cd05891      88 VTVSV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5984-6059 3.16e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.88  E-value: 3.16e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5984 KSVDVTEKDPVTLEC-VVAGTPELKVKWLKDGKQIVPSRYFSMSF-ENNVASFRIQSVMKQDSGQYTFKVENDFGSSS 6059
Cdd:pfam00047     4 PTVTVLEGDSATLTCsASTGSPGPDVTWSKEGGTLIESLKVKHDNgRTTQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
21982-22063 3.16e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 44.71  E-value: 3.16e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21982 TITLKAGEAFKLEADVSGRPPPTMEWAKDGKEL-EGTGKLEikiaDFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFN 22060
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELpKGRTKFE----NFNKTLKIENVSEADSGEYQCTASNTMGSARHTIS 79

                    ...
gi 1958765569 22061 VKV 22063
Cdd:cd05731      80 VTV 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
23747-23829 3.17e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 45.18  E-value: 3.17e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23747 AFSSYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVI-DSLDLTTLSIKETHKDDGGHYGITVANVVGQKTA 23825
Cdd:cd05744       6 APGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLvRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSF 85

                    ....
gi 1958765569 23826 AIEI 23829
Cdd:cd05744      86 NAEL 89
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
31439-31531 3.18e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 44.93  E-value: 3.18e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31439 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEFKGgyhQLIIASVTDDDATVYQVRATN 31518
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVG---ELHIQDVLPEDHGTYTCLAKN 77
                            90
                    ....*....|...
gi 1958765569 31519 QGGSVSGTASLEV 31531
Cdd:cd20976      78 AAGQVSCSAWVTV 90
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6073-6162 3.19e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 45.09  E-value: 3.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTV-SLEVSNLELEDTANYTCKVSNVA 6151
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVhSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  6152 GDNACSGILTV 6162
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
5149-5225 3.20e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.90  E-value: 3.20e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5149 KGDATQLVCKVTGTPPIKITWFANDRELrESSKHKMSFVESTAVLRLT--DVAIEDSGEYMCEAQNEAGSDHCTSIVIV 5225
Cdd:cd05891      15 EGKTLNLTCTVFGNPDPEVIWFKNDQDI-ELSEHYSVKLEQGKYASLTikGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6729-6819 3.20e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.10  E-value: 3.20e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6729 PSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGAREL---VKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSN 6805
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  6806 NAGQASCTTRLFVK 6819
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
4389-4476 3.21e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.79  E-value: 3.21e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4389 FLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALsPSPDCRITDADNKhSLELSNLTVQDRGVYSCKASNKFGAD 4468
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPL-LGKDERITTLENG-SLQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569  4469 ICQAELTI 4476
Cdd:cd20952      80 TWSAVLDV 87
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
6539-6629 3.21e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 45.08  E-value: 3.21e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6539 PAVIVEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQKhKFSFYNkiSSLKILSVEKEDAGTYTFQVQNNV 6618
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPME-RATVED--GTLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  6619 GKSSCTAVVDV 6629
Cdd:cd20978      78 GDIYTETLLHV 88
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5233-5318 3.21e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 3.21e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5233 KEFKSIEVLKEYDVMLLAE-VAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVS--LQILKFVASDAGEYQCRVTNEVGS 5309
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNseLQINKAKLEDSGEYTCVVENILGK 83

                    ....*....
gi 1958765569  5310 STCSARVTL 5318
Cdd:cd05750      84 DTVTGNVTV 92
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
29972-30046 3.22e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 45.29  E-value: 3.22e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 29972 AGASLRLMVSVSGRPSPVITWSKKGIDLANRAII---DNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLVKV 30046
Cdd:cd05729      18 AANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIggtKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7956-8040 3.23e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 44.69  E-value: 3.23e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7956 RKLKDVHETLGFPVAFECRINGSEPLQVSWYKDgqllkdDSNLQMSFVH--HVATLQILQTDQSHVGQYNCSASNPLGTA 8033
Cdd:cd05725       2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKE------DGELPKGRYEilDDHSLKIRKVTAGDMGSYTCVAENMVGKI 75

                    ....*..
gi 1958765569  8034 SSSAKLI 8040
Cdd:cd05725      76 EASATLT 82
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
9188-9271 3.27e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 44.69  E-value: 3.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9188 LTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTavlelkdtakaDSGDYVCKASNVAGSDTSKc 9267
Cdd:pfam13895     6 PSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTLSVSAE-----------DSGTYTCVARNGRGGKVSN- 73

                    ....
gi 1958765569  9268 KVTI 9271
Cdd:pfam13895    74 PVEL 77
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
112-188 3.27e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 44.83  E-value: 3.27e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   112 SMTVRQGSQARLQVRVTGIPTPVVKFYR-DGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATST 188
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRgDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS 81
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
6073-6152 3.28e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 45.29  E-value: 3.28e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6073 PSFTKKLTKMDKVL----GSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENT-VSLEVSNLELEDTANYTCKV 6147
Cdd:cd05729       1 PRFTDTEKMEEREHalpaANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKgWSLIIERAIPRDKGKYTCIV 80

                    ....*
gi 1958765569  6148 SNVAG 6152
Cdd:cd05729      81 ENEYG 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8054-8124 3.29e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.88  E-value: 3.29e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8054 PVSVDLALGESGSFKCHV-TGTAPIKITWAK-DNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASN 8124
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSKeGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNN 75
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
12883-12960 3.31e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.48  E-value: 3.31e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12883 PPHVEFlrPLTDLQVKEKETARFECEISKENV-KVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEVR 12960
Cdd:pfam13927     1 KPVITV--SPSSVTVREGETVTLTCEATGSPPpTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2859-2912 3.33e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.24  E-value: 3.33e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  2859 ASFECEVSHFNVPSM-WLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYT 2912
Cdd:cd00096       1 VTLTCSASGNPPPTItWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYT 55
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
20301-20491 3.33e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.94  E-value: 3.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20301 PPVNVTVKE--------ISKDSAYITWDPPiidggSPIINYVVEKRdAERKSWSTVTTEcPKTSFRVSNLEEGkSYFFRV 20372
Cdd:COG4733     532 PPVNVTTSEslsvvaqgTAVTTLTVSWDAP-----AGAVAYEVEWR-RDDGNWVSVPRT-SGTSFEVPGIYAG-DYEVRV 603
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20373 FAENEYGIGDPGET--RDAVKASETPGPvvdlKVLAVTKSS----CTIGWKKPRsdgGSRITGYVVdFLTEENKWQRVMK 20446
Cdd:COG4733     604 RAINALGVSSAWAAssETTVTGKTAPPP----APTGLTATGglggITLSWSFPV---DADTLRTEI-RYSTTGDWASATV 675
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 1958765569 20447 SLSL----QYSTKDLKEGKEYTFRVSAENENGEGTPSEIMVVAKDDVVA 20491
Cdd:COG4733     676 AQALypgnTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAG 724
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
29968-30043 3.33e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.92  E-value: 3.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29968 VIIRAGASLRLMVSVSGRPSPVITWSKK-GIDLA---NRAIIDNTESYSLLIVDkVNRYDAGKYTIEAENQSGKKSA--- 30040
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDgGTDFPaarERRMHVMPEDDVFFIVD-VKIEDTGVYSCTAQNSAGSISAnat 87

                    ....
gi 1958765569 30041 -TVL 30043
Cdd:cd05763      88 lTVL 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
8254-8324 3.34e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 3.34e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  8254 LECELQG-TPPFQVSWYKDKRELRSGK--KYKIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDTCVGSVTL 8324
Cdd:cd05750      19 LKCEATSeNPSPRYRWFKDGKELNRKRpkNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
7487-7560 3.35e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 45.23  E-value: 3.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7487 PEPM-----TVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHITFVRNLA-SLKIPSAEMNDKGLYSFEVENSVG 7560
Cdd:cd05857       6 PEKMekklhAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHwSLIMESVVPSDKGNYTCVVENEYG 85
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
7308-7381 3.38e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 44.98  E-value: 3.38e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7308 GSDVILQCE-ISGTPPFEVVWVKDRKQVRSSKK---FKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCACTV 7381
Cdd:cd05895      14 GSKLVLRCEtSSEYPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSASANV 91
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
4951-5038 3.43e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.92  E-value: 3.43e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4951 FTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKD-GKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGS 5029
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDgGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81

                    ....*....
gi 1958765569  5030 KDSRGALIV 5038
Cdd:cd05763      82 ISANATLTV 90
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4389-4478 3.43e-04

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 45.33  E-value: 3.43e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4389 FLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTAL------SPSPDCRITdADNKHSLELSNLTVQDRGVYSCKAS 4462
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNllfpyqPPQPSSRFS-VSPTGDLTITNVQRSDVGYYICQAL 80
                            90
                    ....*....|....*.
gi 1958765569  4463 NKFGADICQAELTIID 4478
Cdd:cd05726      81 NVAGSILAKAQLEVTD 96
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
3602-3667 3.44e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.79  E-value: 3.44e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  3602 GEPAPTVLWFKEDMPLYT-NVCYTIIHNpdgsGTFIVNDPQRGDSGLYICKAENLWGTSTCTAELLV 3667
Cdd:cd20952      25 GEPVPTISWLKDGVPLLGkDERITTLEN----GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
15613-15692 3.44e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.48  E-value: 3.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15613 PPTVeldVSVKGGIQIMAGKTLRIPAVVTGRPVPTKVWTIEEGELDKERV-VIENVGTKSELIIKNALRKDHGRYVITAT 15691
Cdd:pfam13927     1 KPVI---TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTrSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 15692 N 15692
Cdd:pfam13927    78 N 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
9518-9578 3.44e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 3.44e-04
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   9518 NYPEIKLSWYK-GTEKLEPSNKYEITINGDRHTLRVRNCQLKDQGNYRlvC------GPHIASAKLTV 9578
Cdd:smart00410    20 GSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYT--CaatnssGSASSGTTLTV 85
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
32223-32293 3.44e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 3.44e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 32223 TITVHPEPRVTWYKSGQKIKPgDDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVARNKHGEDSCKAKLTV 32293
Cdd:cd05750      23 ATSENPSPRYRWFKDGKELNR-KRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4852-4935 3.45e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.88  E-value: 3.45e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4852 PAKIIERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEV 4931
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....
gi 1958765569  4932 GSSS 4935
Cdd:cd20972      81 GSDT 84
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
15918-16006 3.46e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.90  E-value: 3.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15918 DTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEkPTDALNITKEevsrSEAKTELSIPKAVREDKGTYTITASNRLGS 15997
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIE-LSEHYSVKLE----QGKYASLTIKGVTSEDSGKYSINVKNKYGG 83

                    ....*....
gi 1958765569 15998 VFRNVHVEV 16006
Cdd:cd05891      84 ETVDVTVSV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
7762-7843 3.46e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.04  E-value: 3.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7762 PATFVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEA 7841
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  7842 GQ 7843
Cdd:cd05747      83 GK 84
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
4393-4468 3.49e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.90  E-value: 3.49e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4393 PKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKH-SLELSNLTVQDRGVYSCKASNKFGAD 4468
Cdd:cd05891       8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYaSLTIKGVTSEDSGKYSINVKNKYGGE 84
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
4298-4381 3.52e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 44.90  E-value: 3.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4298 IEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSnyisSLEILRTQVVDCGEYTCKASNEYGSVSCTA 4377
Cdd:cd05728       6 ISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAG----DLRITKLSLSDSGMYQCVAENKHGTIYASA 81

                    ....
gi 1958765569  4378 TLTV 4381
Cdd:cd05728      82 ELAV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
9294-9378 3.52e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.88  E-value: 3.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9294 SEPQSIRVVEKTTATFIAKV-GGDPIPNVKWTKGKwRQLNQGGRILIHQKGDESK-LEIRDTTKTDSGLYRCVAFNKHGE 9371
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEG-GTLIESLKVKHDNGRTTQSsLLISNVTKEDAGTYTCVVNNPGGS 79

                    ....*..
gi 1958765569  9372 IESNVNL 9378
Cdd:pfam00047    80 ATLSTSL 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
21982-22063 3.54e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 3.54e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  21982 TITLKAGEAFKLEADVSGRPPPTMEWAKDG-KELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFN 22060
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                     ...
gi 1958765569  22061 VKV 22063
Cdd:smart00410    83 LTV 85
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
8714-8786 3.56e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 44.89  E-value: 3.56e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  8714 SIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTE-KSAILEILSSTVEDSGQYNCYIENASGKDS 8786
Cdd:cd05737      12 TIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGSET 85
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
19822-19887 3.58e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 44.85  E-value: 3.58e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 19822 GTNVCLDATVFGKPMPTVSWKK-DSTPIKQTEgvkmaMKRNLCTLELFSVNRKDSGDYTITAENSSG 19887
Cdd:cd04968      16 GQTVTLECFALGNPVPQIKWRKvDGSPSSQWE-----ITTSEPVLEIPNVQFEDEGTYECEAENSRG 77
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
1041-1124 3.58e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 44.85  E-value: 3.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1041 ISKPVvqklveGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTgecrLVISMTFADDAGEYTIVIRNKHGE 1120
Cdd:cd05856      14 IARPV------GSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWT----LSLKNLKPEDSGKYTCHVSNRAGE 83

                    ....
gi 1958765569  1121 TSAS 1124
Cdd:cd05856      84 INAT 87
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7966-8041 3.59e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 44.54  E-value: 3.59e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  7966 GFPVAFECRINGSEPLQVSWYKDG-QLLKDDSNLQMSfvhhVATLQILQTDQSHVGQYNCSASNPLGTASSSAKLIL 8041
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGsQLSVDRRHLVLS----SGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
23469-23542 3.60e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 44.52  E-value: 3.60e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 23469 GGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSSFTsLVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRV 23542
Cdd:cd05876      10 GQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNKT-LQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
32904-32975 3.61e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 44.69  E-value: 3.61e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 32904 RFILNVQSK--PTAEVKWYHNGVELQESS-KIHYTNTsgvlTLEILDCQTEDSGTYRAVCTNYKGEASDYATLDV 32975
Cdd:cd20978      18 DVTLPCQVTgvPQPKITWLHNGKPLQGPMeRATVEDG----TLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
5893-5973 3.64e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.79  E-value: 3.64e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5893 VTTVLKSSATfqstvaGSPPISITWLKDDqILEENDNVHISFEDSvATLQVRSVDNGHSGRYTCQAKNESGVERCYAFLL 5972
Cdd:cd20952      15 GTVVLNCQAT------GEPVPTISWLKDG-VPLLGKDERITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLD 86

                    .
gi 1958765569  5973 V 5973
Cdd:cd20952      87 V 87
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
18429-18506 3.65e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.83  E-value: 3.65e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 18429 VITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDlPRveLQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd20957      10 VQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSE-DV--LVIPSVKREDKGMYQCFVRNDGDSAQATA 84
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
914-989 3.66e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 44.51  E-value: 3.66e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569   914 GESVTLECHISGYPSPKVTWYREDYQIESSIDFQItfQSGiaRLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAV 989
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEV--EAG--DLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
28481-28560 3.66e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 44.69  E-value: 3.66e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28481 VIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMnmeiTDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEITVKV 28560
Cdd:cd05725       8 VVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGR----YEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6188-6255 3.67e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 44.79  E-value: 3.67e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  6188 VLKGTPPFKIKWLKDDVELVSgpkcFIGLEGS-----TSFLNLYSVDASKTGQYTCQVTNDVGSDSCTTMLLV 6255
Cdd:cd20959      26 VPGGDLPLNIRWTLDGQPISD----DLGITVSrlgrrSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
7215-7290 3.73e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 44.51  E-value: 3.73e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7215 GESIQLECKISGSPEIKVVWFRNDSELHESWKYNMsfvnSVALLTINEASVEDTGDYICEAHNGVGHASCSTALKV 7290
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEV----EAGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
33074-33152 3.73e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 44.93  E-value: 3.73e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 33074 RILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAkykSTFEISSVQASDEGNYSVVVENTDG 33152
Cdd:cd20968       1 KITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLES---GSLRIHNVQKEDAGQYRCVAKNSLG 76
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
31439-31531 3.73e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 3.73e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31439 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIiADGLKYRVQEFKGGYHQLI----IASVTDDDATVYQV 31514
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPI-PESPRFRVGDYVTSDGDVVsyvnISSVRVEDGGEYTC 79
                            90
                    ....*....|....*..
gi 1958765569 31515 RATNQGGSVSGTASLEV 31531
Cdd:cd20956      80 TATNDVGSVSHSARINV 96
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
18019-18119 3.74e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.94  E-value: 3.74e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18019 PPSVeldVKLIEGLVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVS 18098
Cdd:cd05762       1 PPQI---IQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVE 77
                            90       100
                    ....*....|....*....|.
gi 1958765569 18099 NAAGTKTVAVHLTVLDVPGPP 18119
Cdd:cd05762      78 NKLGSRQAQVNLTVVDKPDPP 98
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
5135-5221 3.74e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 44.76  E-value: 3.74e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5135 ATFTEKLEPSQLLKkGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRL--TDVAIEDSGEYMCEAQN 5212
Cdd:cd05892       1 PMFIQKPQNKKVLE-GDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLliQNANKKDAGWYTVSAVN 79

                    ....*....
gi 1958765569  5213 EAGSDHCTS 5221
Cdd:cd05892      80 EAGVVSCNA 88
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
17745-17810 3.78e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.04  E-value: 3.78e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 17745 GDTLRLSAIIKGVPFPKVTWKKEDREAPTKA--QIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSK 17810
Cdd:cd05747      18 GESARFSCDVDGEPAPTVTWMREGQIIVSSQrhQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQ 85
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
107-193 3.84e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 3.84e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   107 SQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQS-SLDFQISQEGDLysLLIAEAYPEDSGTYSVNATNSVGRA 185
Cdd:cd20970       6 PQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEfNTRYIVRENGTT--LTIRNIRRSDMGIYLCIASNGVPGS 83

                    ....*...
gi 1958765569   186 TSTADLLV 193
Cdd:cd20970      84 VEKRITLQ 91
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
9191-9263 3.85e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 44.82  E-value: 3.85e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9191 VTASEGDFLQLSCHVQGsEPI-RIQWLRAGREIKPSD-----RCSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSD 9263
Cdd:cd05732      11 QTAVELEQITLTCEAEG-DPIpEITWRRATRGISFEEgdldgRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNRIGGD 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4759-4850 3.85e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 44.87  E-value: 3.85e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4759 PPtFVKKVDDFTALAGQTVTLQAAVRGSePI-SVMWMKGQEVIKEDGKIKmSFSSGvaVLTISDVQIGL-GGKYTCLAEN 4836
Cdd:cd20958       1 PP-FIRPMGNLTAVAGQTLRLHCPVAGY-PIsSITWEKDGRRLPLNHRQR-VFPNG--TLVIENVQRSSdEGEYTCTARN 75
                            90
                    ....*....|....
gi 1958765569  4837 EAGsQTSVGELIVK 4850
Cdd:cd20958      76 QQG-QSASRSVFVK 88
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
5530-5600 3.86e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 44.92  E-value: 3.86e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5530 LECIVAGSHPISIQWFKDDQEISASDKyKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTV 5600
Cdd:cd05730      23 LACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
6929-6994 3.87e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 44.94  E-value: 3.87e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6929 GDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENSIG 6994
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5901-5961 3.87e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.83  E-value: 3.87e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5901 ATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDsvaTLQVRSVDNGHSGRYTCQAKNE 5961
Cdd:cd20957      19 AVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRND 76
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
5523-5601 3.89e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 44.71  E-value: 3.89e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5523 IKGSFIDLECIVAGSHPISIQWFKDDQEISASdkyKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTVK 5601
Cdd:cd05731       8 LRGGVLLLECIAEGLPTPDIRWIKLGGELPKG---RTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTVE 83
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
29964-30046 3.93e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.90  E-value: 3.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29964 LKKTVIIRAGASLRLMVSVSGRPSPVITWSK--KGIDLANRAIID-NTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSA 30040
Cdd:cd05891       7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKndQDIELSEHYSVKlEQGKYASLTIKGVTSEDSGKYSINVKNKYGGETV 86

                    ....*.
gi 1958765569 30041 TVLVKV 30046
Cdd:cd05891      87 DVTVSV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12705-12793 3.93e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 44.72  E-value: 3.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12705 PRVIGLLRPLkdvTVTAGETATFDCELSYEDIP-VEWYLKGKKLEPND---KVVTRSEGRVHTLTLRDVKLEDAGEVQLT 12780
Cdd:cd20951       1 PEFIIRLQSH---TVWEKSDAKLRVEVQGKPDPeVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAV 77
                            90
                    ....*....|....*..
gi 1958765569 12781 AKD----FKTQANLFVK 12793
Cdd:cd20951      78 AKNihgeASSSASVVVE 94
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
9292-9380 3.93e-04

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 44.95  E-value: 3.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQL---NQ----GGRILIHQKGDeskLEIRDTTKTDSGLYRCV 9364
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLlfpYQppqpSSRFSVSPTGD---LTITNVQRSDVGYYICQ 78
                            90
                    ....*....|....*.
gi 1958765569  9365 AFNKHGEIESNVNLQV 9380
Cdd:cd05726      79 ALNVAGSILAKAQLEV 94
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
16640-16725 3.97e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 44.72  E-value: 3.97e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16640 VEEGTDVNIVAKIKGVPFPTLTWFKAPPKKPDSKEPVVYDTHVNKQVvddtCTLVIPQSRRSDTGLYSITAVNNLGTASK 16719
Cdd:cd20951      12 VWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGV----HVLHIRRVTVEDSAVYSAVAKNIHGEASS 87

                    ....*.
gi 1958765569 16720 EMRLNV 16725
Cdd:cd20951      88 SASVVV 93
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
33408-33505 3.97e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 44.31  E-value: 3.97e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33408 APESVSSKPVIVTGlrdttvssdSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYklsndkeeFILEIlktETSDGGLYS 33487
Cdd:pfam13895     1 KPVLTPSPTVVTEG---------EPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF--------FTLSV---SAEDSGTYT 60
                            90
                    ....*....|....*....
gi 1958765569 33488 CTVANSAGS-VSSSCKLTI 33505
Cdd:pfam13895    61 CVARNGRGGkVSNPVELTV 79
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
12800-12881 3.98e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.49  E-value: 3.98e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12800 TKPLEDQTVEEEATAVLECEVSRE-NAKVKWFKNGTEILKSKKYEIVADGR-VRKLIIHGCTPEDIKTYTC----DAKDF 12873
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYpDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCkavnSLGEA 80

                    ....*...
gi 1958765569 12874 KTSCNLNV 12881
Cdd:cd20973      81 TCSAELTV 88
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
17341-17418 3.99e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 3.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17341 TVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLaLEKTKAKRSDSGRYCVVVENSTG---SRKGFCQ 17417
Cdd:cd20970      13 TAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGTT-LTIRNIRRSDMGIYLCIASNGVPgsvEKRITLQ 91

                    .
gi 1958765569 17418 V 17418
Cdd:cd20970      92 V 92
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
31059-31126 4.00e-04

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 44.40  E-value: 4.00e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNEVGEV 31126
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMV 68
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7585-7666 4.01e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 44.31  E-value: 4.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7585 DTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKcqpsfadnvctLTLSSLEPSDTGAYTCVAAN-VAGQDESSAL 7663
Cdd:pfam13895     8 PTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN-----------FFTLSVSAEDSGTYTCVARNgRGGKVSNPVE 76

                    ...
gi 1958765569  7664 LTV 7666
Cdd:pfam13895    77 LTV 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
32092-32157 4.06e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.48  E-value: 4.06e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 32092 EEGGYVKYVCKIENYDQSTqVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVN 32157
Cdd:pfam13927    14 REGETVTLTCEATGSPPPT-ITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
3305-3391 4.06e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 44.69  E-value: 4.06e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3305 PAIVTPLQDAVT-SEGRPARFQCQVSGT-DLKVSWYCRDKKIKPSRFfrMTQFEDTyQLEIAEAFPEDEGTYAFVANNAV 3382
Cdd:cd20978       1 PKFIQKPEKNVVvKGGQDVTLPCQVTGVpQPKITWLHNGKPLQGPME--RATVEDG-TLTIINVQPEDTGYYGCVATNEI 77

                    ....*....
gi 1958765569  3383 GQVSSTATL 3391
Cdd:cd20978      78 GDIYTETLL 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
22668-22743 4.07e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 4.07e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 22668 TFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVpLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATE 22743
Cdd:cd20970      11 TVTAREGENATFMCRAEGSPEPEISWTRNGN-LIIEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGVPGSVE 85
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
5245-5317 4.10e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.41  E-value: 4.10e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5245 DVMLLAEVAGTPPFEITWFKDNTTLRsGRKYKTFIQDQlVSLQILKFVASDAGEYQCRVTNEVGSSTCSARVT 5317
Cdd:cd20952      16 TVVLNCQATGEPVPTISWLKDGVPLL-GKDERITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLD 86
PRK10819 PRK10819
transport protein TonB; Provisional
10812-10984 4.10e-04

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 48.14  E-value: 4.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10812 VPEIPKkPEEKVSVPV--PKKEKAPPAKVPEVPKKPVPEEKapvpvpkkvepppakvPEVPKKPVPEKKVPAPTPKKVEA 10889
Cdd:PRK10819     38 VIELPA-PAQPISVTMvaPADLEPPQAVQPPPEPVVEPEPE----------------PEPIPEPPKEAPVVIPKPEPKPK 100
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10890 PPAKaPEVPPKEVTPekkvpvvppkkpeapppkvpeppkevvpekkvsmVPPKRPEAPPAKVPEAS-KEVVPEKKVSVAP 10968
Cdd:PRK10819    101 PKPK-PKPKPVKKVE----------------------------------EQPKREVKPVEPRPASPfENTAPARPTSSTA 145
                           170
                    ....*....|....*.
gi 1958765569 10969 KKKPEAPAVKVPEAPK 10984
Cdd:PRK10819    146 TAAASKPVTSVSSGPR 161
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
3461-3551 4.11e-04

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 44.85  E-value: 4.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADykfvfDGNNHSLI-----ILFTRF-------QDE 3528
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKD-----DPRSHRIVlpsgsLFFLRVvhgrkgrSDE 75
                            90       100
                    ....*....|....*....|....
gi 1958765569  3529 GEYTCMASNEYGRAVC-SAHLKVS 3551
Cdd:cd07693      76 GVYVCVAHNSLGEAVSrNASLEVA 99
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5525-5593 4.12e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.49  E-value: 4.12e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5525 GSFIDLECIV-AGSHPISIQWFKDDQEISASDKYKFSFHDNTAF-LEISQLEGTDSGTYTCSATNKAGHSQ 5593
Cdd:pfam00047    11 GDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSsLLISNVTKEDAGTYTCVVNNPGGSAT 81
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
9677-9740 4.12e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.49  E-value: 4.12e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  9677 QNIVVSEHQSATFECEVSF--DDAIVTWYKGPTELTESQKYNFRNDGRCHYM-TIHNVTPDDEGVYS 9740
Cdd:pfam00047     4 PTVTVLEGDSATLTCSASTgsPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSlLISNVTKEDAGTYT 70
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
22659-22749 4.12e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 44.48  E-value: 4.12e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22659 PPAFKLLFNtFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRvnaESTENNSLLTIKEACR-EDVGHYTVKLTNS 22737
Cdd:cd20958       1 PPFIRPMGN-LTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR---QRVFPNGTLVIENVQRsSDEGEYTCTARNQ 76
                            90
                    ....*....|...
gi 1958765569 22738 AGE-ATETLNVIV 22749
Cdd:cd20958      77 QGQsASRSVFVKV 89
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7856-7945 4.19e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 44.70  E-value: 4.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLR-SAPAYKMQFK-NNVASLVINKVDHSDVGEYTCKAENS 7933
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  7934 VGAVASSAVLVI 7945
Cdd:cd05893      81 QGRISCTGRLMV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
13931-13985 4.21e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.86  E-value: 4.21e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 13931 TGYPRPKATWTFGDQVLEAGDRVKIKTISAYAELIISPSERPDKGIYTLTLENPV 13985
Cdd:cd00096       8 SGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSA 62
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
6367-6434 4.24e-04

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 45.00  E-value: 4.24e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6367 NTEVSLECELSGTPPFEVVWYK-------DKRQLRSSKKYKIASknfHASIHILNVDSTDIGEYHCKAQNEVGSD 6434
Cdd:cd20954      16 GQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYDPNVRILP---NGTLVFGHVQKENEGHYLCEAKNGIGSG 87
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
23514-23759 4.25e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.56  E-value: 4.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23514 NVNRYDSGKYTLTLENSSGTKSAFVTVRVLDTPSP---PVNLKVTE--------ITKDSVSITWEPPlldgGSKIKNYIV 23582
Cdd:COG4733     495 SIEENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPqwpPVNVTTSEslsvvaqgTAVTTLTVSWDAP----AGAVAYEVE 570
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23583 EKREATRKSYAAVVTNChknSWKIDQLQEGcSYYFRVTAENEYGIGLPARTADPI----KVAEVPQPPGkITVDDVTRnS 23658
Cdd:COG4733     571 WRRDDGNWVSVPRTSGT---SFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETtvtgKTAPPPAPTG-LTATGGLG-G 644
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23659 VSLSWTKPEHDGGSKIiqyivEMQAKNTDKWS----ECARVKSLEAVITSLTQGEEYLFRVIAVNEKGRSDPrsLAVPIT 23734
Cdd:COG4733     645 ITLSWSFPVDADTLRT-----EIRYSTTGDWAsatvAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSA--WWVSGQ 717
                           250       260
                    ....*....|....*....|....*
gi 1958765569 23735 AKDLVIEPDVRPAFSSYSVQVGQDL 23759
Cdd:COG4733     718 ASADAAGILDAITGQILETELGQEL 742
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
2043-2128 4.25e-04

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 44.50  E-value: 4.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2043 RIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVceLVIRDVTAEDSASIMVKAINIAGETSS 2122
Cdd:cd05867       5 RPQSHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGA--LILTDVQPSDTAVYQCEARNRHGNLLA 82

                    ....*.
gi 1958765569  2123 HAFLLV 2128
Cdd:cd05867      83 NAHVHV 88
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
3201-3288 4.26e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.41  E-value: 4.26e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3201 VLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKE-EQLLSTGFKCKFLHDGqeyTLLLIEAFPEDAAVYTCEAKNDYGV 3279
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDgVPLLGKDERITTLENG---SLQIKGAEKSDTGEYTCVALNLSGE 78

                    ....*....
gi 1958765569  3280 ATTSASLSV 3288
Cdd:cd20952      79 ATWSAVLDV 87
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
6915-6998 4.27e-04

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 44.77  E-value: 4.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLrstPEYRTYFTNN----VATLVFNKVGIN-DSGEYTCVA 6989
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEI---IADGLKYRIQefkgGYHQLIIASVTDdDATVYQVRA 78

                    ....*....
gi 1958765569  6990 ENSIGTAAS 6998
Cdd:cd20971      79 TNQGGSVSG 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
17046-17111 4.31e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.09  E-value: 4.31e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 17046 IVVHAGGVIRIIAYVSGKPPPTVTWNMNERALPQEATI--ETTAISSSMVIKNCQRSHQGVYSLLAKN 17111
Cdd:pfam13927    11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRsrSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
24821-24905 4.31e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.44  E-value: 4.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24821 TIQPsfklpfNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVnveETATSTILHIKESSKDDFGKYSVTATN 24900
Cdd:cd20957       5 TIDP------PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRV---QILSEDVLVIPSVKREDKGMYQCFVRN 75

                    ....*
gi 1958765569 24901 NAGTA 24905
Cdd:cd20957      76 DGDSA 80
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
4492-4569 4.32e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 44.51  E-value: 4.32e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4492 AINKKIHLECQVDEDRKVSITWSKDGQKLPagKDYKIYFEDkiASLEIPLAKLKDSGTYSCTASNEAGSSSSSATVAV 4569
Cdd:cd05728      12 DIGSSLRWECKASGNPRPAYRWLKNGQPLA--SENRIEVEA--GDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
12978-13046 4.32e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 44.54  E-value: 4.32e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12978 TKNLANLEVSEGDTIKLVC-EVSKPGAEVTWYKGDEEVIETGRFEILTDGRKRiliIQNAQLEDAGSYNC 13046
Cdd:cd20968       3 TRPPTNVTIIEGLKAVLPCtTMGNPKPSVSWIKGDDLIKENNRIAVLESGSLR---IHNVQKEDAGQYRC 69
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
5893-5966 4.33e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.52  E-value: 4.33e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5893 VTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDS-VATLQVRSVDNGHSGRYTCQAKNESGVER 5966
Cdd:cd05891      11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGkYASLTIKGVTSEDSGKYSINVKNKYGGET 85
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
12801-12870 4.35e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 4.35e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 12801 KPLEDQTVEEEATAVLECEVSRENA--KVKWFKNGTEILKSKKYEIVADGRVR--KLIIHGCTPEDIKTYTCDA 12870
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEATSENPspRYRWFKDGKELNRKRPKNIKIRNKKKnsELQINKAKLEDSGEYTCVV 77
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1678-1754 4.35e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 4.35e-04
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569   1678 GPAHFECRLTpiGDPTMVVEWLHDG-KPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:smart00410    10 ESVTLSCEAS--GSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
23066-23145 4.35e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.49  E-value: 4.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23066 VVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEI-KTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNVK 23144
Cdd:cd20973       8 EVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87

                    .
gi 1958765569 23145 V 23145
Cdd:cd20973      88 V 88
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
32885-32973 4.38e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 44.65  E-value: 4.38e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32885 APRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNYK 32964
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ....*....
gi 1958765569 32965 GEASDYATL 32973
Cdd:cd05747      83 GKQEAQFTL 91
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
12713-12793 4.41e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.49  E-value: 4.41e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12713 PLKDVTVTAGETATFDCELS--YEDIPVEWYLKGKKLEPNDKVV-TRSEGRVHTLTLRDVKLEDAGEVQLTAKDFKTQAN 12789
Cdd:pfam00047     2 APPTVTVLEGDSATLTCSAStgSPGPDVTWSKEGGTLIESLKVKhDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81

                    ....
gi 1958765569 12790 LFVK 12793
Cdd:pfam00047    82 LSTS 85
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8235-8317 4.41e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 44.71  E-value: 4.41e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIM-SENLLTSIHILNVDTADIGEYQCKATNDV 8313
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLvRENGVHSLIIEPVTSRDAGIYTCIATNRA 80

                    ....
gi 1958765569  8314 GSDT 8317
Cdd:cd20990      81 GQNS 84
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
8532-8611 4.43e-04

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 44.85  E-value: 4.43e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8532 GSSVVMECKVFGSPP--ISVLWLHDGNAI----SSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAGSDECSAPL 8605
Cdd:cd04970      17 GENATLQCHASHDPTldLTFTWSFNGVPIdlekIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSDSASATL 96

                    ....*.
gi 1958765569  8606 TVREPP 8611
Cdd:cd04970      97 VVRGPP 102
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4227-4286 4.45e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.50  E-value: 4.45e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4227 EVNWYFKGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNGKAMTSAKLTV 4286
Cdd:cd20972      32 VVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
23063-23145 4.45e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 44.50  E-value: 4.45e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23063 DTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKTTDFAT-SLSVKDAVRVDSGNYILKAKNVAGEKSVTV 23141
Cdd:cd05737       9 DVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTvYFTINGVSSEDSGKYGLVVKNKYGSETSDV 88

                    ....
gi 1958765569 23142 NVKV 23145
Cdd:cd05737      89 TVSV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
31455-31529 4.45e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.49  E-value: 4.45e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31455 SNATLVCKV-TGHPKPIVKWYRQGKEIIaDGLKYRVQEFKGGYHQLIIASVTDDDATVYQVRATNQGGSVSGTASL 31529
Cdd:pfam00047    12 DSATLTCSAsTGSPGPDVTWSKEGGTLI-ESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7576-7670 4.45e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.94  E-value: 4.45e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7576 PPSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVA 7655
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*
gi 1958765569  7656 GQDESSALLTVQEPP 7670
Cdd:cd05762      81 GSRQAQVNLTVVDKP 95
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
21981-22053 4.46e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.79  E-value: 4.46e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 21981 DTITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTH-LINKDSSRTDSGAYILTATNPGG 22053
Cdd:cd05744       8 GDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRAG 81
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
16336-16420 4.46e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 44.72  E-value: 4.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16336 AGSQIRIPAVIKGRPTPKSSWefdgkAKKAMKDGIHDIPEDAQLETAENSSVIVIPECTRAHSGKYSITAKNKAGQKTAN 16415
Cdd:cd20951      14 EKSDAKLRVEVQGKPDPEVKW-----YKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSS 88

                    ....*
gi 1958765569 16416 CRVKV 16420
Cdd:cd20951      89 ASVVV 93
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
7578-7666 4.47e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.53  E-value: 4.47e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7578 SFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGN---------EIISSPKCQPSFADNVctltlsslEPSDTGAYT 7648
Cdd:cd05763       1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGtdfpaarerRMHVMPEDDVFFIVDV--------KIEDTGVYS 72
                            90
                    ....*....|....*...
gi 1958765569  7649 CVAANVAGQDESSALLTV 7666
Cdd:cd05763      73 CTAQNSAGSISANATLTV 90
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
1807-1885 4.47e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 44.31  E-value: 4.47e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1807 PEPVRVLEGETARFRCRV-TGYPQPKVNWYLNGQLIR-KSKRFRVRYDGihYLDIVDCKSYDTGEVKVTAENPEGVTEHK 1884
Cdd:cd05724       4 PSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNlDNERVRIVDDG--NLLIAEARKSDEGTYKCVATNMVGERESR 81

                    .
gi 1958765569  1885 V 1885
Cdd:cd05724      82 A 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
18032-18112 4.50e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.79  E-value: 4.50e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18032 LVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDD-HYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHL 18110
Cdd:cd05744      10 LEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSaHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAEL 89

                    ..
gi 1958765569 18111 TV 18112
Cdd:cd05744      90 VV 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
33076-33162 4.52e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 4.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33076 LTKPRSITVHEGESARFSCDTDGE-PVPTVTWLRGGQVV--STSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDG 33152
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLKCEATSEnPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILG 82
                            90
                    ....*....|
gi 1958765569 33153 KQEAQFTLTV 33162
Cdd:cd05750      83 KDTVTGNVTV 92
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8989-9078 4.53e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 44.70  E-value: 4.53e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8989 PFFDIPLAPVDAVVGESADLECHVTGTQPIKVTWAKDNREIR-SGGNYQISY-LENSAHLTIVKVDKGDSGQYTCYAINE 9066
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRdLDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  9067 VGKDSCTAQLNI 9078
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2229-2296 4.54e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.41  E-value: 4.54e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  2229 FVKELQDIEVPESYSGELECIIS----PENIegkWYHNDVELKSNGKYSITSRR-GRQNLTVKDVTKEDQGEY 2296
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSglptPDLF---WQLNGKPVRPDSAHKMLVREnGRHSLIIEPVTKRDAGIY 72
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
27415-27560 4.55e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.56  E-value: 4.55e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27415 TIEWYKDDKELQTNAlvcvenSTDLASILIKDanrLNSGSYELKLR--NAMGSASA---TIRVQILDKPGPPGGPIEFkT 27489
Cdd:COG4733     568 EVEWRRDDGNWVSVP------RTSGTSFEVPG---IYAGDYEVRVRaiNALGVSSAwaaSSETTVTGKTAPPPAPTGL-T 637
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 27490 VTA--EKITLLWRPPADDGgakITHYIVEKRETSRVVWSMVAENLEECIITTTKIIKGN-EYIFRVRAVNKYGI 27560
Cdd:COG4733     638 ATGglGGITLSWSFPVDAD---TLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGqTYYYRARAVDRSGN 708
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
20520-20575 4.58e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 44.54  E-value: 4.58e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 20520 GKPAPSVSWKKGEDPLATDTRVSVESTAvntTLVVYDCQKSDAGKYTITLKNVAGT 20575
Cdd:cd20968      25 GNPKPSVSWIKGDDLIKENNRIAVLESG---SLRIHNVQKEDAGQYRCVAKNSLGI 77
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
14691-14887 4.59e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.56  E-value: 4.59e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14691 DTFTTPGPPYALTVVDVTKRH-----------VDLKWEPPKNDGgrpiqRYIIE-KKEklGTRWVKAGKTSGPdcNFRVT 14758
Cdd:COG4733     522 GAFDDVPPQWPPVNVTTSESLsvvaqgtavttLTVSWDAPAGAV-----AYEVEwRRD--DGNWVSVPRTSGT--SFEVP 592
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14759 DVIEGTeVQFQVRAENEAGV-GHPSEPTEILsIEDPVGPPSPPLDLHVTdAGRKHIAIAWKPPEkngGSPIIGYHVEMCP 14837
Cdd:COG4733     593 GIYAGD-YEVRVRAINALGVsSAWAASSETT-VTGKTAPPPAPTGLTAT-GGLGGITLSWSFPV---DADTLRTEIRYST 666
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 14838 VGTekW----MRVNSRPIKDLkfkVEEGVVPDKEYVLRVRAVNAVGVSDPSEIS 14887
Cdd:COG4733     667 TGD--WasatVAQALYPGNTY---TLAGLKAGQTYYYRARAVDRSGNVSAWWVS 715
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
1804-1847 4.60e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 44.31  E-value: 4.60e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1958765569  1804 VLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRF 1847
Cdd:pfam13895     3 VLTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF 46
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
5413-5504 4.60e-04

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 44.85  E-value: 4.60e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5413 EPATITEEAVSIDVTQGDPATLQVKFS--GTKEISAKWFKDGQELTL----GPKYKISVTDTVSILKIISTEKKDSGEYT 5486
Cdd:cd04970       1 DATRITLAPSNADITVGENATLQCHAShdPTLDLTFTWSFNGVPIDLekieGHYRRRYGKDSNGDLEIVNAQLKHAGRYT 80
                            90
                    ....*....|....*...
gi 1958765569  5487 FEVQNDVGRSSCKASINV 5504
Cdd:cd04970      81 CTAQTVVDSDSASATLVV 98
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
13511-13604 4.63e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.94  E-value: 4.63e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13511 PPKIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFK------ENEPLSTKTVDTTAEQTsfrILEAKKEDKGRYKIVLQ 13584
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKfrkqiqEGEGIKIENTENSSKLT---ITEGQQEHCGCYTLEVE 77
                            90       100
                    ....*....|....*....|
gi 1958765569 13585 NKHGKAEGFINLQVIDVPGP 13604
Cdd:cd05762      78 NKLGSRQAQVNLTVVDKPDP 97
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
28083-28152 4.65e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.41  E-value: 4.65e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28083 AQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYvRFSKTENKiTLSIKNVKKENGGKYTVILDN 28152
Cdd:cd20952       7 QNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDE-RITTLENG-SLQIKGAEKSDTGEYTCVALN 74
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9181-9262 4.67e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 4.67e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9181 PPVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRcsFSF-----ASGTAV--LELKDTAKADSGDYV 9253
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPR--FRVgdyvtSDGDVVsyVNISSVRVEDGGEYT 78

                    ....*....
gi 1958765569  9254 CKASNVAGS 9262
Cdd:cd20956      79 CTATNDVGS 87
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
5524-5590 4.67e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 44.50  E-value: 4.67e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5524 KGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHD-NTAFLEISQLEGTDSGTYTCSATNKAG 5590
Cdd:cd05737      15 EGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYG 82
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
2758-2839 4.68e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 44.31  E-value: 4.68e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2758 IKKPKDVTALENATVAFEVSVSHDTVP-VKWFHKNVEIkPSDKHRLVSErkvHKLMLQNISPSDAGEYTAV----VGQLE 2832
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPtVRWRKEDGEL-PKGRYEILDD---HSLKIRKVTAGDMGSYTCVaenmVGKIE 76

                    ....*..
gi 1958765569  2833 CKAKLFV 2839
Cdd:cd05725      77 ASATLTV 83
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
18032-18112 4.70e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 44.31  E-value: 4.70e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18032 LVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDD-HYTVETDSfssvLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHL 18110
Cdd:cd20978      11 VVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMeRATVEDGT----LTIINVQPEDTGYYGCVATNEIGDIYTETLL 86

                    ..
gi 1958765569 18111 TV 18112
Cdd:cd20978      87 HV 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7489-7571 4.73e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 44.48  E-value: 4.73e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7489 PMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHitfVRNLASLKIPSAEMN-DKGLYSFEVENSVGKSScTVS 7567
Cdd:cd20958       9 NLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQR---VFPNGTLVIENVQRSsDEGEYTCTARNQQGQSA-SRS 84

                    ....
gi 1958765569  7568 VHVS 7571
Cdd:cd20958      85 VFVK 88
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
8703-8793 4.76e-04

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 44.63  E-value: 4.76e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8703 PAIFVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKngVNVTASQRCNITTTekSAILEILSSTVEDSGQYNCYIENAS 8782
Cdd:cd05851       1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRK--ILEPMPATAEISMS--GAVLKIFNIQPEDEGTYECEAENIK 76
                            90
                    ....*....|.
gi 1958765569  8783 GKDSCSAQILI 8793
Cdd:cd05851      77 GKDKHQARVYV 87
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
27638-27773 4.78e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.56  E-value: 4.78e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27638 KVTGLTENSDYQYRVCAVNAAgmgpfsepSDFYKAAD-----PIDPPGPPAKIRIADST--------KSSITLGWskpvy 27704
Cdd:COG4733     492 RVVSIEENEDGTYTITAVQHA--------PEKYAAIDagafdDVPPQWPPVNVTTSESLsvvaqgtaVTTLTVSW----- 558
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 27705 DGGSDVTGYVVEMRQGeEEEWTIVstkGEARTTEYVVSNLKPGvNYYFQVSAVNCAGQGEPITMTEPVQ 27773
Cdd:COG4733     559 DAPAGAVAYEVEWRRD-DGNWVSV---PRTSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETT 622
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
15634-15700 4.79e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.86  E-value: 4.79e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 15634 LRIPAVVTGRPVPTKVWTIEEGELD-KERVVIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAA 15700
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPpSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4312-4381 4.81e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.47  E-value: 4.81e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4312 TCEIQGAPNVRFQWFKAGREIYESDKcsIRSSNY-------ISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTV 4381
Cdd:cd20956      22 KCVASGNPLPQITWTLDGFPIPESPR--FRVGDYvtsdgdvVSYVNISSVRVEDGGEYTCTATNDVGSVSHSARINV 96
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
19869-20081 4.82e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.56  E-value: 4.82e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19869 SVNRKDSGDYTITAENSSGSKSATIKLKVLDKPGP---PASVKINKMYAD--------RAMLSWEPPledggseiTNYIV 19937
Cdd:COG4733     495 SIEENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPqwpPVNVTTSESLSVvaqgtavtTLTVSWDAP--------AGAVA 566
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19938 DKRETSRPNWAQVS-ATVPITSCTVEKLIEGhEYQFRICAENKYGVGDPIFTEPVIAKNPYDPPgrcdPPVISNIT---- 20012
Cdd:COG4733     567 YEVEWRRDDGNWVSvPRTSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETTVTGKTAP----PPAPTGLTatgg 641
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 20013 KDHMTVSWKAPADdggSPITGYlvEKRETQAVNWT--KVNRKPVIERTLKATGLQEGTEYEFRVTAINKAG 20081
Cdd:COG4733     642 LGGITLSWSFPVD---ADTLRT--EIRYSTTGDWAsaTVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
I-set pfam07679
Immunoglobulin I-set domain;
12620-12703 4.88e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.56  E-value: 4.88e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12620 KLVRPLYSVEVMETETARFETEISED-DIHANWKLKGEALLQTPECEIKEEGKIHVLILHNCRLDQTGGVDFQAAN---- 12694
Cdd:pfam07679     2 KFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNsage 81

                    ....*....
gi 1958765569 12695 VKSSAHLRV 12703
Cdd:pfam07679    82 AEASAELTV 90
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
4201-4286 4.92e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 44.63  E-value: 4.92e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4201 ILKPLVDTISEKGDTVHLTSSISNAK-EVNWYFKGDLVPPGAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGNGKAM 4279
Cdd:cd20949       3 TENAYVTTVKEGQSATILCEVKGEPQpNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82

                    ....*..
gi 1958765569  4280 TSAKLTV 4286
Cdd:cd20949      83 DMQERTV 89
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
18034-18112 4.94e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 44.52  E-value: 4.94e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18034 VKAGTTVRFPAIIRGVPVPTAKWATDGTE---ITTDDHYTVETDSFSsvLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHL 18110
Cdd:cd05729      16 LPAANKVRLECGAGGNPMPNITWLKDGKEfkkEHRIGGTKVEEKGWS--LIIERAIPRDKGKYTCIVENEYGSINHTYDV 93

                    ..
gi 1958765569 18111 TV 18112
Cdd:cd05729      94 DV 95
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
9189-9256 4.96e-04

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 44.16  E-value: 4.96e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9189 TPVTASEGDFLQLSCHVQGSEPiRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKA 9256
Cdd:cd20967       5 PAVQVSKGHKIRLTVELADPDA-EVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA 71
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
26311-26381 4.97e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 44.65  E-value: 4.97e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 26311 IVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAG 26381
Cdd:cd05747      13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5322-5412 5.01e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 44.65  E-value: 5.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5322 PSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEI--TEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKND 5399
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIstSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  5400 AGIQRCSALLSVK 5412
Cdd:cd20974      81 SGQATSTAELLVL 93
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8252-8315 5.01e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 43.71  E-value: 5.01e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  8252 VHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTsihILNVDTADIGEYQCKATNDVGS 8315
Cdd:cd05746       1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEGYLA---IRDVGVADQGRYECVARNTIGY 61
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
25638-25706 5.02e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 44.72  E-value: 5.02e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 25638 RLFVTIKGRPEPEVKWEKaEGILTERA------QIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSG--SKTAFVNVR 25706
Cdd:cd20951      19 KLRVEVQGKPDPEVKWYK-NGVPIDPSsipgkyKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGeaSSSASVVVE 94
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
6549-6629 5.02e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.53  E-value: 5.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6549 MTVTVGETCSLECKVAGTPELSVEWYKDGKL-LTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVV 6627
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGGTdFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATL 88

                    ..
gi 1958765569  6628 DV 6629
Cdd:cd05763      89 TV 90
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
4292-4384 5.04e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 44.56  E-value: 5.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIY--ESDKCSIRSSNyiSSLEILRTQVVDCGEYTCKASNE 4369
Cdd:cd05736       1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINpkLSKQLTLIANG--SELHISNVRYEDTGAYTCIAKNE 78
                            90
                    ....*....|....*
gi 1958765569  4370 YGSVSCTATLTVTEA 4384
Cdd:cd05736      79 GGVDEDISSLFVEDS 93
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9190-9271 5.06e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 44.48  E-value: 5.06e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9190 PVTASEGDFLQLSCHVQGSePI-RIQWLRAGREIkPSDRCSFSFASGTavLELKDTAKA-DSGDYVCKASNVAG-SDTSK 9266
Cdd:cd20958       9 NLTAVAGQTLRLHCPVAGY-PIsSITWEKDGRRL-PLNHRQRVFPNGT--LVIENVQRSsDEGEYTCTARNQQGqSASRS 84

                    ....*
gi 1958765569  9267 CKVTI 9271
Cdd:cd20958      85 VFVKV 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
10144-10254 5.06e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 5.06e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10144 PKKVEPPAVKVPEAPKKPVPEEKKPVPIPKKEPAAPPKvPEAPKKPAPEEKTAVPVAKKKEAPPPKVTEVQKKVVTEeki 10223
Cdd:PHA03247   2873 AKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ-PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTD--- 2948
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1958765569 10224 tiiPQREESPPPAVPEIPKKKVPEEKRPVPR 10254
Cdd:PHA03247   2949 ---PAGAGEPSGAVPQPWLGALVPGRVAVPR 2976
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
26316-26394 5.07e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 44.54  E-value: 5.07e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 26316 GEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSnTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNCKVLDK 26394
Cdd:cd05730      18 GQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDG-SEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFAK 95
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
6356-6433 5.07e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.92  E-value: 5.07e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6356 SSFPPVVEtlkNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYkiasknfhasiHILNVDSTDIGEYHCKAQNEVGS 6433
Cdd:pfam13895     6 PSPTVVTE---GEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF-----------FTLSVSAEDSGTYTCVARNGRGG 69
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
31549-31617 5.09e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.09  E-value: 5.09e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31549 VHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKN 31617
Cdd:pfam13927    11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISN-VTRSDAGTYTCVASN 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
5336-5411 5.09e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.49  E-value: 5.09e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5336 GGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTF-ENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSV 5411
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
14910-14988 5.10e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.50  E-value: 5.10e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 14910 VIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASINVKV 14988
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
6271-6347 5.10e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.49  E-value: 5.10e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6271 VKAGDSARLECKI-TGSPEIRVVWYRN----EHELTASDKYQMTFIDSVavmQMNSLGTEDSGDFICEAQNPAGSTSCST 6345
Cdd:pfam00047     8 VLEGDSATLTCSAsTGSPGPDVTWSKEggtlIESLKVKHDNGRTTQSSL---LISNVTKEDAGTYTCVVNNPGGSATLST 84

                    ..
gi 1958765569  6346 KV 6347
Cdd:pfam00047    85 SL 86
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
9195-9265 5.11e-04

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 44.64  E-value: 5.11e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  9195 EGDFLQLSCHVQG-SEPIRIQWLRAGREIKPSDRCSFSFASGTAVLELKDTAKADSGDYVCKASNVAGSDTS 9265
Cdd:cd20927      13 EGGHVKYVCKIENyDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSS 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
27809-27869 5.11e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.41  E-value: 5.11e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 27809 GRPPPTVTWRKDEKNLGSDARYSI--QNTDSSSLLvIPQVTRNDTGKYILTIENGVGQPKSST 27869
Cdd:cd05744      26 GLPTPDLFWQLNGKPVRPDSAHKMlvRENGRHSLI-IEPVTKRDAGIYTCIARNRAGENSFNA 87
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8427-8511 5.12e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.53  E-value: 5.12e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8427 KPESIKVTTGDTCTLECMVSGTPELSTKWFKD-GKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSC 8505
Cdd:cd05763       5 TPHDITIRAGSTARLECAATGHPTPQIAWQKDgGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISA 84

                    ....*.
gi 1958765569  8506 TVSIQV 8511
Cdd:cd05763      85 NATLTV 90
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
1524-1597 5.13e-04

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 44.11  E-value: 5.13e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  1524 NVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIriegtKGEAALKIDSTISQDSAWYTATAINKAG 1597
Cdd:cd05723       6 NIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKI-----VKEHNLQVLGLVKSDEGFYQCIAENDVG 74
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
30-97 5.15e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.47  E-value: 5.15e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569    30 SGSPVPEVSWFRDGQVISTS---------TLPGVQISFsdgrarLMIPAVTKANSGRYSLRATNGSGQATSTAELLV 97
Cdd:cd20956      26 SGNPLPQITWTLDGFPIPESprfrvgdyvTSDGDVVSY------VNISSVRVEDGGEYTCTATNDVGSVSHSARINV 96
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
7762-7852 5.15e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 44.69  E-value: 5.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7762 PATFVKRLADT-SVETGSPIVLEATYSGTPPIAVSWL-KNEYPLSQSPNcGITTTERSSILEILESTIEDYAQYACLIEN 7839
Cdd:cd20969       1 RAAIRDRKAQQvFVDEGHTVQFVCRADGDPPPAILWLsPRKHLVSAKSN-GRLTVFPDGTLEVRYAQVQDNGTYLCIAAN 79
                            90
                    ....*....|...
gi 1958765569  7840 EAGQDICEALVSV 7852
Cdd:cd20969      80 AGGNDSMPAHLHV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
14900-14982 5.22e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 44.65  E-value: 5.22e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14900 TIDLETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGS 14979
Cdd:cd05747       5 TILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84

                    ...
gi 1958765569 14980 ATA 14982
Cdd:cd05747      85 QEA 87
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
21984-22063 5.22e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 44.54  E-value: 5.22e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21984 TLKAGEAFKLEADVSGRPPPTMEWAKDGKELEgTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNVKV 22063
Cdd:cd05730      14 TANLGQSVTLACDADGFPEPTMTWTKDGEPIE-SGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7485-7560 5.22e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 44.31  E-value: 5.22e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7485 EKPEPMTVTTGNPFTLECVVA-GTPELSAKWLKDGREL-SSGSRHHITFVRNLAslkIPSAEMNDKGLYSFEVENSVG 7560
Cdd:cd05724       2 VEPSDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLnLDNERVRIVDDGNLL---IAEARKSDEGTYKCVATNMVG 76
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
31045-31132 5.24e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 44.38  E-value: 5.24e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31045 PGVRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRfGKELVQ--SRKYKMSSDGRTHTLTVMTEEQEDEGVYTCVATNE 31122
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLR-NRQPVRpdQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNE 79
                            90
                    ....*....|
gi 1958765569 31123 VGEVETSSKL 31132
Cdd:cd20975      80 YGARQCEARL 89
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
8894-8980 5.25e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.42  E-value: 5.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8894 SFSRQLRDVQETVGLPVVFECAVSGS-EPIsVSWYKDGKPLKDSpNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPI- 8971
Cdd:cd20970       4 STPQPSFTVTAREGENATFMCRAEGSpEPE-ISWTRNGNLIIEF-NTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGVp 81

                    ....*....
gi 1958765569  8972 GSASSSAKL 8980
Cdd:cd20970      82 GSVEKRITL 90
PTZ00121 PTZ00121
MAEBL; Provisional
10942-11432 5.28e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 5.28e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10942 KRPEAPPAKVPEASKEVVPEKKVSVAPKKKPEAPAVKVPEAPKKVVPEKKVPVAAPKKPEAPAAEVPEVPKAAVPQKKIP 11021
Cdd:PTZ00121   1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11022 EAVPPKPESPPPEVYEEPAEEIVPEEPPEEVVEEPEPAPPPKVTVPPKKPVPEKKAPPAVVKKPEPPPAKAPEVPKEApP 11101
Cdd:PTZ00121   1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA-E 1480
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11102 EKKVPSVVPKKPEAPPAKVPEVPKEVVPEKKVAVPKKPEvpPAKVPEVPKKpvVEEKPVIEE-KPAIPVAEKVESPPTEV 11180
Cdd:PTZ00121   1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE--EAKKADEAKK--AEEAKKADEaKKAEEKKKADELKKAEE 1556
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11181 YEEPEEVAAQEEEPAPVVEEEEYEAPPPPAPEIPVPQVPEEPKKVVPEKKypvikkpepppPKVPEVSKKPAPMKKVPVV 11260
Cdd:PTZ00121   1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK-----------MKAEEAKKAEEAKIKAEEL 1625
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11261 KKPEPPEAEVPEVPKKLAPVKKEPVPVTKKPEVLPEKVPEAPKKITPEKRESAPVPEEPEAPPAPVEEIPEETiyEEKAT 11340
Cdd:PTZ00121   1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKK 1703
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11341 ITIGRKETPpvEEREIERFIQPEEPGMEPQPEETPVQEPEPEKKVIEKPKlkprppirapsppKEDVKEKIFQLKAVSKK 11420
Cdd:PTZ00121   1704 AEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK-------------DEEEKKKIAHLKKEEEK 1768
                           490
                    ....*....|..
gi 1958765569 11421 KVPEKPEVVEKV 11432
Cdd:PTZ00121   1769 KAEEIRKEKEAV 1780
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
4773-4840 5.30e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 44.46  E-value: 5.30e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4773 AGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIK-MSFSSGVAVLTISDVQIGLGGKYTCLAENEAGS 4840
Cdd:cd05857      18 AANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGgYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGS 86
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5136-5226 5.31e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 44.65  E-value: 5.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5136 TFTEKLEpSQLLKKGDATQLVCKVTGTPPIKITWFANDR--ELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNE 5213
Cdd:cd20974       2 VFTQPLQ-SVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  5214 AGSDHCTSIVIVK 5226
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8518-8594 5.37e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 44.10  E-value: 5.37e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8518 PSFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDGNAISSGRKyQTTLTDNTcaLTVNMLE-DADAGDYTCIATN 8594
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR-QRVFPNGT--LVIENVQrSSDEGEYTCTARN 75
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3322-3389 5.38e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.86  E-value: 5.38e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3322 ARFQCQVSGT-DLKVSWYCRDKKIKPSRFFRMTQFEDTYQLEIAEAFPEDEGTYAFVANNAV-GQVSSTA 3389
Cdd:cd00096       1 VTLTCSASGNpPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
1253-1337 5.41e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 44.13  E-value: 5.41e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1253 IKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDflqdgRASLRIPVVLPEDEGIYTAFASNIKGNAICS 1332
Cdd:cd05728       6 ISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE-----AGDLRITKLSLSDSGMYQCVAENKHGTIYAS 80

                    ....*
gi 1958765569  1333 GKLYV 1337
Cdd:cd05728      81 AELAV 85
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8519-8607 5.43e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.53  E-value: 5.43e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8519 SFTRKLKETNGLSGSSVVMECKVFGSPPISVLWLHDG-NAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAG 8597
Cdd:cd05763       1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAG 80
                            90
                    ....*....|
gi 1958765569  8598 SDECSAPLTV 8607
Cdd:cd05763      81 SISANATLTV 90
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11366-11634 5.44e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 49.00  E-value: 5.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11366 GMEPQPEETPVQEPEPEKKVIEKPKLKPRPPIRAPSPPKEDVKEKIFQLKAVSKKKVPEKPEVVEKVEPTPLKVPTAEKK 11445
Cdd:NF033839    154 GSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVAL 233
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11446 VRKL-------LPE---PKPQPKEEVVLKSVLRKRPEEEEPKVEPKKVEKVKKPEEPPPPPKAVEVEAPPEPKPKERKVP 11515
Cdd:NF033839    234 IKELdelkkqaLSEidnVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPE 313
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11516 EPTKVPEIKPAIPLPGPEPKPKPEPEVKTMKA------PPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKP---KGPIK 11586
Cdd:NF033839    314 PETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPqletpkPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPevkPQPEK 393
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11587 GVAKKTPSPiEAERKKLRPGSGGEKP---PDEAPFTYQLKAVPLKFVKEIK 11634
Cdd:NF033839    394 PKPEVKPQP-EKPKPEVKPQPEKPKPevkPQPEKPKPEVKPQPEKPKPEVK 443
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
23756-23830 5.45e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.10  E-value: 5.45e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 23756 GQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVI-DSLDLTTLSIKETHKDDGGHYGITVANVVGQKTAAIEII 23830
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
33435-33505 5.48e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 43.77  E-value: 5.48e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33435 FVIKVTGEPQPTVTWTKDGKaiaqsskyKLSNDKEEFIL-----EILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd05745       7 FLCEAQGYPQPVIAWTKGGS--------QLSVDRRHLVLssgtlRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
3461-3550 5.50e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 44.38  E-value: 5.50e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSaDYKFVFDGNNH--SLIILFTRFQDEGEYTCMASNE 3538
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPD-QRRFAEEAEGGlcRLRILAAERGDAGFYTCKAVNE 79
                            90
                    ....*....|..
gi 1958765569  3539 YGRAVCSAHLKV 3550
Cdd:cd20975      80 YGARQCEARLEV 91
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
8433-8511 5.51e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 44.46  E-value: 5.51e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8433 VTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSK---YKISffNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCTVSI 8509
Cdd:cd05857      16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKVR--NQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHL 93

                    ..
gi 1958765569  8510 QV 8511
Cdd:cd05857      94 DV 95
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
5698-5779 5.53e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 44.36  E-value: 5.53e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5698 QFIKKPSPvLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGlATFQISNARVENSGTYVCEARNDAG 5777
Cdd:cd04978       1 YWIIEPPS-LVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDG-RTLIFSNLQPNDTAVYQCNASNVHG 78

                    ..
gi 1958765569  5778 TA 5779
Cdd:cd04978      79 YL 80
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
5144-5215 5.54e-04

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 44.12  E-value: 5.54e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  5144 SQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAvLRLTDVAIEDSGEYMCEAQNEAG 5215
Cdd:cd05867       8 SHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGA-LILTDVQPSDTAVYQCEARNRHG 78
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
4588-4661 5.56e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 44.47  E-value: 5.56e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSfaNSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEV 4661
Cdd:cd05856      19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENK--KKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKV 90
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
27791-27874 5.56e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.42  E-value: 5.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27791 TSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNL-GSDARYSIQntDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSST 27869
Cdd:cd20970      10 FTVTAREGENATFMCRAEGSPEPEISWTRNGNLIiEFNTRYIVR--ENGTTLTIRNIRRSDMGIYLCIASNGVPGSVEKR 87

                    ....*
gi 1958765569 27870 VSVKV 27874
Cdd:cd20970      88 ITLQV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
5887-5965 5.57e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 44.50  E-value: 5.57e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5887 IKKIENVTTVLKSSA-TFQSTVAGSPPISITWLKDDQILEENDNVHISFED-SVATLQVRSVDNGHSGRYTCQAKNESGV 5964
Cdd:cd05737       4 LGGLPDVVTIMEGKTlNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGS 83

                    .
gi 1958765569  5965 E 5965
Cdd:cd05737      84 E 84
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
18034-18112 5.59e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 44.33  E-value: 5.59e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18034 VKAGTTVRFPAIIRGVPVPTAKWATDGTEIT---TDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHL 18110
Cdd:cd20951      12 VWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDpssIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASV 91

                    ..
gi 1958765569 18111 TV 18112
Cdd:cd20951      92 VV 93
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
1530-1607 5.59e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 44.06  E-value: 5.59e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1530 GSRLEMKVRATGNPNPDIVWLKnSDIIVPHKYPRIRIEGTKGEAALKIDSTISQDSAWYTATAINKAGRDTTRCKVNI 1607
Cdd:cd05894      10 GNKLRLDVPISGEPAPTVTWSR-GDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5321-5411 5.61e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 44.16  E-value: 5.61e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5321 PPSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNiRMTFENNVASLYLSGIEVKHDGKYVCQAKNDA 5400
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  5401 GIQRCSALLSV 5411
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
12354-12428 5.63e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.41  E-value: 5.63e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 12354 FITPLSDVKVFEKDEAKFECEVSR--EPKTFrWLKGTQEIAGDDRFELIKDGT-RHSLVIKSAAFEDEAKYMFEAEDK 12428
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSGlpTPDLF-WQLNGKPVRPDSAHKMLVRENgRHSLIIEPVTKRDAGIYTCIARNR 79
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
9191-9264 5.66e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.02  E-value: 5.66e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  9191 VTASEGDFLqLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGTavLELKDTAKADSGDYVCKASNVAGSDT 9264
Cdd:cd20952      10 TVAVGGTVV-LNCQATGEPVPTISWLKDGVPLLGKDERITTLENGS--LQIKGAEKSDTGEYTCVALNLSGEAT 80
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
33704-33787 5.68e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 44.13  E-value: 5.68e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33704 PRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSrnmyTLEIRNASVSDSGKYTVKAKNFRGQCSATA 33783
Cdd:cd05728       6 ISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAG----DLRITKLSLSDSGMYQCVAENKHGTIYASA 81

                    ....
gi 1958765569 33784 SLTV 33787
Cdd:cd05728      82 ELAV 85
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
13001-13046 5.71e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 44.37  E-value: 5.71e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569 13001 PGAEVTWYKGDEEVIETGRFEILTDGRkriLIIQNAQLEDAGSYNC 13046
Cdd:cd04969      30 PKPTISWSKGTELLTNSSRICILPDGS---LKIKNVTKSDEGKYTC 72
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
5697-5787 5.75e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 44.37  E-value: 5.75e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5697 PQFIKKPSPVLVLrNGQSTTFECQVTGTPEIRVSWYLDgNEITDLRRYGISFVD---GLATFQISNARVENSGTYVCEAR 5773
Cdd:cd05892       1 PMFIQKPQNKKVL-EGDPVRLECQISAIPPPQIFWKKN-NEMLQYNTDRISLYQdncGRICLLIQNANKKDAGWYTVSAV 78
                            90
                    ....*....|....
gi 1958765569  5774 NDAGTASCSIELKV 5787
Cdd:cd05892      79 NEAGVVSCNARLDV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
8428-8511 5.76e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 44.06  E-value: 5.76e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8428 PESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELT-GDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCT 8506
Cdd:cd05894       2 ENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTaTEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS 81

                    ....*
gi 1958765569  8507 VSIQV 8511
Cdd:cd05894      82 LFVKV 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2141-2222 5.78e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.03  E-value: 5.78e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   2141 QDVVAKEKDTmATFECE-TSEPFVKVKWYKDGIE-VHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSC-VLVEDENIKTT 2217
Cdd:smart00410     2 PSVTVKEGES-VTLSCEaSGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCaATNSSGSASSG 80

                     ....*
gi 1958765569   2218 AKLIV 2222
Cdd:smart00410    81 TTLTV 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8062-8137 5.83e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.10  E-value: 5.83e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8062 GESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVEN-TATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQLGV 8137
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
5145-5216 5.83e-04

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 44.46  E-value: 5.83e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5145 QLLKKGDATQLVCKVTGTPPIKITW--FANDRE---LRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGS 5216
Cdd:cd05765      10 QTVKVGETASFHCDVTGRPQPEITWekQVPGKEnliMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGL 86
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
15934-16006 5.86e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 44.36  E-value: 5.86e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 15934 VTGLPMPKIEWSKNEKVIEkptdalnITKEEVSRSEAKTELSIPKAVREDKGTYTITASNRLGSVFRNVHVEV 16006
Cdd:cd04978      23 AEGNPQPTITWRLNGVPIE-------PAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHGYLLANAFLHV 88
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
4875-4942 5.90e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 44.21  E-value: 5.90e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  4875 TVSGTPELKPKWYKDGRPLVASKK---YRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTV 4942
Cdd:cd05895      23 TSSEYPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSASANVTI 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
2048-2129 5.91e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.12  E-value: 5.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2048 TVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVCeLVIRDVTAEDSASIMVKAINIAGETSshAFLL 2127
Cdd:cd05748       3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTS-LVIKNAKRSDSGKYTLTLKNSAGEKS--ATIN 79

                    ..
gi 1958765569  2128 VQ 2129
Cdd:cd05748      80 VK 81
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
9295-9380 5.91e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 44.44  E-value: 5.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9295 EPQSIRVVEKTT-----ATFIAKVGGDPIPNVKWTKGK----WRQLNQGGRILIHQKGDESKLEIRDTTKTDSGLYRCVA 9365
Cdd:cd05732       2 QPKITYLENQTAveleqITLTCEAEGDPIPEITWRRATrgisFEEGDLDGRIVVRGHARVSSLTLKDVQLTDAGRYDCEA 81
                            90
                    ....*....|....*
gi 1958765569  9366 FNKHGEIESNVNLQV 9380
Cdd:cd05732      82 SNRIGGDQQSMYLEV 96
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
7293-7373 5.93e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 44.27  E-value: 5.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7293 PPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    .
gi 1958765569  7373 G 7373
Cdd:cd05747      83 G 83
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
9002-9078 5.96e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 44.21  E-value: 5.96e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9002 VGESADLECHVTGTQP-IKVTWAKDNREIRSGG---NYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLN 9077
Cdd:cd05895      13 AGSKLVLRCETSSEYPsLRFKWFKNGKEINRKNkpeNIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSASANVT 92

                    .
gi 1958765569  9078 I 9078
Cdd:cd05895      93 I 93
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
31059-31134 5.96e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 44.32  E-value: 5.96e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRFGKELV-QSRKYKMSSD-GRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSKLLL 31134
Cdd:cd05893      15 GMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDlDGTCSLHTTASTLDDDGNYTIMAANPQGRISCTGRLMV 92
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
11644-11717 6.01e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.06  E-value: 6.01e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 11644 VGSSAIFECLVSPSTAIT-TWMKDGSNIRESPKHRFIADgkDRkLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKL 11717
Cdd:cd20957      15 FGRTAVFNCSVTGNPIHTvLWMKDGKPLGHSSRVQILSE--DV-LVIPSVKREDKGMYQCFVRNDGDSAQATAEL 86
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
9000-9078 6.05e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.99  E-value: 6.05e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9000 AVVGESADLECHVTGTQPIKVTWAKDNREIRSGGnyQISYLENSAhLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLNI 9078
Cdd:cd04969      14 AAKGGDVIIECKPKASPKPTISWSKGTELLTNSS--RICILPDGS-LKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
31058-31132 6.07e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 44.47  E-value: 6.07e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31058 LGEAAQLSCQIVGRPLPDIKWYRFGKELV-----QSRKYKMssdgrthTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:cd05856      18 VGSSVRLKCVASGNPRPDITWLKDNKPLTppeigENKKKKW-------TLSLKNLKPEDSGKYTCHVSNRAGEINATYKV 90
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
33078-33153 6.08e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 44.32  E-value: 6.08e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 33078 KPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQAS--DEGNYSVVVENTDGK 33153
Cdd:cd05893       6 KLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTldDDGNYTIMAANPQGR 83
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
26327-26381 6.10e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 43.71  E-value: 6.10e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 26327 GRPLPVISWAKDGVEIEERAKTEIvSTDSntTLTVKDCVRRDTGQYVLTLKNVAG 26381
Cdd:cd05746       9 GDPEPTITWNKDGVQVTESGKFHI-SPEG--YLAIRDVGVADQGRYECVARNTIG 60
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
5996-6067 6.10e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.15  E-value: 6.10e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5996 LECVVAGTPELKVKWLKDGKQIVP-SRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRVL 6067
Cdd:cd05763      19 LECAATGHPTPQIAWQKDGGTDFPaARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATLTVL 91
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
21286-21369 6.11e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.99  E-value: 6.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21286 PDFELDAELRRTLVVRAGlsiRIFVPIK--GRPAPEVTWTKDNINLKHRANIENTESFTLLIIpECNRYDTGKFVMTIEN 21363
Cdd:cd04969       1 PDFELNPVKKKILAAKGG---DVIIECKpkASPKPTISWSKGTELLTNSSRICILPDGSLKIK-NVTKSDEGKYTCFAVN 76

                    ....*.
gi 1958765569 21364 PAGKKS 21369
Cdd:cd04969      77 FFGKAN 82
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
31448-31531 6.12e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.02  E-value: 6.12e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31448 NLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEfkGGYHQLIiaSVTDDDATVYQVRATNQGGSVSGTA 31527
Cdd:cd20952       8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLE--NGSLQIK--GAEKSDTGEYTCVALNLSGEATWSA 83

                    ....
gi 1958765569 31528 SLEV 31531
Cdd:cd20952      84 VLDV 87
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
5712-5787 6.13e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 44.26  E-value: 6.13e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5712 GQSTTFECQVTGTPEIR-VSWYLDGNEITDLRRYGISFV---DGLATFQISNARVENSGTYVCEARNDAGTAS-CSIELK 5786
Cdd:cd05865      15 GESKFFLCQVAGEAKDKdISWFSPNGEKLTPNQQRISVVrndDYSSTLTIYNANIDDAGIYKCVVSNEDEGESeATVNVK 94

                    .
gi 1958765569  5787 V 5787
Cdd:cd05865      95 I 95
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
7297-7374 6.14e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 44.16  E-value: 6.14e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7297 TQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNfdtSLHIFNLEAPDIGEYHCKATNEVGS 7374
Cdd:cd20968       3 TRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLESG---SLRIHNVQKEDAGQYRCVAKNSLGI 77
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4511-4570 6.14e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 43.73  E-value: 6.14e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4511 ITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAGssSSSATVAVR 4570
Cdd:cd05748      24 VTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG--EKSATINVK 81
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6370-6433 6.15e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 43.92  E-value: 6.15e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  6370 VSLECELSGTPPFEVVWYKDKRQLRSSKkYKIASKNfhaSIHILNVDSTDIGEYHCKAQNEVGS 6433
Cdd:cd05725      15 AEFQCEVGGDPVPTVRWRKEDGELPKGR-YEILDDH---SLKIRKVTAGDMGSYTCVAENMVGK 74
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
4313-4381 6.17e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.99  E-value: 6.17e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4313 CEIQGAPNVRFQWFKAGREIYESDKCSIRSSnyiSSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTV 4381
Cdd:cd04969      24 CKPKASPKPTISWSKGTELLTNSSRICILPD---GSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8332-8418 6.31e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.10  E-value: 6.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8332 KKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDkGEIVRESDNIWISHSEN-VATLHFSRAEPANAGKYTCQIKNDAGVQ 8410
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKD-DNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*...
gi 1958765569  8411 ECYATLSV 8418
Cdd:cd20973      81 TCSAELTV 88
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
5978-6066 6.31e-04

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 44.46  E-value: 6.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5978 QIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVAS---FRIQSV----MKQDSGQYTFK 6050
Cdd:cd07693       2 RIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRIVLPSgslFFLRVVhgrkGRSDEGVYVCV 81
                            90
                    ....*....|....*..
gi 1958765569  6051 VENDFGSS-SCDAYLRV 6066
Cdd:cd07693      82 AHNSLGEAvSRNASLEV 98
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
4680-4746 6.32e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.04  E-value: 6.32e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4680 RGANALLQCEVAGTGPFEVSWFKDKKQIRS-SKKYRLFTQKTfvFLEITSFNSADIGDYECVVANEVG 4746
Cdd:cd20970      16 EGENATFMCRAEGSPEPEISWTRNGNLIIEfNTRYIVRENGT--TLTIRNIRRSDMGIYLCIASNGVP 81
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
29967-30230 6.37e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.17  E-value: 6.37e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29967 TVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLANR-----AIIDNTE-SYSLLIVDkvnrYDAGKYTIEAEnqsgkkSA 30040
Cdd:COG4733     454 TVQSVAGRTLTVSTAYSETPEAGAVWAFGPDELETQlfrvvSIEENEDgTYTITAVQ----HAPEKYAAIDA------GA 523
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30041 TVLVKVYDTPGPCPSVNVKEVSRD-----SVTITWEIPTidggaPVNNYIIEKREAAMRAFKTVTTkcSKTLYRISGLVE 30115
Cdd:COG4733     524 FDDVPPQWPPVNVTTSESLSVVAQgtavtTLTVSWDAPA-----GAVAYEVEWRRDDGNWVSVPRT--SGTSFEVPGIYA 596
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30116 GTmYYFRVLPENIYGIGEPCETSDAVLVS---EVPLVPTKLEVVDVTKStVTLAWEKPLydgGSRLTGYVLEACKAGTER 30192
Cdd:COG4733     597 GD-YEVRVRAINALGVSSAWAASSETTVTgktAPPPAPTGLTATGGLGG-ITLSWSFPV---DADTLRTEIRYSTTGDWA 671
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1958765569 30193 WMKVVTLKPTVLDHTVISLNEGEQYLFRVRAQNEKGVS 30230
Cdd:COG4733     672 SATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNV 709
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
31054-31127 6.39e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 43.73  E-value: 6.39e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31054 VTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKM-SSDGRThTLTVMTEEQEDEGVYTCVATNEVGEVE 31127
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIeTTASST-SLVIKNAKRSDSGKYTLTLKNSAGEKS 75
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
20203-20295 6.42e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.99  E-value: 6.42e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20203 PEGELDAELRKTLILRAGvtmRLYVPVK--GRPPPKITWSKPNVNLREriGLDIKSTDfDTFLRCENVNKYDAGKYILTL 20280
Cdd:cd04969       1 PDFELNPVKKKILAAKGG---DVIIECKpkASPKPTISWSKGTELLTN--SSRICILP-DGSLKIKNVTKSDEGKYTCFA 74
                            90
                    ....*....|....*
gi 1958765569 20281 ENSCGKKEYTIVVKV 20295
Cdd:cd04969      75 VNFFGKANSTGSLSV 89
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
26089-26388 6.42e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 49.17  E-value: 6.42e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26089 AVVAEYPFSPPGPPGTPKVVHATKS-----------TMVVSWQVPVNdggsqVIGYHLEYKeRSSILWSKANKVliADTQ 26157
Cdd:COG4733     517 AAIDAGAFDDVPPQWPPVNVTTSESlsvvaqgtavtTLTVSWDAPAG-----AVAYEVEWR-RDDGNWVSVPRT--SGTS 588
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26158 MKVSGLDEGLlYEYRVYAENIAGIGKCSKACEPVPARDPCDPPgqPEVTNIT----RKSVSLKWSKPRYDGgakITGYIV 26233
Cdd:COG4733     589 FEVPGIYAGD-YEVRVRAINALGVSSAWAASSETTVTGKTAPP--PAPTGLTatggLGGITLSWSFPVDAD---TLRTEI 662
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26234 ERRELPDGRWLKCNFTNVQETYFEVTELTEDQRYEFRVFARNAADSVSEPsesTGPITVKDDVEAPRIMMDVKFRDVIVV 26313
Cdd:COG4733     663 RYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAW---WVSGQASADAAGILDAITGQILETELG 739
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26314 KAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEI------VSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAV 26387
Cdd:COG4733     740 QELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVAtaaaigAEARVAATVAESATAAAATGTAADAAGDASGGVTAGT 819

                    .
gi 1958765569 26388 N 26388
Cdd:COG4733     820 S 820
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
6084-6152 6.43e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 44.17  E-value: 6.43e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6084 KVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAG 6152
Cdd:cd05736      12 KEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
6636-6725 6.44e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 44.32  E-value: 6.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6636 PSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFS--DNVCTLQLNSLDSSDMGSYTCVAANV 6713
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRdlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  6714 AGSDECRALLTV 6725
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
5322-5411 6.46e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 44.37  E-value: 6.46e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5322 PSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITED-DNIRMTFEN-NVASLYLSGIEVKHDGKYVCQAKND 5399
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNtDRISLYQDNcGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  5400 AGIQRCSALLSV 5411
Cdd:cd05892      81 AGVVSCNARLDV 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
28085-28152 6.48e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.99  E-value: 6.48e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 28085 ISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEyvRFSKTENKiTLSIKNVKKENGGKYTVILDN 28152
Cdd:cd04969      12 ILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS--RICILPDG-SLKIKNVTKSDEGKYTCFAVN 76
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5621-5694 6.52e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 43.73  E-value: 6.52e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5621 VQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSNDVGTTSskATIFVK 5694
Cdd:cd05748      10 LRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS--ATINVK 81
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
5712-5787 6.54e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 43.77  E-value: 6.54e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5712 GQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYgisFVDGLATFQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRH---LVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
7203-7280 6.55e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 44.17  E-value: 6.55e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7203 IKKLDTSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVG 7280
Cdd:cd05736       3 IRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9003-9078 6.57e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.09  E-value: 6.57e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9003 GESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSA-----HLTIVKVDKGDSGQYTCYAINEVGKDSCTAQLN 9077
Cdd:cd20956      16 GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYVTSDgdvvsYVNISSVRVEDGGEYTCTATNDVGSVSHSARIN 95

                    .
gi 1958765569  9078 I 9078
Cdd:cd20956      96 V 96
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5883-5966 6.57e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.56  E-value: 6.57e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5883 PPSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNES 5962
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80

                    ....
gi 1958765569  5963 GVER 5966
Cdd:cd05762      81 GSRQ 84
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8163-8218 6.61e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.92  E-value: 6.61e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8163 CKIGGSPEIKVLWYKDEVEIQESSKFRMSfedsvailemhNLSVEDSGDYTCEARN 8218
Cdd:pfam13895    21 CSAPGNPPPSYTWYKDGSAISSSPNFFTL-----------SVSAEDSGTYTCVARN 65
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7669-7759 6.62e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 44.16  E-value: 6.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7669 PPSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELESGEAcTISLEDFVTELELLEVEPLQSGDYSCLVTNDA 7748
Cdd:cd20976       1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                            90
                    ....*....|.
gi 1958765569  7749 GSASCTTHLFV 7759
Cdd:cd20976      80 GQVSCSAWVTV 90
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
8328-8418 6.62e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 44.00  E-value: 6.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8328 PQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEIVRESDNIWISHSENVATLHFSRAEPANAGKYTCQIKNDA 8407
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569  8408 GVQECYATLSV 8418
Cdd:cd20975      81 GARQCEARLEV 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
25227-25310 6.62e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.92  E-value: 6.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25227 DVIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEEtaaRMEiKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIPI 25306
Cdd:cd20978       9 KNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG---PME-RATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTET 84

                    ....
gi 1958765569 25307 TVKV 25310
Cdd:cd20978      85 LLHV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13253-13330 6.62e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.03  E-value: 6.62e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  13253 KDIETMEKKSVTFWCKVN-RLNVTLKWTKNG-EEVAFDNRISYRIDKYKHSLIIKDCGFPDEGEYIVTA----GQDKSVA 13326
Cdd:smart00410     2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSGT 81

                     ....
gi 1958765569  13327 ELLI 13330
Cdd:smart00410    82 TLTV 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
30254-30341 6.65e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 44.27  E-value: 6.65e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30254 TMPQKTIHVPAGRPIELVIPITGRPPPTASWFFAG--SKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGT 30331
Cdd:cd20974       4 TQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQ 83
                            90
                    ....*....|
gi 1958765569 30332 TSETIKVVIL 30341
Cdd:cd20974      84 ATSTAELLVL 93
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
2063-2131 6.66e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 44.15  E-value: 6.66e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  2063 GKPDPECEWYKNGVKIERSDRIYWYwpEDNVCELVIRDVTAEDSASIMVKAINIAGETSSHAFLLVQAK 2131
Cdd:cd05730      29 GFPEPTMTWTKDGEPIESGEEKYSF--NEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFAK 95
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4480-4569 6.78e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 44.27  E-value: 6.78e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQ--KLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNE 4557
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|..
gi 1958765569  4558 AGSSSSSATVAV 4569
Cdd:cd20974      81 SGQATSTAELLV 92
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4762-4851 6.79e-04

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 44.18  E-value: 6.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4762 FVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMK-GQEVIKEDGKIKMSFS----SGVAVLTISDVQIGLGGKYTCLAEN 4836
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKeGSQNLLFPYQPPQPSSrfsvSPTGDLTITNVQRSDVGYYICQALN 81
                            90
                    ....*....|....*
gi 1958765569  4837 EAGSQTSVGELIVKE 4851
Cdd:cd05726      82 VAGSILAKAQLEVTD 96
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
33710-33787 6.79e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 44.15  E-value: 6.79e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 33710 NEGQNVLFSCEISGEPSPEIEWFKNNLPiSISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQCSATASLTV 33787
Cdd:cd05730      16 NLGQSVTLACDADGFPEPTMTWTKDGEP-IESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
3480-3550 6.81e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 44.16  E-value: 6.81e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  3480 LSVTVVGCPKPKIQWFFNGMLLTPSADyKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYGRAVCSAHLKV 3550
Cdd:cd20976      21 AQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
3461-3550 6.85e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.99  E-value: 6.85e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3461 PVFIKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTPSADYKFVFDGNN--HSLIILFTRFQDEGEYTCMASNE 3538
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCgrICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  3539 YGRAVCSAHLKV 3550
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33898-33979 6.85e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 43.92  E-value: 6.85e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWscggRRIQSQEQQGRFHIenTDDlTTLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:cd05725       4 PQNQVVLVDDSAEFQCEVGGDPVPTVRW----RKEDGELPKGRYEI--LDD-HSLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ..
gi 1958765569 33978 AT 33979
Cdd:cd05725      77 AS 78
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
104-187 6.89e-04

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 44.46  E-value: 6.89e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQ-----EGDLYSLLI--AEAYPEDSGTYSV 176
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHrivlpSGSLFFLRVvhGRKGRSDEGVYVC 80
                            90
                    ....*....|.
gi 1958765569   177 NATNSVGRATS 187
Cdd:cd07693      81 VAHNSLGEAVS 91
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
8797-8886 6.89e-04

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 44.08  E-value: 6.89e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYK---GDTKL--RPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRA 8871
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKqvpGKENLimRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTA 80
                            90
                    ....*....|....*
gi 1958765569  8872 ENSVGEVSSSTFLTV 8886
Cdd:cd05765      81 RNSGGLLRANFPLSV 95
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
3468-3543 6.90e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.04  E-value: 6.90e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  3468 SDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLTpSADYKFVFDGNNHSLIILFTRFQDEGEYTCMASNEYGRAV 3543
Cdd:cd20970      10 FTVTAREGENATFMCRAEGSPEPEISWTRNGNLII-EFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGVPGSV 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2245-2299 6.95e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.47  E-value: 6.95e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  2245 ELECIIS-PENIEGKWYHNDVELKSNGKYSITSRRGRQNLTVKDVTKEDQGEY-CFV 2299
Cdd:cd00096       2 TLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYtCVA 58
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
11631-11719 6.95e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.10  E-value: 6.95e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11631 KEIKDIVLTEaesvGSSAIFECLVS--PSTAITtWMKDGSNIRESPKHRFIADGKDR-KLHIIDVQLSDAGEYTCVLRLG 11707
Cdd:cd20973       2 QTLRDKEVVE----GSAARFDCKVEgyPDPEVK-WMKDDNPIVESRRFQIDQDEDGLcSLIISDVCGDDSGKYTCKAVNS 76
                            90
                    ....*....|..
gi 1958765569 11708 NKEKTSTAKLIV 11719
Cdd:cd20973      77 LGEATCSAELTV 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
3577-3667 6.99e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.99  E-value: 6.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3577 PYFLKELKPVHCAPGIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIIHNpDGSG--TFIVNDPQRGDSGLYICKAEN 3654
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQ-DNCGriCLLIQNANKKDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569  3655 LWGTSTCTAELLV 3667
Cdd:cd05892      80 EAGVVSCNARLDV 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
4390-4476 7.02e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.04  E-value: 7.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4390 LSRPKSLTTFVGKAAKFLC-TVSGTPVIETIWQKDGTALSPSPDCRITDADNKHS--LELSNLTVQDRGVYSCKASNKFG 4466
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLKCeATSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNseLQINKAKLEDSGEYTCVVENILG 82
                            90
                    ....*....|
gi 1958765569  4467 ADICQAELTI 4476
Cdd:cd05750      83 KDTVTGNVTV 92
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
19412-19500 7.02e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 44.08  E-value: 7.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19412 PKILM--PEQITIKAGKKLRVEAHVYGKPNPICKWKKGedDVVTSSHLAIHKadSSSVLIIKDVTRKDSGYYSLTAENSS 19489
Cdd:cd04968       1 PSIKVrfPADTYALKGQTVTLECFALGNPVPQIKWRKV--DGSPSSQWEITT--SEPVLEIPNVQFEDEGTYECEAENSR 76
                            90
                    ....*....|.
gi 1958765569 19490 GTDTQKIKVTV 19500
Cdd:cd04968      77 GKDTVQGRIIV 87
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
1690-1748 7.02e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 44.13  E-value: 7.02e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  1690 GDPTMVVEWLHDGKPLEAANRLRLI-NEFGYCSLDYEAAYSRDSGVITCRATNKYGT-DHT 1748
Cdd:cd05729      30 GNPMPNITWLKDGKEFKKEHRIGGTkVEEKGWSLIIERAIPRDKGKYTCIVENEYGSiNHT 90
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
6072-6166 7.04e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.17  E-value: 7.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6072 PPSFTKKLTKMDKVLGSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVA 6151
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*
gi 1958765569  6152 GDNACSGILTVKEPP 6166
Cdd:cd05762      81 GSRQAQVNLTVVDKP 95
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
19818-19897 7.06e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 43.92  E-value: 7.06e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19818 TVKAGTNVCLDATVFGKPMPTVSWKKD--STPIKQTEgvkmamKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKL 19895
Cdd:cd05725       8 VVLVDDSAEFQCEVGGDPVPTVRWRKEdgELPKGRYE------ILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATL 81

                    ..
gi 1958765569 19896 KV 19897
Cdd:cd05725      82 TV 83
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
3025-3091 7.07e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.93  E-value: 7.07e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3025 KDIKVLEKKRAMFECE--VSEPDITVQWMKDGQELQIVD-RIKIQKEKyvhRLLIPSARMSDAGKYTVVA 3091
Cdd:cd05724       5 SDTQVAVGEMAVLECSppRGHPEPTVSWRKDGQPLNLDNeRVRIVDDG---NLLIAEARKSDEGTYKCVA 71
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
33604-33674 7.10e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 43.71  E-value: 7.10e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 33604 EIKALSTQMNITSGQRVTLKANIAG--ATDVKWVLNGTELSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCI 33674
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEATGspPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
13334-13406 7.11e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.11  E-value: 7.11e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 13334 PTEFVEHLEDQTVTEFDDAVFSCQLS-REKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLEDECEYAC 13406
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTgNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSC 74
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7311-7378 7.13e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 43.32  E-value: 7.13e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7311 VILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFdtsLHIFNLEAPDIGEYHCKATNEVGSDTCA 7378
Cdd:cd05746       1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEGY---LAIRDVGVADQGRYECVARNTIGYASVS 65
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
22670-22742 7.16e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.02  E-value: 7.16e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLK-QTTRVnaeSTENNSLLTIKEACREDVGHYTVKLTNSAGEAT 22742
Cdd:cd20952      10 TVAVGGTVVLNCQATGEPVPTISWLKDGVPLLgKDERI---TTLENGSLQIKGAEKSDTGEYTCVALNLSGEAT 80
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7580-7666 7.16e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.04  E-value: 7.16e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7580 IRKLKDTTATLGASVVLECRVSGSAP-ISVGWFLDGNEI-------ISSPKCQPSfadnvCTLTLSSLEPSDTGAYTCVA 7651
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLKCEATSENPsPRYRWFKDGKELnrkrpknIKIRNKKKN-----SELQINKAKLEDSGEYTCVV 77
                            90
                    ....*....|....*
gi 1958765569  7652 ANVAGQDESSALLTV 7666
Cdd:cd05750      78 ENILGKDTVTGNVTV 92
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
8893-8976 7.16e-04

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 44.46  E-value: 7.16e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8893 PSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPL---KDSPNVQTSFLDNiATLNIFKT-----DRSLAGQYS 8964
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLetdKDDPRSHRIVLPS-GSLFFLRVvhgrkGRSDEGVYV 79
                            90
                    ....*....|..
gi 1958765569  8965 CTVTNPIGSASS 8976
Cdd:cd07693      80 CVAHNSLGEAVS 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
33076-33162 7.19e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 43.94  E-value: 7.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33076 LTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYK-STFEISSVQASDEGNYSVVVENTDGKQ 33154
Cdd:cd20990       4 LQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGvHSLIIEPVTSRDAGIYTCIATNRAGQN 83

                    ....*...
gi 1958765569 33155 EAQFTLTV 33162
Cdd:cd20990      84 SFNLELVV 91
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
4680-4746 7.19e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 43.72  E-value: 7.19e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4680 RGANALLQCEV-AGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVF-LEITSFNSADIGDYECVVANEVG 4746
Cdd:pfam00047    10 EGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSsLLISNVTKEDAGTYTCVVNNPGG 78
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
1807-1879 7.20e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 43.98  E-value: 7.20e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd04978       6 PPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
5231-5305 7.20e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.86  E-value: 7.20e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5231 FTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRVTN 5305
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQ 76
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7969-8039 7.24e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.04  E-value: 7.24e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  7969 VAFECRINGSEPLQVSWYKDGQLLKdDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPL-GTASSSAKL 8039
Cdd:cd20970      20 ATFMCRAEGSPEPEISWTRNGNLII-EFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGVpGSVEKRITL 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
3203-3286 7.26e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 43.72  E-value: 7.26e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3203 QELQPVTVQSGKPARF-CAVIAGRPQPKISWYKEEQLLSTGFKcKFLHDGQEY--TLLLIEAFPEDAAVYTCEAKNDYGV 3279
Cdd:pfam00047     1 SAPPTVTVLEGDSATLtCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTqsSLLISNVTKEDAGTYTCVVNNPGGS 79

                    ....*..
gi 1958765569  3280 ATTSASL 3286
Cdd:pfam00047    80 ATLSTSL 86
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
7487-7570 7.27e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.13  E-value: 7.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7487 PEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSgSRHHITFVRN--LASLKIPSAEMNDKGLYSFEVENSVGKSSC 7564
Cdd:cd05891       8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIEL-SEHYSVKLEQgkYASLTIKGVTSEDSGKYSINVKNKYGGETV 86

                    ....*.
gi 1958765569  7565 TVSVHV 7570
Cdd:cd05891      87 DVTVSV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
18444-18510 7.30e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 44.16  E-value: 7.30e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 18444 VKGRPEPDITWSKEGKVLVKDK-RVDLihDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVNV 18510
Cdd:cd20976      25 ARGKPVPRITWIRNAQPLQYAAdRSTC--EAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
5233-5318 7.31e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 44.21  E-value: 7.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5233 KEFKSIEVLKEYDVMLLAE-VAGTPPFEITWFKDNTTL-RSGRKYKTFIQDQLVS--LQILKFVASDAGEYQCRVTNEVG 5308
Cdd:cd05895       4 KEMKSQEVAAGSKLVLRCEtSSEYPSLRFKWFKNGKEInRKNKPENIKIQKKKKKseLRINKASLADSGEYMCKVSSKLG 83
                            90
                    ....*....|
gi 1958765569  5309 SSTCSARVTL 5318
Cdd:cd05895      84 NDSASANVTI 93
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
9292-9380 7.34e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.99  E-value: 7.34e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRILIHQKG-DESKLEIRDTTKTDSGLYRCVAFNKHG 9370
Cdd:cd05892       3 FIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNcGRICLLIQNANKKDAGWYTVSAVNEAG 82
                            90
                    ....*....|
gi 1958765569  9371 EIESNVNLQV 9380
Cdd:cd05892      83 VVSCNARLDV 92
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
5993-6066 7.36e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 43.75  E-value: 7.36e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5993 PVTLECVVAGTPELKVKWLKDGKQIVPSRyfsMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRV 6066
Cdd:cd05876      12 SLVLECIAEGLPTPTVKWLRPSGPLPPDR---VKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
14899-14994 7.39e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.17  E-value: 7.39e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14899 PTIDLETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLG 14978
Cdd:cd05762       2 PQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLG 81
                            90
                    ....*....|....*.
gi 1958765569 14979 SATASINVKVIGLPGP 14994
Cdd:cd05762      82 SRQAQVNLTVVDKPDP 97
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
23752-23829 7.39e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 43.77  E-value: 7.39e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23752 SVQVGQDLKIEVPIS--GRPKPSISWTKDGAPLKQTTRINVIDSldlTTLSIKETHKDDGGHYGITVANVVG---QKTAA 23826
Cdd:cd20968       8 NVTIIEGLKAVLPCTtmGNPKPSVSWIKGDDLIKENNRIAVLES---GSLRIHNVQKEDAGQYRCVAKNSLGiaySKPVT 84

                    ...
gi 1958765569 23827 IEI 23829
Cdd:cd20968      85 IEV 87
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
28090-28159 7.41e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.02  E-value: 7.41e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 28090 GHNVHLELPYKGKPKPSISWLKDGLPLKE-SEYVRFSKTENKITLSIKNVKKENGGKYTVILDNAVCRNSF 28159
Cdd:cd05744      15 GRLCRFDCKVSGLPTPDLFWQLNGKPVRPdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSF 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
33899-33984 7.48e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 44.27  E-value: 7.48e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33899 SDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIqSQEQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDSA 33978
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVI-STSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86

                    ....*.
gi 1958765569 33979 TVNINI 33984
Cdd:cd20974      87 TAELLV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
29574-29649 7.51e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 43.78  E-value: 7.51e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29574 GSDLVLDAAVGGKPEPKIIWTKGDKEldlcekvsLQYTGKRATA-------VIKYCDRSDSGKYTLTVKNASGTKSVSVM 29646
Cdd:cd20976      16 GQDFVAQCSARGKPVPRITWIRNAQP--------LQYAADRSTCeagvgelHIQDVLPEDHGTYTCLAKNAAGQVSCSAW 87

                    ...
gi 1958765569 29647 VKV 29649
Cdd:cd20976      88 VTV 90
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7764-7853 7.55e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 43.88  E-value: 7.55e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7764 TFVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNE--YPLSQSPNCGITTTERSSILEILESTIEDYAQYACLIENEA 7841
Cdd:cd20974       2 VFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|..
gi 1958765569  7842 GQDICEALVSVL 7853
Cdd:cd20974      82 GQATSTAELLVL 93
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
19411-19493 7.55e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.99  E-value: 7.55e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19411 PPKILMPEQITIKAGKKLRVEAHVYGKPNPICKWKKgEDDVVT--SSHLAIHKADSSSV-LIIKDVTRKDSGYYSLTAEN 19487
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKK-NNEMLQynTDRISLYQDNCGRIcLLIQNANKKDAGWYTVSAVN 79

                    ....*.
gi 1958765569 19488 SSGTDT 19493
Cdd:cd05892      80 EAGVVS 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4864-4942 7.59e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.72  E-value: 7.59e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4864 VTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNN-IAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTV 4942
Cdd:cd20973       9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4480-4569 7.63e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.02  E-value: 7.63e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYF-EDKIASLEIPLAKLKDSGTYSCTASNEA 4558
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVrENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  4559 GSSSSSATVAV 4569
Cdd:cd05744      81 GENSFNAELVV 91
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
6370-6433 7.65e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 43.39  E-value: 7.65e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  6370 VSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKnfhASIHILNVDSTDIGEYHCKAQNEVGS 6433
Cdd:cd05745       5 VDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS---GTLRISRVALHDQGQYECQAVNIVGS 65
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
6548-6629 7.72e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 43.68  E-value: 7.72e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6548 SMTVTVGETCSLECKVAGTPELSVEWYKDGKLLTSSQ-KHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAV 6626
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                    ...
gi 1958765569  6627 VDV 6629
Cdd:cd05894      84 VKV 86
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
6456-6536 7.74e-04

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 44.08  E-value: 7.74e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6456 TVVAGEPAELQASIEGAPPISVHWLKE---KEEVVRESENVRISFV-NNVATLQFAKAEPANAGKYICQVKNDGGVRENM 6531
Cdd:cd05765      11 TVKVGETASFHCDVTGRPQPEITWEKQvpgKENLIMRPNHVRGNVVvTNIGQLVIYNAQPQDAGLYTCTARNSGGLLRAN 90

                    ....*
gi 1958765569  6532 ASLTV 6536
Cdd:cd05765      91 FPLSV 95
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
19142-19200 7.74e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.47  E-value: 7.74e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19142 VRGRPAPKVTWRKVGIDNVVRKGQVDLVDTM-AFLVIPNSTRDDSGKYSLTLVNPAGEKA 19200
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLPPSSRDSRRSELGnGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
24546-24611 7.75e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 43.71  E-value: 7.75e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 24546 IVVRAGGSARIHIPFKGRPTPEITWSKEEGEFTDKVQIEKGINFTQ--LSIDNCDRNDAGKYILKLEN 24611
Cdd:pfam13927    11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNstLTISNVTRSDAGTYTCVASN 78
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
9098-9166 7.81e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.54  E-value: 7.81e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9098 TEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNceitfknnallLQVKKASMADAGLYTCKATNDAGS 9166
Cdd:pfam13895    12 TEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN-----------FFTLSVSAEDSGTYTCVARNGRGG 69
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
23742-23823 7.81e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 44.00  E-value: 7.81e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23742 PDVRPAFSSYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLD-LTTLSIKETHKDDGGHYGITVANVV 23820
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGgLCRLRILAAERGDAGFYTCKAVNEY 80

                    ...
gi 1958765569 23821 GQK 23823
Cdd:cd20975      81 GAR 83
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
33892-33982 7.82e-04

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 44.08  E-value: 7.82e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENTDDlTTLIIMDV-----QKQDGGLYT 33966
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRIVLPS-GSLFFLRVvhgrkGRSDEGVYV 79
                            90
                    ....*....|....*....
gi 1958765569 33967 LSLGNEFG---SDSATVNI 33982
Cdd:cd07693      80 CVAHNSLGeavSRNASLEV 98
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
22378-22460 7.84e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 44.12  E-value: 7.84e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22378 LRKVVTIRACCTLRLFVPIKGRPAPEVKWAREHG--ESLDKASIE-STSSYTLLVVGNVNRFDSGKYILTVENSSGSKSA 22454
Cdd:cd05737       7 LPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQalAFLDHCNLKvEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETS 86

                    ....*.
gi 1958765569 22455 FVNVRV 22460
Cdd:cd05737      87 DVTVSV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
9670-9757 7.86e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 44.15  E-value: 7.86e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9670 IQFTKRIQNIVVSEHQSATFECEVS-FDDAIVTWYKG--PTElTESQKYNFRNDGRchYMTIHNVTPDDEGVYSVIARlE 9746
Cdd:cd05730       4 IRARQSEVNATANLGQSVTLACDADgFPEPTMTWTKDgePIE-SGEEKYSFNEDGS--EMTILDVDKLDEAEYTCIAE-N 79
                            90
                    ....*....|.
gi 1958765569  9747 PRGEARSTAEL 9757
Cdd:cd05730      80 KAGEQEAEIHL 90
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8532-8607 7.87e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 43.39  E-value: 7.87e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8532 GSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTltdNTCALTVNMLEDADAGDYTCIATNVAGSDECSAPLTV 8607
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVL---SSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
5985-6066 7.94e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 43.55  E-value: 7.94e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5985 SVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFsmsFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYL 6064
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTK---FENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISV 80

                    ..
gi 1958765569  6065 RV 6066
Cdd:cd05731      81 TV 82
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
129-191 8.03e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 43.32  E-value: 8.03e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569   129 GIPTPVVKFYRDGAEIQSSLDFQISQEGdlySLLIAEAYPEDSGTYSVNATNSVGRATSTADL 191
Cdd:cd05746       9 GDPEPTITWNKDGVQVTESGKFHISPEG---YLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
5329-5413 8.05e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.79  E-value: 8.05e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5329 ETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSAL 5408
Cdd:cd05736       8 EFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISS 87

                    ....*
gi 1958765569  5409 LSVKE 5413
Cdd:cd05736      88 LFVED 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5516-5600 8.05e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.04  E-value: 8.05e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5516 KLRKMDS---IKGSFIDLECIVAGSHP-ISIQWFKDDQEI--SASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKA 5589
Cdd:cd05750       2 KLKEMKSqtvQEGSKLVLKCEATSENPsPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENIL 81
                            90
                    ....*....|.
gi 1958765569  5590 GHSQCSGHLTV 5600
Cdd:cd05750      82 GKDTVTGNVTV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
31540-31630 8.09e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.02  E-value: 8.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31540 PKTLEGMGAVHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFT-SLVFPNgVERKDAGFYVVCAKNR 31618
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRhSLIIEP-VTKRDAGIYTCIARNR 79
                            90
                    ....*....|..
gi 1958765569 31619 FGIDQKTVELDV 31630
Cdd:cd05744      80 AGENSFNAELVV 91
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
5042-5133 8.12e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.79  E-value: 8.12e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5042 PSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEASESSLELYAVKTTDSGTYTCKVSNVAG 5121
Cdd:cd05736       1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
                            90
                    ....*....|..
gi 1958765569  5122 SVECSANLFVKE 5133
Cdd:cd05736      81 VDEDISSLFVED 92
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7855-7941 8.14e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.09  E-value: 8.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7855 PPYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDV-----GEYTCK 7929
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYVTSDGDVVSYVNISSVrvedgGEYTCT 80
                            90
                    ....*....|..
gi 1958765569  7930 AENSVGAVASSA 7941
Cdd:cd20956      81 ATNDVGSVSHSA 92
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
5049-5131 8.14e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 43.83  E-value: 8.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5049 ESRDVLPGSAVCLKSAFQGSTP-LTIRWFKGDKELVSGG---SCYITKEASESSLELYAVKTTDSGTYTCKVSNVAGSVE 5124
Cdd:cd05895       7 KSQEVAAGSKLVLRCETSSEYPsLRFKWFKNGKEINRKNkpeNIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDS 86

                    ....*..
gi 1958765569  5125 CSANLFV 5131
Cdd:cd05895      87 ASANVTI 93
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
6537-6629 8.17e-04

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 43.77  E-value: 8.17e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6537 LEPAVIVEKAGSMTVTvgetcsleCKVAGtPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYtfqvQN 6616
Cdd:cd20967       3 AQPAVQVSKGHKIRLT--------VELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEY----QC 69
                            90
                    ....*....|...
gi 1958765569  6617 NVGKSSCTAVVDV 6629
Cdd:cd20967      70 VAGGEKCSFELFV 82
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
23756-23826 8.19e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 43.39  E-value: 8.19e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 23756 GQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSldlTTLSIKETHKDDGGHYGITVANVVG-QKTAA 23826
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS---GTLRISRVALHDQGQYECQAVNIVGsQRTVA 70
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
1051-1127 8.19e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 43.39  E-value: 8.19e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  1051 EGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVsynKQTGECRlvISMTFADDAGEYTIVIRNKHGETSASASL 1127
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLV---LSSGTLR--ISRVALHDQGQYECQAVNIVGSQRTVAQL 72
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
7208-7282 8.19e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 43.75  E-value: 8.19e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  7208 TSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEasvEDTGDYICEAHNGVGHA 7282
Cdd:cd05876       3 SSLVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNKTLQLLNVGE---SDDGEYVCLAENSLGSA 74
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
26702-26786 8.20e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 43.78  E-value: 8.20e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26702 SEMRKTLTVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRTS-LTIENANRNDSGKYTLTIQNVLSAASM 26780
Cdd:cd20976       5 SSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVGeLHIQDVLPEDHGTYTCLAKNAAGQVSC 84

                    ....*.
gi 1958765569 26781 TFVVKV 26786
Cdd:cd20976      85 SAWVTV 90
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
8327-8408 8.24e-04

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 43.84  E-value: 8.24e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8327 PPQFVKKLSDVSTIIGKEVQLQTTIEGAEPISVAWFKDKGEI------VRESDNIwisHSENVATLHFSRAEPANAGKYT 8400
Cdd:cd20954       1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKATGSTpgeykdLLYDPNV---RILPNGTLVFGHVQKENEGHYL 77

                    ....*...
gi 1958765569  8401 CQIKNDAG 8408
Cdd:cd20954      78 CEAKNGIG 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7577-7666 8.25e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.99  E-value: 8.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7577 PSFIRKLKDTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNV--CTLTLSSLEPSDTGAYTCVAANV 7654
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCgrICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  7655 AGQDESSALLTV 7666
Cdd:cd05892      81 AGVVSCNARLDV 92
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
31059-31124 8.25e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 43.55  E-value: 8.25e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRFGKELvQSRKYKMSSDGRTHTLTVMTEeqEDEGVYTCVATNEVG 31124
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIKLGGEL-PKGRTKFENFNKTLKIENVSE--ADSGEYQCTASNTMG 72
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
33898-33984 8.26e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.86  E-value: 8.26e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRI-QSQEQQGRFHIeNTDDLTtliIMDVQKQDGGLYTLSLGNEFGSD 33976
Cdd:cd20949       6 AYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPIsASVADMSKYRI-LADGLL---INKVTQDDTGEYTCRAYQVNSIA 81

                    ....*...
gi 1958765569 33977 SATVNINI 33984
Cdd:cd20949      82 SDMQERTV 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
3602-3667 8.27e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.54  E-value: 8.27e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  3602 GEPAPTVLWFKEDMPL-YTNVCYTIIHNpdgsGTFIVNDPQRGDSGLYICKAENLWGT-STCTAELLV 3667
Cdd:cd05724      24 GHPEPTVSWRKDGQPLnLDNERVRIVDD----GNLLIAEARKSDEGTYKCVATNMVGErESRAARLSV 87
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
1429-1507 8.31e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 43.73  E-value: 8.31e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  1429 LEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDSGEWTVVAQNRAGKSTISVTLTV 1507
Cdd:cd05737      14 MEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
14907-14988 8.31e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 43.73  E-value: 8.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14907 DIVVI-EGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHIS-AHLEVPKSVHADAGVYTITLENKLGSATASI 14984
Cdd:cd05737       9 DVVTImEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRtVYFTINGVSSEDSGKYGLVVKNKYGSETSDV 88

                    ....
gi 1958765569 14985 NVKV 14988
Cdd:cd05737      89 TVSV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8611-8700 8.33e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.99  E-value: 8.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8611 PSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWfKGSSELVPGARCNVSL-QDSVAELELF--DVDTSQSGDYTCIVSN 8687
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFW-KKNNEMLQYNTDRISLyQDNCGRICLLiqNANKKDAGWYTVSAVN 79
                            90
                    ....*....|...
gi 1958765569  8688 EAGRASCTTQLFV 8700
Cdd:cd05892      80 EAGVVSCNARLDV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
18428-18510 8.33e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 43.74  E-value: 8.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18428 DVITVRVGQTIRILARVKGRPEPDITWSKEGKVL-VKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIeLSEHYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDV 88

                    ....
gi 1958765569 18507 IVNV 18510
Cdd:cd05891      89 TVSV 92
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
23764-23826 8.35e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.54  E-value: 8.35e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 23764 PISGRPKPSISWTKDGAPLK-QTTRINVidsLDLTTLSIKETHKDDGGHYGITVANVVGQKTAA 23826
Cdd:cd05724      21 PPRGHPEPTVSWRKDGQPLNlDNERVRI---VDDGNLLIAEARKSDEGTYKCVATNMVGERESR 81
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
19813-19897 8.35e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.60  E-value: 8.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19813 MKSLLTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRnlcTLELFSVNRKDSGDYTITAENSSGSKSAT 19892
Cdd:cd04969       8 VKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDG---SLKIKNVTKSDEGKYTCFAVNFFGKANST 84

                    ....*
gi 1958765569 19893 IKLKV 19897
Cdd:cd04969      85 GSLSV 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8705-8794 8.41e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 43.88  E-value: 8.41e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8705 IFVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNG--VNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENAS 8782
Cdd:cd20974       2 VFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                            90
                    ....*....|..
gi 1958765569  8783 GKDSCSAQILIL 8794
Cdd:cd20974      82 GQATSTAELLVL 93
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
30660-30736 8.45e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 43.64  E-value: 8.45e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 30660 VRQGGVIRLTIPIKGKPFPICKWTKEGQDVSKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVKV 30736
Cdd:cd20952      11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
4588-4658 8.45e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 43.64  E-value: 8.45e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTvRMsFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCS 4658
Cdd:cd20952      14 GGTVVLNCQATGEPVPTISWLKDGVPLLGKDE-RI-TTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWS 82
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
8624-8702 8.59e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.77  E-value: 8.59e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8624 TGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARcNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAGRASCTTQLFVKA 8702
Cdd:cd05730      17 LGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFA 94
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
11644-11719 8.60e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.54  E-value: 8.60e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11644 VGSSAIFEClvSPSTAI----TTWMKDGSNIRESPKHRFIADGKdrKLHIIDVQLSDAGEYTCVLR--LGNKEkTSTAKL 11717
Cdd:cd05724      11 VGEMAVLEC--SPPRGHpeptVSWRKDGQPLNLDNERVRIVDDG--NLLIAEARKSDEGTYKCVATnmVGERE-SRAARL 85

                    ..
gi 1958765569 11718 IV 11719
Cdd:cd05724      86 SV 87
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
9016-9076 8.65e-04

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 43.87  E-value: 8.65e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  9016 QPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQL 9076
Cdd:cd20927      28 QSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAEL 88
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
4499-4556 8.74e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 43.72  E-value: 8.74e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4499 LECQVDEDRK-VSITWSKDGQKLPAGKDYKIYFEDK-IASLEIPLAKLKDSGTYSCTASN 4556
Cdd:pfam00047    16 LTCSASTGSPgPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNN 75
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5604-5694 8.75e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.95  E-value: 8.75e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5604 PYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHP---GAARSVWKDDTSTILELFSAKAADSGTYICQLSN 5680
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  5681 DVGTTSSKATIFVK 5694
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
15921-16006 8.75e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.95  E-value: 8.75e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15921 KVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKptdALNITKEEVSRSEAKTELSIPKAVREDKGTYTITASNRLGSVFR 16000
Cdd:cd20951      11 TVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDP---SSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASS 87

                    ....*.
gi 1958765569 16001 NVHVEV 16006
Cdd:cd20951      88 SASVVV 93
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
10804-11016 8.81e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 48.69  E-value: 8.81e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10804 KKEAPPAKVPEIPKKPEEKVSVPVPKKEKAPPAKVPEVPKKPVPEEKAPVPVPKKVEPPPAKVPEVPKKPVPekkVPAPT 10883
Cdd:PRK07003    379 AVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVP---AKANA 455
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10884 PKKVEAPPAKAPEVPPKEVtpekkvpVVPPKKPEAPPPKVPEPPKEVVPEKKVSMVPPKRPEAPPAKVPEASkevVPEKK 10963
Cdd:PRK07003    456 RASADSRCDERDAQPPADS-------GSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASRED---APAAA 525
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10964 VSVAPKKKPEAPAVKVP---------------EAPKKVVPEKKVPVAAPKKPEA--PAAEVPEVPKAAVP 11016
Cdd:PRK07003    526 APPAPEARPPTPAAAAPaaraggaaaaldvlrNAGMRVSSDRGARAAAAAKPAAapAAAPKPAAPRVAVQ 595
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
27399-27474 8.83e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 43.64  E-value: 8.83e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 27399 GTSVKLRAGISGKPEPTIEWYKDDKELQTNA-LVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRVQI 27474
Cdd:cd05744      15 GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSaHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
7969-8041 8.88e-04

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 43.72  E-value: 8.88e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  7969 VAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQshvGQYNCSASNPLGTASSSAKLIL 8041
Cdd:cd05723      15 IVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKSDE---GFYQCIAENDVGNAQASAQLII 84
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
17745-17818 8.89e-04

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 43.86  E-value: 8.89e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 17745 GDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDVTpvGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd05851      16 GQNVTLECFALGNPVPVIRWRKILEPMPATAEISMS--GAVLKIFNIQPEDEGTYECEAENIKGKDKHQARVYV 87
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
5980-6059 8.93e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.86  E-value: 8.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5980 IEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSS 6059
Cdd:cd20949       3 TENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
6456-6526 8.98e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 43.92  E-value: 8.98e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  6456 TVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESENVRISFVNNvATLQFAKAEPANAGKYICQVKNDGG 6526
Cdd:cd20969      13 FVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPD-GTLEVRYAQVQDNGTYLCIAANAGG 82
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
19804-19887 9.07e-04

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 43.86  E-value: 9.07e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19804 PPRIelSVEMKSLLTVKaGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMkrnlCTLELFSVNRKDSGDYTITAE 19883
Cdd:cd05851       1 PADI--NVKFKDTYALK-GQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSG----AVLKIFNIQPEDEGTYECEAE 73

                    ....
gi 1958765569 19884 NSSG 19887
Cdd:cd05851      74 NIKG 77
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7011-7098 9.09e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 43.88  E-value: 9.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDG--VLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNP 7088
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|
gi 1958765569  7089 LGTASSTARL 7098
Cdd:cd20974      81 SGQATSTAEL 90
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33087-33162 9.09e-04

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 44.02  E-value: 9.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33087 GESARFSCD-TDGEPVPTVTWLRGGQVVSTSarHQVTTAK---YKSTFEISSVQASDEGNYSVVVENTDGkqEAQFT--L 33160
Cdd:cd20959      17 GMRAQLHCGvPGGDLPLNIRWTLDGQPISDD--LGITVSRlgrRSSILSIDSLEASHAGNYTCHARNSAG--SASYTapL 92

                    ..
gi 1958765569 33161 TV 33162
Cdd:cd20959      93 TV 94
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
32227-32293 9.12e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.54  E-value: 9.12e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 32227 HPEPRVTWYKSGQKIKpgDDDKKYTFESDKglyQLTINSVTTDDDAEYAVVARNKHGE-DSCKAKLTV 32293
Cdd:cd05724      25 HPEPTVSWRKDGQPLN--LDNERVRIVDDG---NLLIAEARKSDEGTYKCVATNMVGErESRAARLSV 87
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
31066-31132 9.12e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.60  E-value: 9.12e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31066 CQIVGRPLPDIKWYRFGKELVQSRKYKMSSDGrthTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:cd04969      24 CKPKASPKPTISWSKGTELLTNSSRICILPDG---SLKIKNVTKSDEGKYTCFAVNFFGKANSTGSL 87
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
6925-7001 9.14e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 43.88  E-value: 9.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6925 EASVGDSVSLQCQVAGTPEIT-VSWFKGDTKLRSTPEYRTYFTNN---VATLVFNKVGINDSGEYTCVAENSIGTAASKT 7000
Cdd:cd05865      11 EISVGESKFFLCQVAGEAKDKdISWFSPNGEKLTPNQQRISVVRNddySSTLTIYNANIDDAGIYKCVVSNEDEGESEAT 90

                    .
gi 1958765569  7001 V 7001
Cdd:cd05865      91 V 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
21971-22070 9.16e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.17  E-value: 9.16e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21971 PRImvdVKFKDTITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATN 22050
Cdd:cd05762       2 PQI---IQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVEN 78
                            90       100
                    ....*....|....*....|
gi 1958765569 22051 PGGFAKHIFNVKVLDRPGPP 22070
Cdd:cd05762      79 KLGSRQAQVNLTVVDKPDPP 98
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6915-6998 9.18e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 43.88  E-value: 9.18e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFK-GD-TKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVAENS 6992
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRdGQvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80

                    ....*.
gi 1958765569  6993 IGTAAS 6998
Cdd:cd20974      81 SGQATS 86
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
30262-30340 9.19e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.95  E-value: 9.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30262 VPAGRPIELVIPITGRPPPTASWF---FAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKV 30338
Cdd:cd20951      12 VWEKSDAKLRVEVQGKPDPEVKWYkngVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASV 91

                    ..
gi 1958765569 30339 VI 30340
Cdd:cd20951      92 VV 93
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7118-7196 9.22e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 43.65  E-value: 9.22e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7118 VIAGESADFECHVTGAQP-MRVTWSKDNKEIRPGGNYTITcVGNTP---HLRILKVGKGDSGQYTCQATNDVGKDMCSAQ 7193
Cdd:cd05750      11 VQEGSKLVLKCEATSENPsPRYRWFKDGKELNRKRPKNIK-IRNKKknsELQINKAKLEDSGEYTCVVENILGKDTVTGN 89

                    ...
gi 1958765569  7194 LSV 7196
Cdd:cd05750      90 VTV 92
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
8245-8324 9.25e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 43.83  E-value: 9.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8245 ETLKGADVHLECELQGT-PPFQVSWYKDKRELRSGKK---YKIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDTCVG 8320
Cdd:cd05895      10 EVAAGSKLVLRCETSSEyPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSASA 89

                    ....
gi 1958765569  8321 SVTL 8324
Cdd:cd05895      90 NVTI 93
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
5134-5217 9.25e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 43.92  E-value: 9.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5134 PATFTEKLEPSQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNE 5213
Cdd:cd20969       1 RAAIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANA 80

                    ....
gi 1958765569  5214 AGSD 5217
Cdd:cd20969      81 GGND 84
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
25227-25310 9.26e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 43.73  E-value: 9.26e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25227 DVIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETA-ARMEIKSTlQKTTLTVKDCIRTDGGQYTLKLSNVGGTKTIP 25305
Cdd:cd05737       9 DVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDhCNLKVEAG-RTVYFTINGVSSEDSGKYGLVVKNKYGSETSD 87

                    ....*
gi 1958765569 25306 ITVKV 25310
Cdd:cd05737      88 VTVSV 92
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
8053-8127 9.28e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 43.59  E-value: 9.28e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  8053 KPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGnYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAG 8127
Cdd:cd04978       5 EPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAP-EDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7296-7370 9.29e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.86  E-value: 9.29e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  7296 FTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATN 7370
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQ 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
26311-26378 9.34e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 43.32  E-value: 9.34e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 26311 IVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKN 26378
Cdd:pfam13927    11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
16335-16420 9.42e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 43.65  E-value: 9.42e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  16335 KAGSQIRIPAVIKGRPTPKSSWEFDGKAKKAMKDGIhdipedaQLETAENSSVIVIPECTRAHSGKYSITAKNKAGQKTA 16414
Cdd:smart00410     7 KEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRF-------SVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                     ....*.
gi 1958765569  16415 NCRVKV 16420
Cdd:smart00410    80 GTTLTV 85
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
17330-17413 9.50e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 43.61  E-value: 9.50e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17330 PTLDLDFRDKlTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLA-LEKTKAKRSDSGRYCVVVENS 17408
Cdd:cd20975       1 PTFKVSLMDQ-SVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCrLRILAAERGDAGFYTCKAVNE 79

                    ....*
gi 1958765569 17409 TGSRK 17413
Cdd:cd20975      80 YGARQ 84
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5321-5411 9.52e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.79  E-value: 9.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5321 PPSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDA 5400
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|.
gi 1958765569  5401 GIQRCSALLSV 5411
Cdd:cd05762      81 GSRQAQVNLTV 91
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
4483-4569 9.57e-04

First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 43.73  E-value: 9.57e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4483 IKELEPVQSAINKKIHLECQVDEDrKVSITWSKDGQKLPAGKDYKIYFEDkiasLEIPLAKLKDSGTYSCTASNEAGSSS 4562
Cdd:cd04973      13 ISEVESYSAHPGDLLQLRCRLRDD-VQSINWTKDGVQLGENNRTRITGEE----VQIKDAVPRDSGLYACVTSSPSGSDT 87

                    ....*..
gi 1958765569  4563 SSATVAV 4569
Cdd:cd04973      88 TYFSVNV 94
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2597-2650 9.61e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.09  E-value: 9.61e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  2597 AVFECEV-ANPESEGEWLKDGKHLTLSNNFRSESDGHKRRLVIAAAKLDDIGEYT 2650
Cdd:cd00096       1 VTLTCSAsGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYT 55
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6352-6433 9.61e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 43.70  E-value: 9.61e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6352 PPVF-SSFPPvvETLK-NTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKI----ASKNFHAS-IHILNVDSTDIGEYH 6424
Cdd:cd20956       1 APVLlETFSE--QTLQpGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgdyvTSDGDVVSyVNISSVRVEDGGEYT 78

                    ....*....
gi 1958765569  6425 CKAQNEVGS 6433
Cdd:cd20956      79 CTATNDVGS 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
32093-32170 9.62e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 43.73  E-value: 9.62e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 32093 EGGYVKYVCKIENyDQSTQVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 32170
Cdd:cd20972      15 EGSKVRLECRVTG-NPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
104-193 9.69e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 43.61  E-value: 9.69e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   104 PNFSQRLQSMTVRQGSQARLQVRVTGIPTPVVKFYRDGAEIQ-SSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSV 182
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRpDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569   183 GRATSTADLLV 193
Cdd:cd20975      81 GARQCEARLEV 91
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
1258-1327 9.74e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 43.74  E-value: 9.74e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1258 ILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05891      13 IMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYG 82
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
4588-4653 9.75e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.77  E-value: 9.75e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELsESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAG 4653
Cdd:cd05730      18 GQSVTLACDADGFPEPTMTWTKDGEPI-ESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAG 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
9085-9165 9.79e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.53  E-value: 9.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLSETIEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHpTSNCEITFKNNALLLQ-VKKAsmaDAGLYTCKATND 9163
Cdd:cd20978       1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ-GPMERATVEDGTLTIInVQPE---DTGYYGCVATNE 76

                    ..
gi 1958765569  9164 AG 9165
Cdd:cd20978      77 IG 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
17745-17818 9.79e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.72  E-value: 9.79e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 17745 GDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDVT---PVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqdeDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
9182-9265 9.80e-04

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 43.61  E-value: 9.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9182 PVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIkPSDRCSFSFAS--GTAVLELKD-TAKADSGDYVCKASN 9258
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEI-IADGLKYRIQEfkGGYHQLIIAsVTDDDATVYQVRATN 80

                    ....*..
gi 1958765569  9259 VAGSDTS 9265
Cdd:cd20971      81 QGGSVSG 87
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
899-989 9.91e-04

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 43.84  E-value: 9.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   899 PPTLVSGLKNVTVVEGESVTLECHISGYPSPKVTWYRE------DYQIESSIDFQITFQSGiaRLMIREAFAEDSGRFTC 972
Cdd:cd20954       1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKAtgstpgEYKDLLYDPNVRILPNG--TLVFGHVQKENEGHYLC 78
                            90
                    ....*....|....*...
gi 1958765569   973 SAVNEAGT-VSTSCYLAV 989
Cdd:cd20954      79 EAKNGIGSgLSKVIFLKV 96
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7958-8041 9.99e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.72  E-value: 9.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7958 LKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVH-HVATLQILQTDQSHVGQYNCSASNPLGTASSS 8036
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEdGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                    ....*
gi 1958765569  8037 AKLIL 8041
Cdd:cd20973      84 AELTV 88
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
5134-5226 1.00e-03

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 43.47  E-value: 1.00e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5134 PATFTEKLEPSQLLKKGDATqLVCKVTGTPPIKITWfandRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNE 5213
Cdd:cd05851       1 PADINVKFKDTYALKGQNVT-LECFALGNPVPVIRW----RKILEPMPATAEISMSGAVLKIFNIQPEDEGTYECEAENI 75
                            90
                    ....*....|...
gi 1958765569  5214 AGSDHCTSIVIVK 5226
Cdd:cd05851      76 KGKDKHQARVYVQ 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8149-8218 1.00e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 43.54  E-value: 1.00e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8149 QSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESsKFRMSFEDSvaiLEMHNLSVEDSGDYTCEARN 8218
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDHS---LKIRKVTAGDMGSYTCVAEN 70
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8906-8980 1.01e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 43.64  E-value: 1.01e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  8906 VGLPVVFECAVSGSEPISVSWYKDGKPLKdSPNVQTSFLDNiATLNIFKTDRSLAGQYSCTVTNPIGSASSSAKL 8980
Cdd:cd20952      13 VGGTVVLNCQATGEPVPTISWLKDGVPLL-GKDERITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVL 85
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
8421-8511 1.01e-03

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 43.47  E-value: 1.01e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8421 PATIVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTgdSKYKISFFNKVsgLKIISVAPGDSGVYSFEVQNPV 8500
Cdd:cd05851       1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMP--ATAEISMSGAV--LKIFNIQPEDEGTYECEAENIK 76
                            90
                    ....*....|.
gi 1958765569  8501 GKDSCTVSIQV 8511
Cdd:cd05851      77 GKDKHQARVYV 87
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
4483-4569 1.01e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 43.83  E-value: 1.01e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4483 IKELEPVQSAINKKIHLECQ-VDEDRKVSITWSKDGQKLPAG---KDYKIYFEDKIASLEIPLAKLKDSGTYSCTASNEA 4558
Cdd:cd05895       3 LKEMKSQEVAAGSKLVLRCEtSSEYPSLRFKWFKNGKEINRKnkpENIKIQKKKKKSELRINKASLADSGEYMCKVSSKL 82
                            90
                    ....*....|.
gi 1958765569  4559 GSSSSSATVAV 4569
Cdd:cd05895      83 GNDSASANVTI 93
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
4967-5029 1.01e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 43.69  E-value: 1.01e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  4967 RLDCKIAGSLPMRVSWFKDGKEIAASDRY-QIAFVEGTASLEISRVDMNDAGNFTCRATNSVGS 5029
Cdd:cd05857      23 KFRCPAAGNPTPTMRWLKNGKEFKQEHRIgGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGS 86
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5133-5216 1.01e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 43.64  E-value: 1.01e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5133 EPATFTEklEPSQLlkkGDATQLVCKVT-GTPPIKITWFANDRELRESSKHKMSFVES-TAVLRLTDVAIEDSGEYMCEA 5210
Cdd:cd20959       5 IPFAFGE--GAAQV---GMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRrSSILSIDSLEASHAGNYTCHA 79

                    ....*.
gi 1958765569  5211 QNEAGS 5216
Cdd:cd20959      80 RNSAGS 85
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
18719-18805 1.01e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 43.74  E-value: 1.01e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18719 LSGVLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDtSAESSKFSLTKAKRSDGGKYVVTATNPAGSFV 18798
Cdd:cd05891       7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLE-QGKYASLTIKGVTSEDSGKYSINVKNKYGGET 85

                    ....*..
gi 1958765569 18799 AYATVNV 18805
Cdd:cd05891      86 VDVTVSV 92
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
33712-33777 1.01e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 43.25  E-value: 1.01e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33712 GQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRG 33777
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRG 66
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
17740-17818 1.01e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 43.15  E-value: 1.01e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17740 QHIKVGDTLRLSAIIKGVPFPKVTWKKEDREAP-TKAQI--DVTpvgskLEIRNAAHEDGGIYSLTVENPAGSKTVSVKV 17816
Cdd:cd05725       7 QVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPkGRYEIldDHS-----LKIRKVTAGDMGSYTCVAENMVGKIEASATL 81

                    ..
gi 1958765569 17817 LV 17818
Cdd:cd05725      82 TV 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
23472-23536 1.02e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.09  E-value: 1.02e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 23472 LRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSSFT--SLVLDNVNRYDSGKYTLTLENSSGTKSA 23536
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGngTLTISNVTLEDSGTYTCVASNSAGGSAS 67
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7670-7759 1.03e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 43.55  E-value: 1.03e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7670 PSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELE-SGEACTISLE-DFVTELELLEVEPLQSGDYSCLVTND 7747
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  7748 AGSASCTTHLFV 7759
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
14211-14292 1.04e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.47  E-value: 1.04e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14211 GLTVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEV 14290
Cdd:cd20949       8 VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQER 87

                    ..
gi 1958765569 14291 NV 14292
Cdd:cd20949      88 TV 89
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
6551-6629 1.05e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 43.75  E-value: 1.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6551 VTVGETCSLECKVAGTPELSVEWYKDGKLLTssQKHKFSFY---NKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVV 6627
Cdd:cd05729      16 LPAANKVRLECGAGGNPMPNITWLKDGKEFK--KEHRIGGTkveEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDV 93

                    ..
gi 1958765569  6628 DV 6629
Cdd:cd05729      94 DV 95
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
21590-21674 1.05e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.79  E-value: 1.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21590 RAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGAYPLTAKNTVGEVGDVITIQVHD 21669
Cdd:cd05762      14 RAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVD 93

                    ....*
gi 1958765569 21670 IPGPP 21674
Cdd:cd05762      94 KPDPP 98
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
25226-25301 1.06e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 43.75  E-value: 1.06e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 25226 RDVIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGT 25301
Cdd:cd05729      11 EREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVENEYGS 86
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
7214-7290 1.06e-03

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 43.53  E-value: 1.06e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  7214 QGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVGHASCSTALKV 7290
Cdd:cd20969      16 EGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
20508-20584 1.06e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 43.73  E-value: 1.06e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 20508 ENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNT-TLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKV 20584
Cdd:cd05737      15 EGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTvYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
28068-28154 1.07e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.79  E-value: 1.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28068 ELVITPEVDLSEiPGAQISVRighnVHLElpykGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYT 28147
Cdd:cd05736       2 VIRVYPEFQAKE-PGVEASLR----CHAE----GIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYT 72

                    ....*..
gi 1958765569 28148 VILDNAV 28154
Cdd:cd05736      73 CIAKNEG 79
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
7870-7935 1.08e-03

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 43.50  E-value: 1.08e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7870 GEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVG 7935
Cdd:cd05747      18 GESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
5525-5600 1.08e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 43.25  E-value: 1.08e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5525 GSFIDLECIVAGSHPISIQWFKDDQEISASDKyKFSFHDNTAfLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTV 5600
Cdd:cd20952      14 GGTVVLNCQATGEPVPTISWLKDGVPLLGKDE-RITTLENGS-LQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
5806-5878 1.08e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 43.75  E-value: 1.08e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5806 SDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSE-KMSVFYLHITKCAPSDVGEYQCIIANEGGSCACTARV 5878
Cdd:cd05729      20 NKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKvEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDV 93
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
6355-6429 1.09e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.47  E-value: 1.09e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6355 FSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQN 6429
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQ 76
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
4388-4476 1.09e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.47  E-value: 1.09e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4388 TFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADNKHSLELSNLTVQDRGVYSCKASNKFGA 4467
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                    ....*....
gi 1958765569  4468 DICQAELTI 4476
Cdd:cd20949      81 ASDMQERTV 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
6267-6349 1.09e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 43.25  E-value: 1.09e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6267 ASKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDkyQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTK 6346
Cdd:cd20952       7 QNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKD--ERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAV 84

                    ...
gi 1958765569  6347 VIV 6349
Cdd:cd20952      85 LDV 87
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
5245-5318 1.09e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 43.34  E-value: 1.09e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5245 DVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKtFIQDQlvSLQILKFVASDAGEYQCRVTNEVGSSTCSARVTL 5318
Cdd:cd05723      14 DIVFECEVTGKPTPTVKWVKNGDVVIPSDYFK-IVKEH--NLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
6370-6433 1.10e-03

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 42.94  E-value: 1.10e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  6370 VSLECELSGTPPFEVVWYKDKRQLRSSKKYKIaSKNFHASIHILNVDstDIGEYHCKAQNEVGS 6433
Cdd:cd05746       1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHI-SPEGYLAIRDVGVA--DQGRYECVARNTIGY 61
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
9292-9380 1.10e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 43.55  E-value: 1.10e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9292 FVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWT-KGKWRQLNQGGRILIHQKGDESkLEIRDTTKTDSGLYRCVAFNKHG 9370
Cdd:cd20990       3 FLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQlDGKPIRPDSAHKMLVRENGVHS-LIIEPVTSRDAGIYTCIATNRAG 81
                            90
                    ....*....|
gi 1958765569  9371 EIESNVNLQV 9380
Cdd:cd20990      82 QNSFNLELVV 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
2045-2128 1.11e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 43.15  E-value: 1.11e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2045 QSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWywpEDNvcELVIRDVTAEDSASIMVKAINIAGETSSHA 2124
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEIL---DDH--SLKIRKVTAGDMGSYTCVAENMVGKIEASA 79

                    ....
gi 1958765569  2125 FLLV 2128
Cdd:cd05725      80 TLTV 83
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
6367-6433 1.11e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 43.75  E-value: 1.11e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6367 NTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIAS-KNFHASIHILNVDSTDIGEYHCKAQNEVGS 6433
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKvEEKGWSLIIERAIPRDKGKYTCIVENEYGS 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
28081-28154 1.12e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 43.65  E-value: 1.12e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 28081 PGAQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEyVRFSKTENKITLSIKNVKKENGGKYTVILDNAV 28154
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFN-TRYIVRENGTTLTIRNIRRSDMGIYLCIASNGV 80
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
7301-7371 1.13e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 43.38  E-value: 1.13e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  7301 PPVGALKGSDVILQCEISGtPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNE 7371
Cdd:cd20967       5 PAVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGE 74
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
9081-9177 1.13e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.40  E-value: 1.13e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9081 RLTPPSFTKKLSETIEetegnsfkLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKA 9160
Cdd:cd05736       4 RVYPEFQAKEPGVEAS--------LRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIA 75
                            90
                    ....*....|....*..
gi 1958765569  9161 TNDAGSALCTSSIVIRE 9177
Cdd:cd05736      76 KNEGGVDEDISSLFVED 92
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
8793-8880 1.14e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 43.38  E-value: 1.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8793 ILEPPYFVKQLEPLKvtvgdsASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNvatLVFTQVDSNDSGEYICRAE 8872
Cdd:cd20968       2 ITRPPTNVTIIEGLK------AVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLESGS---LRIHNVQKEDAGQYRCVAK 72

                    ....*...
gi 1958765569  8873 NSVGEVSS 8880
Cdd:cd20968      73 NSLGIAYS 80
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
5997-6066 1.14e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 43.36  E-value: 1.14e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5997 ECVVAGTPELKVKWLKDGkQIVPSryfsmsfENNV----ASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRV 6066
Cdd:cd05728      20 ECKASGNPRPAYRWLKNG-QPLAS-------ENRIeveaGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7959-8040 1.14e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.16  E-value: 1.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7959 KDVHETLGFPVAFECRI-NGSEPLQVSWYKDGQLLkDDSNLQMSFVHHvATLQILQTDQSHVGQYNCSASNPLGT-ASSS 8036
Cdd:cd05724       5 SDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPL-NLDNERVRIVDD-GNLLIAEARKSDEGTYKCVATNMVGErESRA 82

                    ....
gi 1958765569  8037 AKLI 8040
Cdd:cd05724      83 ARLS 86
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
14213-14292 1.14e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 43.65  E-value: 1.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14213 TVKAGTKIELPA-TVTGKPEPKITWTKADTLL--RPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVE 14289
Cdd:cd05750      10 TVQEGSKLVLKCeATSENPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGN 89

                    ...
gi 1958765569 14290 VNV 14292
Cdd:cd05750      90 VTV 92
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
4949-5029 1.14e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 43.75  E-value: 1.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4949 PLFTKPLRNVDSV----VGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGTA-SLEISRVDMNDAGNFTCRA 5023
Cdd:cd05729       1 PRFTDTEKMEEREhalpAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIV 80

                    ....*.
gi 1958765569  5024 TNSVGS 5029
Cdd:cd05729      81 ENEYGS 86
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4480-4569 1.14e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.53  E-value: 1.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAI-NKKIHLECQVDEDRKVSITWSKDGQKLpAGKDYKIYFEDkiASLEIPLAKLKDSGTYSCTASNEA 4558
Cdd:cd20978       1 PKFIQKPEKNVVVKgGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVED--GTLTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  4559 GSSSSSATVAV 4569
Cdd:cd20978      78 GDIYTETLLHV 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
20898-20971 1.16e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 43.25  E-value: 1.16e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 20898 DGLTVKAGDSIVLSAiSILGKPLPKSSWSKAGKDIRPSD-IAQITSTPTSSMLTVKYATRKDAGEYTITATNPFG 20971
Cdd:cd05744       8 GDLEVQEGRLCRFDC-KVSGLPTPDLFWQLNGKPVRPDSaHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAG 81
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6543-6631 1.16e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.79  E-value: 1.16e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6543 VEKAGSMTVTVGETCSLECKVAGTPELSVEWYKDGK--LLTSSQKHKFSFYNKIS---SLKILSVEKEDAGTYTFQVQNN 6617
Cdd:cd05726       3 VVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSqnLLFPYQPPQPSSRFSVSptgDLTITNVQRSDVGYYICQALNV 82
                            90
                    ....*....|....
gi 1958765569  6618 VGKSSCTAVVDVSD 6631
Cdd:cd05726      83 AGSILAKAQLEVTD 96
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7128-7195 1.17e-03

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 42.55  E-value: 1.17e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7128 CHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGntpHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLS 7195
Cdd:cd05746       5 CSAQGDPEPTITWNKDGVQVTESGKFHISPEG---YLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
4389-4476 1.18e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 43.36  E-value: 1.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4389 FLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDADnkhsLELSNLTVQDRGVYSCKASNKFGAD 4468
Cdd:cd05728       2 WLKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTI 77

                    ....*...
gi 1958765569  4469 ICQAELTI 4476
Cdd:cd05728      78 YASAELAV 85
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7857-7947 1.18e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.79  E-value: 1.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7857 YFIEPLEHVeAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVA-----SLVINKVDHSDVGEYTCKAE 7931
Cdd:cd05726       2 FVVKPRDQV-VALGRTVTFQCETKGNPQPAIFWQKEGSQNLLFPYQPPQPSSRFSvsptgDLTITNVQRSDVGYYICQAL 80
                            90
                    ....*....|....*.
gi 1958765569  7932 NSVGAVASSAVLVIKE 7947
Cdd:cd05726      81 NVAGSILAKAQLEVTD 96
I-set pfam07679
Immunoglobulin I-set domain;
3139-3193 1.19e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.40  E-value: 1.19e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  3139 WYKDGIEINfqVEERHQYVVERRIHRMFISEARHSDAGEYTFVA----GRNRSSVTLYV 3193
Cdd:pfam07679    34 WFKDGQPLR--SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGEAEASAELTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7017-7099 1.19e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.33  E-value: 1.19e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7017 LKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSF-VDNVATLKILQTDLSHSGQYSCSASNPLGTASST 7095
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                    ....
gi 1958765569  7096 ARLT 7099
Cdd:cd20973      84 AELT 87
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6087-6161 1.20e-03

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 43.50  E-value: 1.20e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6087 GSSIHMECKVSGSLPINAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAGDNACSGILT 6161
Cdd:cd05747      18 GESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTLT 92
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
1441-1497 1.20e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.16  E-value: 1.20e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  1441 VGRPMPETFWFHNGQQIVNDYTHkVVIKEDGtqSLIIVPALPSDSGEWTVVAQNRAG 1497
Cdd:cd05724      23 RGHPEPTVSWRKDGQPLNLDNER-VRIVDDG--NLLIAEARKSDEGTYKCVATNMVG 76
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
9008-9076 1.20e-03

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 42.55  E-value: 1.20e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9008 LECHVTGTQPIKVTWAKDNREIRSGGNYQISyleNSAHLTIVKVDKGDSGQYTCYAINEVGKDSCTAQL 9076
Cdd:cd05746       3 IPCSAQGDPEPTITWNKDGVQVTESGKFHIS---PEGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
9195-9271 1.20e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 43.00  E-value: 1.20e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  9195 EGDFLQLSCHVQGSEPIRIQWLRAGREIkPSDRCSFSFASGTavLELKDTAKADSGDYVCKASNVAGSDTSKCKVTI 9271
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQL-SVDRRHLVLSSGT--LRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
29973-30046 1.21e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 43.36  E-value: 1.21e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 29973 GASLRLMVSVSGRPSPVITWSKKGIDLA--NRAIIDNTEsyslLIVDKVNRYDAGKYTIEAENQSGKKSATVLVKV 30046
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLAseNRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8613-8701 1.21e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.79  E-value: 1.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8613 FVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFK-GSSELV-------PGARCNVSlqdSVAELELFDVDTSQSGDYTCI 8684
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKeGSQNLLfpyqppqPSSRFSVS---PTGDLTITNVQRSDVGYYICQ 78
                            90
                    ....*....|....*..
gi 1958765569  8685 VSNEAGRASCTTQLFVK 8701
Cdd:cd05726      79 ALNVAGSILAKAQLEVT 95
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
1260-1329 1.21e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.47  E-value: 1.21e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  1260 EGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDF--LQDGrasLRIPVVLPEDEGIYTAFASNIKGNA 1329
Cdd:cd20949      13 EGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYriLADG---LLINKVTQDDTGEYTCRAYQVNSIA 81
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
7594-7666 1.21e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 43.34  E-value: 1.21e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  7594 VVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSlepSDTGAYTCVAANVAGQDESSALLTV 7666
Cdd:cd05723      15 IVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVK---SDEGFYQCIAENDVGNAQASAQLII 84
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8797-8886 1.22e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.22  E-value: 1.22e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTT-CKMHFKN-NVATLVFTQVDSNDSGEYICRAENS 8874
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDrISLYQDNcGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  8875 VGEVSSSTFLTV 8886
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2756-2840 1.22e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.56  E-value: 1.22e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2756 KIIKKPKDVTALENATVAFEVSVSHDTVP-VKWFHKNVEIKPSD---KHRLVSERKVHKLMLQNISPSDAGEYTAVV--- 2828
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKPDPeVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAkni 81
                            90
                    ....*....|...
gi 1958765569  2829 -GQLECKAKLFVE 2840
Cdd:cd20951      82 hGEASSSASVVVE 94
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
33074-33113 1.22e-03

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 43.21  E-value: 1.22e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1958765569 33074 RILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVV 33113
Cdd:cd04978       1 YWIIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPI 40
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
9315-9380 1.23e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.38  E-value: 1.23e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  9315 GDPIPNVKWTKgKWRQLNQGGRILIHQKgDESKLEIRDTTKTDSGLYRCVAFNKHGEIESNVNLQV 9380
Cdd:cd05730      29 GFPEPTMTWTK-DGEPIESGEEKYSFNE-DGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
5885-5973 1.23e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.47  E-value: 1.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5885 SFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGV 5964
Cdd:cd20949       1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                    ....*....
gi 1958765569  5965 ERCYAFLLV 5973
Cdd:cd20949      81 ASDMQERTV 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
20517-20577 1.23e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.16  E-value: 1.23e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 20517 PIKGKPAPSVSWKKGEDPLA-TDTRVSVESTAvntTLVVYDCQKSDAGKYTITLKNVAGTKE 20577
Cdd:cd05724      21 PPRGHPEPTVSWRKDGQPLNlDNERVRIVDDG---NLLIAEARKSDEGTYKCVATNMVGERE 79
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
2942-3013 1.24e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 1.24e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  2942 EKDTITFEVTVNYEGISYKWLKNGVEI--KSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVA----GKATSTATLYV 3013
Cdd:cd05750      15 SKLVLKCEATSENPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVenilGKDTVTGNVTV 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7766-7852 1.24e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 1.24e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7766 VKRLADTSVETGSPIVL--EATySGTPPIAVSWLKNEYPL--SQSPNCGITTTERSSILEILESTIEDYAQYACLIENEA 7841
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLkcEAT-SENPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENIL 81
                            90
                    ....*....|.
gi 1958765569  7842 GQDICEALVSV 7852
Cdd:cd05750      82 GKDTVTGNVTV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
12087-12151 1.24e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.94  E-value: 1.24e-03
                            10        20        30        40        50        60
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gi 1958765569 12087 KFISPLEDQTVKEGQTATFVCE-LSHEKMHVVWFKNDVKLHTTRTVLMSSEGKTYKLEIRETTLDD 12151
Cdd:pfam13927     3 VITVSPSSVTVREGETVTLTCEaTGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSD 68
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4759-4841 1.24e-03

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 43.50  E-value: 1.24e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4759 PPTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGLGGKYTCLAENEA 4838
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ...
gi 1958765569  4839 GSQ 4841
Cdd:cd05747      83 GKQ 85
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
17744-17818 1.25e-03

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 43.30  E-value: 1.25e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 17744 VGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIdvTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd04968      15 KGQTVTLECFALGNPVPQIKWRKVDGSPSSQWEI--TTSEPVLEIPNVQFEDEGTYECEAENSRGKDTVQGRIIV 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8801-8886 1.25e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.33  E-value: 1.25e-03
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gi 1958765569  8801 KQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNN-VATLVFTQVDSNDSGEYICRAENSVGEVS 8879
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569  8880 SSTFLTV 8886
Cdd:cd20973      82 CSAELTV 88
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
20-97 1.25e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 43.25  E-value: 1.25e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    20 GSAATFEAHISGSPVP-EVSWFRDGQVISTstLPGVQISFSDGRARLM-IPAVTKANSGRYSLRATNGSGQATSTAELLV 97
Cdd:cd20959      17 GMRAQLHCGVPGGDLPlNIRWTLDGQPISD--DLGITVSRLGRRSSILsIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4771-4849 1.25e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 43.25  E-value: 1.25e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4771 ALAGQTVTLQAAV-RGSEPISVMWMKGQEVIKEDGKIKMS-FSSGVAVLTISDVQIGLGGKYTCLAENEAGSQTSVGELI 4848
Cdd:cd20959      14 AQVGMRAQLHCGVpGGDLPLNIRWTLDGQPISDDLGITVSrLGRRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLT 93

                    .
gi 1958765569  4849 V 4849
Cdd:cd20959      94 V 94
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2852-2926 1.26e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 43.00  E-value: 1.26e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  2852 EVPETKAASFE--CEVSHFNVPSMWLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVCGNDQVSATLTV 2926
Cdd:cd20967       6 AVQVSKGHKIRltVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
6364-6434 1.26e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 43.67  E-value: 1.26e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6364 TLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKY---KIASKNFH--ASIHILNVDSTDIGEYHCKAQNEVGSD 6434
Cdd:cd05732      13 AVELEQITLTCEAEGDPIPEITWRRATRGISFEEGDldgRIVVRGHArvSSLTLKDVQLTDAGRYDCEASNRIGGD 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
33620-33680 1.26e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.70  E-value: 1.26e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 33620 VTLKANIAG--ATDVKWVLNGTELSNSEEYRYGVSGSDQTLTIKQASHRDEGILTCIGKTSQG 33680
Cdd:cd00096       1 VTLTCSASGnpPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
8428-8511 1.27e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 43.35  E-value: 1.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8428 PESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISF-FNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCT 8506
Cdd:cd05737       8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVeAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSD 87

                    ....*
gi 1958765569  8507 VSIQV 8511
Cdd:cd05737      88 VTVSV 92
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
6383-6435 1.27e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 43.49  E-value: 1.27e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  6383 EVVWYKDKRQLRSSKKYKIASKNFHASIHILNVDSTDIGEYHCKAQNEVGSDT 6435
Cdd:cd20927      31 QVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDS 83
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
33711-33787 1.27e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 42.62  E-value: 1.27e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 33711 EGQNVLFSCEISGEPSPEIEWFK--NNLPISISSNISVSRsrnmyTLEIRNASVSDSGKYTVKAKNFRGQCSATASLTV 33787
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKggSQLSVDRRHLVLSSG-----TLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
5884-5973 1.27e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 43.23  E-value: 1.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQ-ILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNES 5962
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQpVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569  5963 GVERCYAFLLV 5973
Cdd:cd20975      81 GARQCEARLEV 91
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
1264-1327 1.27e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.77  E-value: 1.27e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  1264 VTFHCKMSGYPLPKIAWYKDGKRIrrgeRYQMDFLqdgraslrIPVVLPEDEGIYTAFASNIKG 1327
Cdd:pfam13895    17 VTLTCSAPGNPPPSYTWYKDGSAI----SSSPNFF--------TLSVSAEDSGTYTCVARNGRG 68
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
25237-25303 1.28e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.70  E-value: 1.28e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 25237 FVLEADIRGKPIPDIVWSKDGNELEETaARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKT 25303
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPLPPS-SRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
31054-31124 1.28e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 43.35  E-value: 1.28e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 31054 VTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELVQSRKYKMS-SDGRTHTLTVMTEEQEDEGVYTCVATNEVG 31124
Cdd:cd05737      11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKvEAGRTVYFTINGVSSEDSGKYGLVVKNKYG 82
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
5130-5217 1.28e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 43.55  E-value: 1.28e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5130 FVKEPATFTeklepsqlLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVES-TAVLRLTDVAIEDSGEYMC 5208
Cdd:cd20990       3 FLQAPGDLT--------VQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENgVHSLIIEPVTSRDAGIYTC 74

                    ....*....
gi 1958765569  5209 EAQNEAGSD 5217
Cdd:cd20990      75 IATNRAGQN 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
33439-33500 1.28e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 43.34  E-value: 1.28e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 33439 VTGEPQPTVTWTKDGKAIAQSSKYKLSNDKE-EFILEILKTETSDGGLYSCTVANSAGSVSSS 33500
Cdd:pfam00047    21 STGSPGPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNNPGGSATLS 83
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
1690-1754 1.29e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 43.23  E-value: 1.29e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  1690 GDPTMVVEWLHDGKPLEAANRlRLINEF--GYCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:cd20975      26 GEPKPVVSWLRNRQPVRPDQR-RFAEEAegGLCRLRILAAERGDAGFYTCKAVNEYGARQCEARLEV 91
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
31450-31533 1.29e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.77  E-value: 1.29e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31450 NVRYQSNATLVCKVTGHPKPIVKWYRQGKEIiadglkyrvqefkGGYHQLIIASVTDDDATVYQVRATNQGGSVSgTASL 31529
Cdd:pfam13895    10 VVTEGEPVTLTCSAPGNPPPSYTWYKDGSAI-------------SSSPNFFTLSVSAEDSGTYTCVARNGRGGKV-SNPV 75

                    ....
gi 1958765569 31530 EVEV 31533
Cdd:pfam13895    76 ELTV 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
13081-13137 1.29e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.70  E-value: 1.29e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 13081 AEFVCTIS-KESFEVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVVMV 13137
Cdd:cd00096       1 VTLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVA 58
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
5884-5975 1.30e-03

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409398  Cd Length: 101  Bit Score: 43.63  E-value: 1.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVA-GSPPISITWLKDDQILEENDNV--HISFEDS----VATLQVRSVDNGHSGRYTC 5956
Cdd:cd05735       3 PAMITSYPNTTLATKGQKKEMSCTAhGEKPIIVRWEKEDTIINPSEMSryLVTTKEVgdevISTLQILPTVREDSGFFSC 82
                            90
                    ....*....|....*....
gi 1958765569  5957 QAKNESGVERCYAFLLVQE 5975
Cdd:cd05735      83 HAINSYGEDRGIIQLTVQE 101
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
5148-5217 1.30e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 43.49  E-value: 1.30e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5148 KKGDATQLVCKVTG-TPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSD 5217
Cdd:cd20927      12 EEGGHVKYVCKIENyDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGED 82
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4303-4384 1.32e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.41  E-value: 1.32e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4303 VALGHLAKFTCEIQGAPNVRFQWFKAGREI----YESDKCSIR-SSNYISSLEILRTQVVDCGEYTCKASNEYGSVSCTA 4377
Cdd:cd05726      11 VALGRTVTFQCETKGNPQPAIFWQKEGSQNllfpYQPPQPSSRfSVSPTGDLTITNVQRSDVGYYICQALNVAGSILAKA 90

                    ....*..
gi 1958765569  4378 TLTVTEA 4384
Cdd:cd05726      91 QLEVTDV 97
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
7113-7183 1.32e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.95  E-value: 1.32e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  7113 PVSIDVIAGESADFECHVTGAQPM-RVTWSKDNKEIRPGGNYTITCVGNTPH-LRILKVGKGDSGQYTCQATN 7183
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSASTGSPGpDVTWSKEGGTLIESLKVKHDNGRTTQSsLLISNVTKEDAGTYTCVVNN 75
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
33435-33505 1.33e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 43.16  E-value: 1.33e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 33435 FVIKVTGEPQPTVTWTKDGKAIA-QSSKYKLSNDKEEFI-LEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd05893      20 FTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDLDGTCsLHTTASTLDDDGNYTIMAANPQGRISCTGRLMV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
1261-1338 1.33e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.38  E-value: 1.33e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1261 GMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERyQMDFLQDGrASLRIPVVLPEDEGIYTAFASNIKG--NAICSGKLYVE 1338
Cdd:cd05730      18 GQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDG-SEMTILDVDKLDEAEYTCIAENKAGeqEAEIHLKVFAK 95
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
13337-13406 1.33e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.09  E-value: 1.33e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 13337 FVEHLEDQTVTEFDDAVFSCQLSRE-KANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLEDECEYAC 13406
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEpQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTC 72
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
24824-24915 1.34e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.40  E-value: 1.34e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAG 24903
Cdd:cd05736       1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
                            90
                    ....*....|..
gi 1958765569 24904 TaTENLSVIVLE 24915
Cdd:cd05736      81 V-DEDISSLFVE 91
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
6087-6153 1.34e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.77  E-value: 1.34e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  6087 GSSIHMECKVSGSLPINAQWFKDGKEISTSAKYrlvchentvslEVSNLELEDTANYTCKVSNVAGD 6153
Cdd:pfam13895    14 GEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF-----------FTLSVSAEDSGTYTCVARNGRGG 69
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
24148-24227 1.34e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.33  E-value: 1.34e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24148 VVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEI-KNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNVK 24226
Cdd:cd20973       8 EVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87

                    .
gi 1958765569 24227 V 24227
Cdd:cd20973      88 V 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
29569-29649 1.34e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 43.32  E-value: 1.34e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29569 VTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGkraTAVIKYCDR-SDSGKYTLTVKNASG-TKSVSVM 29646
Cdd:cd20958      10 LTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNG---TLVIENVQRsSDEGEYTCTARNQQGqSASRSVF 86

                    ...
gi 1958765569 29647 VKV 29649
Cdd:cd20958      87 VKV 89
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
24547-24624 1.36e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 43.15  E-value: 1.36e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 24547 VVRAGGSARIHIPFKGRPTPEITWSKEEGEFTD-KVQIekgINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKV 24624
Cdd:cd05725       8 VVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKgRYEI---LDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
4953-5029 1.37e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.97  E-value: 1.37e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4953 KPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIAfvegTASLEISRVDMNDAGNFTCRATNSVGS 5029
Cdd:cd05728       4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE----AGDLRITKLSLSDSGMYQCVAENKHGT 76
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8894-8980 1.37e-03

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 43.38  E-value: 1.37e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8894 SFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDG---------KPLKDSPNVQTSFLDNIatlnifKTDRSlaGQYS 8964
Cdd:cd05763       1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgtdfpaareRRMHVMPEDDVFFIVDV------KIEDT--GVYS 72
                            90
                    ....*....|....*.
gi 1958765569  8965 CTVTNPIGSASSSAKL 8980
Cdd:cd05763      73 CTAQNSAGSISANATL 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
3319-3393 1.38e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 43.29  E-value: 1.38e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  3319 GRPARFQCQVSGTDLK-VSWYCRDKKIKPSRFFRMTQfEDTyqLEIAEAFPEDEGTYAFVANNAVGQVSSTATLRL 3393
Cdd:cd20957      16 GRTAVFNCSVTGNPIHtVLWMKDGKPLGHSSRVQILS-EDV--LVIPSVKREDKGMYQCFVRNDGDSAQATAELKL 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
20224-20292 1.38e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.70  E-value: 1.38e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 20224 RLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIV 20292
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
9296-9370 1.38e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 43.00  E-value: 1.38e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  9296 PQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHQKGDeskLEIRDTTKTDSGLYRCVAFNKHG 9370
Cdd:cd20968       6 PTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGD-DLIKENNRIAVLESGS---LRIHNVQKEDAGQYRCVAKNSLG 76
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
26309-26391 1.38e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 43.36  E-value: 1.38e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26309 DVIVVKAGEVLKINADIAGRPLPVISWAKDGVEIEErAKTEIVSTDSN--TTLTVKDCVRRDTGQYVLTLKNVAGTRTMA 26386
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIEL-SEHYSVKLEQGkyASLTIKGVTSEDSGKYSINVKNKYGGETVD 87

                    ....*
gi 1958765569 26387 VNCKV 26391
Cdd:cd05891      88 VTVSV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
8892-8980 1.38e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.38  E-value: 1.38e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8892 PPSF-SRQLR-DVQETVGLPVVFECAVSG-SEPIsVSWYKDGKPLKDSPNvQTSFLDNIATLNIFKTDRSLAGQYSCTVT 8968
Cdd:cd05730       1 PPTIrARQSEvNATANLGQSVTLACDADGfPEPT-MTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAE 78
                            90
                    ....*....|..
gi 1958765569  8969 NPIGSASSSAKL 8980
Cdd:cd05730      79 NKAGEQEAEIHL 90
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7202-7290 1.39e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.22  E-value: 1.39e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7202 FIKKLDtskVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKynMSFVNSVALLTINeASVEDTGDYICEAHNGVGH 7281
Cdd:cd04969       7 PVKKKI---LAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSR--ICILPDGSLKIKN-VTKSDEGKYTCFAVNFFGK 80

                    ....*....
gi 1958765569  7282 ASCSTALKV 7290
Cdd:cd04969      81 ANSTGSLSV 89
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
22670-22749 1.41e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 43.35  E-value: 1.41e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENNSL-LTIKEACREDVGHYTVKLTNSAGEATETLNVI 22748
Cdd:cd05737      12 TIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVyFTINGVSSEDSGKYGLVVKNKYGSETSDVTVS 91

                    .
gi 1958765569 22749 V 22749
Cdd:cd05737      92 V 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9519-9564 1.41e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.70  E-value: 1.41e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958765569  9519 YPEIKLSWYKGTEKLEPSNKYEITINGDRHTLRVRNCQLKDQGNYR 9564
Cdd:cd00096      10 NPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYT 55
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
6922-6994 1.42e-03

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 42.92  E-value: 1.42e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  6922 EPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTyftnNVATLVFNKVGINDSGEYTCVAENSIG 6994
Cdd:cd04968       9 ADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPSSQWEITT----SEPVLEIPNVQFEDEGTYECEAENSRG 77
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
20213-20282 1.42e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.94  E-value: 1.42e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20213 KTLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLEN 20282
Cdd:pfam13927     9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
2315-2386 1.43e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.22  E-value: 1.43e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  2315 PIAIlQGLSDQKVCEGDIVQLEVKVSLENVEGV-WMKDGQEVQHS-DRVHIVIDKQS-HMLLIEDMTKEDAGNYS 2386
Cdd:cd05892       1 PMFI-QKPQNKKVLEGDPVRLECQISAIPPPQIfWKKNNEMLQYNtDRISLYQDNCGrICLLIQNANKKDAGWYT 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
14903-14986 1.43e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.95  E-value: 1.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14903 LETHDIVVIEGEKLSIPVPFR-AVPVPTVSWHKDGKEVKASDR-LTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSA 14980
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKvKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                    ....*.
gi 1958765569 14981 TASINV 14986
Cdd:pfam00047    81 TLSTSL 86
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6728-6809 1.43e-03

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 43.11  E-value: 1.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6728 PPSFVKEPEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNNA 6807
Cdd:cd05747       3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                    ..
gi 1958765569  6808 GQ 6809
Cdd:cd05747      83 GK 84
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
9581-9665 1.44e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 43.34  E-value: 1.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9581 PAWERHLQDVTLKEGQTCTMTCQFS---VPNVKseWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTCKHEDL 9657
Cdd:cd20972       2 PQFIQKLRSQEVAEGSKVRLECRVTgnpTPVVR--WFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  9658 ----ETSAELRI 9665
Cdd:cd20972      80 vgsdTTSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
23079-23138 1.44e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.70  E-value: 1.44e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23079 IYGKPIPTTQWVKGDQELSSTARLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKS 23138
Cdd:cd00096       7 ASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
1422-1507 1.44e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.77  E-value: 1.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1422 KPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHkvvIKEDgtQSLIIVPALPSDSGEWTVVAQNRAGKSTI 1501
Cdd:cd05725       3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYE---ILDD--HSLKIRKVTAGDMGSYTCVAENMVGKIEA 77

                    ....*.
gi 1958765569  1502 SVTLTV 1507
Cdd:cd05725      78 SATLTV 83
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
15920-16006 1.45e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 43.36  E-value: 1.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15920 IKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIeKPTDALNITKEEvsrsEAKTELSIPKAVREDKGTYTITASNRLGSVF 15999
Cdd:cd05729      14 HALPAANKVRLECGAGGNPMPNITWLKDGKEF-KKEHRIGGTKVE----EKGWSLIIERAIPRDKGKYTCIVENEYGSIN 88

                    ....*..
gi 1958765569 16000 RNVHVEV 16006
Cdd:cd05729      89 HTYDVDV 95
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
4292-4381 1.45e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 43.23  E-value: 1.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIY-ESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEY 4370
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRpDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569  4371 GSVSCTATLTV 4381
Cdd:cd20975      81 GARQCEARLEV 91
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
8230-8315 1.45e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 43.00  E-value: 1.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8230 KVKEPPVfrkkpfPVETLKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENlltSIHILNVDTADIGEYQCKA 8309
Cdd:cd20968       1 KITRPPT------NVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLESG---SLRIHNVQKEDAGQYRCVA 71

                    ....*.
gi 1958765569  8310 TNDVGS 8315
Cdd:cd20968      72 KNSLGI 77
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
11643-11723 1.45e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 43.69  E-value: 1.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11643 SVGSSAIFECLVS--PSTAIT-TWMKDGSNI--RESPKHRFIADGKDR--KLHIIDVQLSDAGEYTCVLRLGNKEKTSTA 11715
Cdd:cd04970      15 TVGENATLQCHAShdPTLDLTfTWSFNGVPIdlEKIEGHYRRRYGKDSngDLEIVNAQLKHAGRYTCTAQTVVDSDSASA 94

                    ....*...
gi 1958765569 11716 KLIVEELP 11723
Cdd:cd04970      95 TLVVRGPP 102
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
6729-6818 1.46e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.15  E-value: 1.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6729 PSFVKEPEPLEI-LPGKNITFTSVIRGTPPFKVGWFRGARELvKGDRCNIYFEDTVaeLELFNIDVSQSGEYTCVVSNNA 6807
Cdd:cd20978       1 PKFIQKPEKNVVvKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDGT--LTIINVQPEDTGYYGCVATNEI 77
                            90
                    ....*....|.
gi 1958765569  6808 GQASCTTRLFV 6818
Cdd:cd20978      78 GDIYTETLLHV 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
5524-5600 1.46e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.77  E-value: 1.46e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5524 KGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKfsfhdntafleISQLEGTDSGTYTCSATN-KAGHSQCSGHLTV 5600
Cdd:pfam13895    13 EGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFF-----------TLSVSAEDSGTYTCVARNgRGGKVSNPVELTV 79
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6453-6534 1.46e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.90  E-value: 1.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6453 NSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVReSENVRISFVNnvaTLQFAKAEPANAGKYICQVKNDGGVRENMA 6532
Cdd:cd20957       9 PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGH-SSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQATA 84

                    ..
gi 1958765569  6533 SL 6534
Cdd:cd20957      85 EL 86
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
19128-19197 1.47e-03

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 42.99  E-value: 1.47e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 19128 VVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDN--VVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAG 19197
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGGTDfpAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAG 80
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
4588-4659 1.47e-03

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 43.49  E-value: 1.47e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4588 GESARLHCKLKGSPVIQ-VTWFKNNKELSESNTVRMSFANSE---AILDITDVKVDDSGTYSCEATNDAGSDSCST 4659
Cdd:cd05865      15 GESKFFLCQVAGEAKDKdISWFSPNGEKLTPNQQRISVVRNDdysSTLTIYNANIDDAGIYKCVVSNEDEGESEAT 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
9587-9653 1.48e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 42.95  E-value: 1.48e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  9587 LQDVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKPQGRVKTEVEHK-VHKLTIADVRAEDQGRYTCK 9653
Cdd:cd20973       4 LRDKEVVEGSAARFDCKVEgYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCK 72
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
1261-1327 1.49e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.40  E-value: 1.49e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  1261 GMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGrASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05736      15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANG-SELHISNVRYEDTGAYTCIAKNEGG 80
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
4681-4747 1.49e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 1.49e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4681 GANALLQCEVAGTGP-FEVSWFKDKKQI--RSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEVGK 4747
Cdd:cd05750      14 GSKLVLKCEATSENPsPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGK 83
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
27000-27070 1.49e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.87  E-value: 1.49e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 27000 VRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATmrfNTEITA-ENLTINLKESVTADAGKYEITAANSSGTT 27070
Cdd:cd20952      11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGK---DERITTlENGSLQIKGAEKSDTGEYTCVALNLSGEA 79
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
5047-5131 1.49e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 1.49e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5047 KPESRDVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEaSESSLELYAVKTTDSGTYTCKVSN-VAGSVEC 5125
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRE-NGTTLTIRNIRRSDMGIYLCIASNgVPGSVEK 86

                    ....*.
gi 1958765569  5126 SANLFV 5131
Cdd:cd20970      87 RITLQV 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
28875-28964 1.51e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.40  E-value: 1.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28875 FKQTHIVRAGASIRLFIAYQGRPTPTAVWSKPDSNL--SIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSIT 28952
Cdd:cd05762       7 FPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIqeGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQ 86
                            90
                    ....*....|..
gi 1958765569 28953 FTVKVLDSPGPP 28964
Cdd:cd05762      87 VNLTVVDKPDPP 98
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
15921-15998 1.51e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 43.16  E-value: 1.51e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 15921 KVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKPTDALNITKEevsrSEAKTELSIPKAVREDKGTYTITASNRLGSV 15998
Cdd:cd05893      11 KIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRD----LDGTCSLHTTASTLDDDGNYTIMAANPQGRI 84
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
5137-5225 1.51e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 43.16  E-value: 1.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5137 FTEKLEPSQLLKkGDATQLVCKVTGTPPIKITWFANDRELRESSKHK--MSFVESTAVLRLTDVAIEDSGEYMCEAQNEA 5214
Cdd:cd05893       3 FEMKLKHYKIFE-GMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYtiQRDLDGTCSLHTTASTLDDDGNYTIMAANPQ 81
                            90
                    ....*....|.
gi 1958765569  5215 GSDHCTSIVIV 5225
Cdd:cd05893      82 GRISCTGRLMV 92
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
33696-33787 1.51e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 43.31  E-value: 1.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33696 DAPSFISQPRSQNINEGQNVLFSCEISGEPSPEIE--WFKNNLPISISSNISVSRSRNMY----TLEIRNASVSDSGKYT 33769
Cdd:cd04970       1 DATRITLAPSNADITVGENATLQCHASHDPTLDLTftWSFNGVPIDLEKIEGHYRRRYGKdsngDLEIVNAQLKHAGRYT 80
                            90
                    ....*....|....*...
gi 1958765569 33770 VKAKNFRGQCSATASLTV 33787
Cdd:cd04970      81 CTAQTVVDSDSASATLVV 98
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
4968-5028 1.51e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.97  E-value: 1.51e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  4968 LDCKIAGSLPMRVSWFKDGKEIAASDRYQIAFVEGT-ASLEISRVDMNDAGNFTCRATNSVG 5028
Cdd:cd05891      21 LTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYG 82
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
23469-23542 1.51e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 42.78  E-value: 1.51e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 23469 GGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIidVTSSFT-SLVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRV 23542
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIKLGGELPKGRT--KFENFNkTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
33696-33787 1.52e-03

Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 409440  Cd Length: 102  Bit Score: 43.49  E-value: 1.52e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33696 DAPSFISQPRSQNINEGQNVLFSCEISGEPSPEIE--WFKNNLPISISSNISVSRSRNMYT----LEIRNASVSDSGKYT 33769
Cdd:cd05854       1 DATKITLAPSSADINQGENLTLQCHASHDPTMDLTftWSLDDFPIDLDKPNGHYRRMEVKEtigdLVIVNAQLSHAGTYT 80
                            90
                    ....*....|....*...
gi 1958765569 33770 VKAKNFRGQCSATASLTV 33787
Cdd:cd05854      81 CTAQTVVDSASASATLVV 98
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
29973-30046 1.53e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.22  E-value: 1.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29973 GASLRLMVSVSGRPSPVITWSKKgidlaNRAIIDNTESYSL---------LIVDKVNRYDAGKYTIEAENQSGKKSATVL 30043
Cdd:cd05892      15 GDPVRLECQISAIPPPQIFWKKN-----NEMLQYNTDRISLyqdncgricLLIQNANKKDAGWYTVSAVNEAGVVSCNAR 89

                    ...
gi 1958765569 30044 VKV 30046
Cdd:cd05892      90 LDV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2668-2753 1.53e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.18  E-value: 1.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2668 KIKKTLRNLTVTETQDAIFSVELT-HPDVKgVQWIKNGVVLDSND---KYEISVKGTLYSLKIKNCAMADESVYGFKL-- 2741
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPE-VKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAkn 80
                            90
                    ....*....|....
gi 1958765569  2742 --GRLGASARLHVE 2753
Cdd:cd20951      81 ihGEASSSASVVVE 94
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
1810-1879 1.53e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 42.96  E-value: 1.53e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  1810 VRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVR-YDGIHYLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd05748       2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIEtTASSTSLVIKNAKRSDSGKYTLTLKNSAG 72
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
15908-15996 1.53e-03

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 43.11  E-value: 1.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15908 TIKLRLAVRGDTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIekptdaLNITKEEVSRSEAKTELSIPKAVREDKGTY 15987
Cdd:cd05747       1 TLPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQII------VSSQRHQITSTEYKSTFEISKVQMSDEGNY 74

                    ....*....
gi 1958765569 15988 TITASNRLG 15996
Cdd:cd05747      75 TVVVENSEG 83
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8907-8982 1.53e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 42.62  E-value: 1.53e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8907 GLPVVFECAVSGSEPISVSWYKDGKPLK-DSPNVQTSfldnIATLNIFKTDRSLAGQYSCTVTNPIGSASSSAKLIL 8982
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSvDRRHLVLS----SGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7025-7099 1.53e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 42.62  E-value: 1.53e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  7025 GLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQmsfVDNVATLKILQTDLSHSGQYSCSASNPLGTASSTARLT 7099
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHL---VLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLT 73
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
27000-27078 1.54e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 42.96  E-value: 1.54e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 27000 VRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKTFINIIV 27078
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
7773-7852 1.54e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.96  E-value: 1.54e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7773 SVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSI-LEILESTIEDYAQYACLIENEAGQDICEALVS 7851
Cdd:cd05737      12 TIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVyFTINGVSSEDSGKYGLVVKNKYGSETSDVTVS 91

                    .
gi 1958765569  7852 V 7852
Cdd:cd05737      92 V 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6449-6536 1.54e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.77  E-value: 1.54e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6449 ISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEV------VRESENVRISFVnnvatlqfakaEPANAGKYICQVK 6522
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELpkgryeILDDHSLKIRKV-----------TAGDMGSYTCVAE 69
                            90
                    ....*....|....
gi 1958765569  6523 NDGGVRENMASLTV 6536
Cdd:cd05725      70 NMVGKIEASATLTV 83
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
3205-3288 1.55e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 42.77  E-value: 1.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3205 LQPVTVQ--SGKPARF-CAVIAGRPQPKISWYKEEQLL-STGFKCKFLHDGQeytLLLIEAFPEDAAVYTCEAKNDYGVA 3280
Cdd:cd05724       2 VEPSDTQvaVGEMAVLeCSPPRGHPEPTVSWRKDGQPLnLDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGER 78

                    ....*....
gi 1958765569  3281 TTS-ASLSV 3288
Cdd:cd05724      79 ESRaARLSV 87
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
6278-6344 1.55e-03

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 42.55  E-value: 1.55e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  6278 RLECKITGSPEIRVVWYRNEHELTASDKYQmtfIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCS 6344
Cdd:cd05746       2 QIPCSAQGDPEPTITWNKDGVQVTESGKFH---ISPEGYLAIRDVGVADQGRYECVARNTIGYASVS 65
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2135-2207 1.55e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 1.55e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2135 TFTQELQDVVAKEKDTmATFECE-TSEPFVKVKWYKDGIEVHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSCV 2207
Cdd:pfam13927     3 VITVSPSSVTVREGET-VTLTCEaTGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
18032-18113 1.56e-03

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 42.99  E-value: 1.56e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18032 LVVKAGTTVRFPAIIRGVPVPTAKWATDG-TEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHL 18110
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATL 88

                    ...
gi 1958765569 18111 TVL 18113
Cdd:cd05763      89 TVL 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
25929-25986 1.56e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 42.77  E-value: 1.56e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 25929 PFKGRPQATVAWKKDGQVLRETT-RVnvsssKIVT--TLSIKEASREDVGTYELCVSNTAG 25986
Cdd:cd05724      21 PPRGHPEPTVSWRKDGQPLNLDNeRV-----RIVDdgNLLIAEARKSDEGTYKCVATNMVG 76
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
6445-6526 1.57e-03

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 43.07  E-value: 1.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6445 PPKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLK-------EKEEvVRESENVRIsFVNnvATLQFAKAEPANAGKY 6517
Cdd:cd20954       1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKatgstpgEYKD-LLYDPNVRI-LPN--GTLVFGHVQKENEGHY 76

                    ....*....
gi 1958765569  6518 ICQVKNDGG 6526
Cdd:cd20954      77 LCEAKNGIG 85
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
30262-30340 1.57e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 42.96  E-value: 1.57e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 30262 VPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSETIKVVI 30340
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
15919-15998 1.57e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.95  E-value: 1.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15919 TIKVKAGEPVNIPADV-TGLPMPKIEWSKNEKVIEkptdaLNITKEEVSRSEAKTELSIPKAVREDKGTYTITASNRLGS 15997
Cdd:pfam00047     5 TVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLI-----ESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                    .
gi 1958765569 15998 V 15998
Cdd:pfam00047    80 A 80
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8062-8124 1.57e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 42.94  E-value: 1.57e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  8062 GESGSFKCHVTGTaPIK-ITWAKDNREIrPGgNYKMTLVENtATLTVLKVAKG-DAGQYTCYASN 8124
Cdd:cd20958      15 GQTLRLHCPVAGY-PISsITWEKDGRRL-PL-NHRQRVFPN-GTLVIENVQRSsDEGEYTCTARN 75
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
22369-22467 1.58e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.40  E-value: 1.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22369 PPEIELDADLRKvvtIRACCTLRLFVPIKGRPAPEVKWA--REHGESLDKASIESTSSYTLLVVGNVNRFDSGKYILTVE 22446
Cdd:cd05762       1 PPQIIQFPEDMK---VRAGESVELFCKVTGTQPITCTWMkfRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVE 77
                            90       100
                    ....*....|....*....|.
gi 1958765569 22447 NSSGSKSAFVNVRVLDTPGPP 22467
Cdd:cd05762      78 NKLGSRQAQVNLTVVDKPDPP 98
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
5794-5880 1.58e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 43.06  E-value: 1.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5794 IRELEPVEVVKDSDVELECEVMGTTP-FEVTWLKNNKEIRSGKK---YTMSEKMSVFYLHITKCAPSDVGEYQCIIANEG 5869
Cdd:cd05895       3 LKEMKSQEVAAGSKLVLRCETSSEYPsLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSSKL 82
                            90
                    ....*....|.
gi 1958765569  5870 GSCACTARVAL 5880
Cdd:cd05895      83 GNDSASANVTI 93
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2514-2577 1.59e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.61  E-value: 1.59e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2514 VELSHSGIDVVWNFKGQEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGEYAFYAGENTTSGKLTV 2577
Cdd:cd20967      19 VELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
14217-14292 1.60e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 42.62  E-value: 1.60e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 14217 GTKIELPATVTGKPEPKITWTKADTLLRPDQRitiENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVNV 14292
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRR---HLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6085-6162 1.61e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.77  E-value: 1.61e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6085 VLGSSIHMECKVSGSLPINAQWFKDGKEISTSaKYRlVCHENtvSLEVSNLELEDTANYTCKVSNVAGDNACSGILTV 6162
Cdd:cd05725      10 LVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYE-ILDDH--SLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
14907-14988 1.61e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 42.95  E-value: 1.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14907 DIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDH-ISAHLEVPKSVHADAGVYTITLENKLGSATASIN 14985
Cdd:cd20973       6 DKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEdGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAE 85

                    ...
gi 1958765569 14986 VKV 14988
Cdd:cd20973      86 LTV 88
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7024-7098 1.61e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.88  E-value: 1.61e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7024 VGLPVTLTCRLNGSAPIHVCWYRDGVlLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPL-GTASSTARL 7098
Cdd:cd20970      16 EGENATFMCRAEGSPEPEISWTRNGN-LIIEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGVpGSVEKRITL 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
1051-1124 1.62e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 42.58  E-value: 1.62e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1051 EGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVsynkQTGECR--LVISMTFADDAGEYTIVIRNKHGETSAS 1124
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQI----ETTASStsLVIKNAKRSDSGKYTLTLKNSAGEKSAT 77
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
1258-1327 1.62e-03

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 43.11  E-value: 1.62e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1258 ILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQdGRASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05747      15 VSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTE-YKSTFEISKVQMSDEGNYTVVVENSEG 83
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
31059-31132 1.62e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 42.90  E-value: 1.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRfGKELVqsrkykMSSDGRTH--------TLTVMTEEQEDEGVYTCVATNEVGEVETSS 31130
Cdd:cd05894      10 GNKLRLDVPISGEPAPTVTWSR-GDKAF------TATEGRVRvesykdlsSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ..
gi 1958765569 31131 KL 31132
Cdd:cd05894      83 FV 84
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
28063-28152 1.63e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.90  E-value: 1.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28063 PLTVKelvITPEVDlseipgaqiSVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTEnkiTLSIKNVKKEN 28142
Cdd:cd20957       1 PLSAT---IDPPVQ---------TVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKRED 65
                            90
                    ....*....|
gi 1958765569 28143 GGKYTVILDN 28152
Cdd:cd20957      66 KGMYQCFVRN 75
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
11345-11617 1.63e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.46  E-value: 1.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11345 RKETPPVEEREIERFIQPE---EPGMEPQPEETPVQEPEPEKkviEKPKL-------KPRPPIRAPSPPKEDVKE---KI 11411
Cdd:NF033839    158 KPETPQPENPEHQKPTTPApdtKPSPQPEGKKPSVPDINQEK---EKAKLavatymsKILDDIQKHHLQKEKHRQivaLI 234
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11412 FQLKAVSKKKVPEKPEVVEKVEP--TPLKVPTAEKKVRKLLPEPKPQ--PKEEVvlksvlRKRPEEEEPKVEPKKVEKVK 11487
Cdd:NF033839    235 KELDELKKQALSEIDNVNTKVEIenTVHKIFADMDAVVTKFKKGLTQdtPKEPG------NKKPSAPKPGMQPSPQPEKK 308
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11488 KPEEPPPPPKAVEVEAPPEPKPKERKVPEPTKvPEIKPAIPLPGPEPKPKPEPEVKTMKAPPIEPAPTPIAAPVTapvvg 11567
Cdd:NF033839    309 EVKPEPETPKPEVKPQLEKPKPEVKPQPEKPK-PEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET----- 382
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11568 KKAEAKPKDEAAKPKGPIKGVAKKTPSPIEAERKKLRPGSGGEKP-PDEAP 11617
Cdd:NF033839    383 PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPkPEVKP 433
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
13262-13330 1.64e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.61  E-value: 1.64e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 13262 SVTFWCKVNRLNVTLKWTKNGEEVAFDNRISYRIDKYKHSLIIKDCGFPDEGEYIVTAGQDKSVAELLI 13330
Cdd:cd20967      14 KIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
25644-25698 1.64e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.83  E-value: 1.64e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 25644 KGRPEPEVKWEKAEGILTERAQIEVTSSYTmLVIDNVTRFDSGRYNLTLENNSGS 25698
Cdd:cd04969      27 KASPKPTISWSKGTELLTNSSRICILPDGS-LKIKNVTKSDEGKYTCFAVNFFGK 80
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
2039-2129 1.64e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.02  E-value: 1.64e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2039 KIFERIQSQTVGQgsDAHFRVRVVGKPDPECEWYKNGVKI--ERSDRiywYWPEDNVCELVIRDVTAEDSASIMVKAINI 2116
Cdd:cd05736       4 RVYPEFQAKEPGV--EASLRCHAEGIPLPRVQWLKNGMDInpKLSKQ---LTLIANGSELHISNVRYEDTGAYTCIAKNE 78
                            90
                    ....*....|...
gi 1958765569  2117 AGETSSHAFLLVQ 2129
Cdd:cd05736      79 GGVDEDISSLFVE 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4588-4667 1.64e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.40  E-value: 1.64e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVIKEPP 4667
Cdd:cd05762      16 GESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVDKP 95
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
5712-5787 1.65e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.97  E-value: 1.65e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5712 GQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISfvdgLATFQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE----AGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
1815-1889 1.66e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 43.30  E-value: 1.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  1815 GETARFRCRVTGYPQPKVNWYLNGQLIRKSKR---FRVRYDgiHYLDIVD-CKSYDTGEVKVTAENPEGVTEHKVKLEI 1889
Cdd:cd05857      19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKVRNQ--HWSLIMEsVVPSDKGNYTCVVENEYGSINHTYHLDV 95
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8711-8780 1.66e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.90  E-value: 1.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8711 NDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTEksaILEILSSTVEDSGQYNCYIEN 8780
Cdd:cd20957       9 PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRN 75
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
9192-9273 1.66e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.41  E-value: 1.66e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9192 TASEGDFLQLSCHVQGSEPIRIQWLRAGREI--------KPSDRCSfsfASGTAVLELKDTAKADSGDYVCKASNVAGSD 9263
Cdd:cd05726      10 VVALGRTVTFQCETKGNPQPAIFWQKEGSQNllfpyqppQPSSRFS---VSPTGDLTITNVQRSDVGYYICQALNVAGSI 86
                            90
                    ....*....|
gi 1958765569  9264 TSKCKVTIKE 9273
Cdd:cd05726      87 LAKAQLEVTD 96
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
13519-13598 1.66e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 43.11  E-value: 1.66e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13519 QDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTKT-----VDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKAEGF 13593
Cdd:cd20974       8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpgvqISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87

                    ....*
gi 1958765569 13594 INLQV 13598
Cdd:cd20974      88 AELLV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
22685-22752 1.67e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.00  E-value: 1.67e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 22685 GRPTPTVTWHKDDVPLKQTTRVNAEStENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNVIVLDK 22752
Cdd:cd05730      29 GFPEPTMTWTKDGEPIESGEEKYSFN-EDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFAK 95
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
2038-2128 1.67e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 43.23  E-value: 1.67e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIA 2117
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569  2118 GETSSHAFLLV 2128
Cdd:cd20975      81 GARQCEARLEV 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
1690-1754 1.68e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.87  E-value: 1.68e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1690 GDPTMVVEWLHDGKPLEAAN-RLRLINEfgyCSLDYEAAYSRDSGVITCRATNKYGTDHTSATLIV 1754
Cdd:cd20952      25 GEPVPTISWLKDGVPLLGKDeRITTLEN---GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7585-7664 1.68e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.90  E-value: 1.68e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7585 DTTATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADnvcTLTLSSLEPSDTGAYTCVAANVAGQDESSALL 7664
Cdd:cd20957      10 VQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQATAEL 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
1521-1597 1.68e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.88  E-value: 1.68e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1521 KLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSD-IIVPHKYPRIRIEGTKgeaaLKIDSTISQDSAWYTATAINKAG 1597
Cdd:cd20970       8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNlIIEFNTRYIVRENGTT----LTIRNIRRSDMGIYLCIASNGVP 81
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
33076-33143 1.68e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.41  E-value: 1.68e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 33076 LTKPRSITVHEGESARFSCDTDGEPVPTVTWLR-GGQVVSTSARHQVTTAKY----KSTFEISSVQASDEGNY 33143
Cdd:cd05726       3 VVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKeGSQNLLFPYQPPQPSSRFsvspTGDLTITNVQRSDVGYY 75
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
4292-4381 1.69e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 43.31  E-value: 1.69e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIyESDKCSIRSSNYI---SSLEILRtqVV-------DCGE 4361
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPL-ETDKDDPRSHRIVlpsGSLFFLR--VVhgrkgrsDEGV 77
                            90       100
                    ....*....|....*....|.
gi 1958765569  4362 YTCKASNEYG-SVSCTATLTV 4381
Cdd:cd07693      78 YVCVAHNSLGeAVSRNASLEV 98
I-set pfam07679
Immunoglobulin I-set domain;
15200-15310 1.69e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 1.69e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15200 SLEVKRGDEIALDATISGSPYPTITWIKDENVIVPeeikkrvappvrrkkgeaeeeepftlplTERLSINNsKQGESQLR 15279
Cdd:pfam07679     9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS----------------------------SDRFKVTY-EGGTYTLT 59
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1958765569 15280 VRDSLRPDHGQYMIKVENDHGVAKAPCTVSV 15310
Cdd:pfam07679    60 ISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5044-5133 1.70e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.02  E-value: 1.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5044 FVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFK-GDKELV-------SGGSCYITKEASessLELYAVKTTDSGTYTCK 5115
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKeGSQNLLfpyqppqPSSRFSVSPTGD---LTITNVQRSDVGYYICQ 78
                            90
                    ....*....|....*...
gi 1958765569  5116 VSNVAGSVECSANLFVKE 5133
Cdd:cd05726      79 ALNVAGSILAKAQLEVTD 96
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
17034-17124 1.72e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.83  E-value: 1.72e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17034 PDLQLDaSVRDRIVVHAGGVIRIIAYVSGKPPPTVTWNMNERALPQEATIETTAiSSSMVIKNCQRSHQGVYSLLAKNEG 17113
Cdd:cd04969       1 PDFELN-PVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILP-DGSLKIKNVTKSDEGKYTCFAVNFF 78
                            90
                    ....*....|.
gi 1958765569 17114 GERKKTIIVDV 17124
Cdd:cd04969      79 GKANSTGSLSV 89
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
9193-9262 1.73e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 42.86  E-value: 1.73e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  9193 ASEGDFLQLSCHV-QGSEPIRIQWLRAGREIkpSDRCSFSFA---SGTAVLELKDTAKADSGDYVCKASNVAGS 9262
Cdd:cd20959      14 AQVGMRAQLHCGVpGGDLPLNIRWTLDGQPI--SDDLGITVSrlgRRSSILSIDSLEASHAGNYTCHARNSAGS 85
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
7491-7570 1.74e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 42.78  E-value: 1.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7491 TVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSrhhiTFVRNL-ASLKIPSAEMNDKGLYSFEVENSVGKSSCTVSVH 7569
Cdd:cd05731       6 MVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGR----TKFENFnKTLKIENVSEADSGEYQCTASNTMGSARHTISVT 81

                    .
gi 1958765569  7570 V 7570
Cdd:cd05731      82 V 82
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
6-91 1.74e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 43.31  E-value: 1.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTLpgvqisfSDGRARLMIPA------------VTKA 73
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKD-------DPRSHRIVLPSgslfflrvvhgrKGRS 73
                            90
                    ....*....|....*...
gi 1958765569    74 NSGRYSLRATNGSGQATS 91
Cdd:cd07693      74 DEGVYVCVAHNSLGEAVS 91
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
7290-7375 1.74e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.02  E-value: 1.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7290 VKAPPVFTQKPPPVGAlkgsdvILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHIFNLEAPDIGEYHCKAT 7369
Cdd:cd05736       3 IRVYPEFQAKEPGVEA------SLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAK 76

                    ....*.
gi 1958765569  7370 NEVGSD 7375
Cdd:cd05736      77 NEGGVD 82
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
5897-5963 1.74e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 42.92  E-value: 1.74e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5897 LKSSATFQSTVAGSPPISITWLKDDQIL---EENDNVHISFedsvaTLQVRSVDNGHSGRYTCQAKNESG 5963
Cdd:cd05856      18 VGSSVRLKCVASGNPRPDITWLKDNKPLtppEIGENKKKKW-----TLSLKNLKPEDSGKYTCHVSNRAG 82
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
1815-1889 1.74e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 42.93  E-value: 1.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1815 GETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFR----VRYDG--IHYLDIVDCKSYDTGEVKVTAENPEGVTEHKVKLE 1888
Cdd:cd20956      16 GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRvgdyVTSDGdvVSYVNISSVRVEDGGEYTCTATNDVGSVSHSARIN 95

                    .
gi 1958765569  1889 I 1889
Cdd:cd20956      96 V 96
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
14899-14982 1.75e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 43.31  E-value: 1.75e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14899 PTIDLETHDIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKasdrlTMKNDHISAHLEVP-------KSVH-----ADA 14966
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLE-----TDKDDPRSHRIVLPsgslfflRVVHgrkgrSDE 75
                            90
                    ....*....|....*.
gi 1958765569 14967 GVYTITLENKLGSATA 14982
Cdd:cd07693      76 GVYVCVAHNSLGEAVS 91
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
8426-8511 1.76e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.98  E-value: 1.76e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8426 EKPEsIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKIS-FFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDS 8504
Cdd:cd05729      10 EERE-HALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTkVEEKGWSLIIERAIPRDKGKYTCIVENEYGSIN 88

                    ....*..
gi 1958765569  8505 CTVSIQV 8511
Cdd:cd05729      89 HTYDVDV 95
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4666-4754 1.76e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 42.93  E-value: 1.76e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4666 PPSFI-----KTLEPahivrGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRL---FTQKTFV--FLEITSFNSADIG 4735
Cdd:cd20956       1 APVLLetfseQTLQP-----GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgdyVTSDGDVvsYVNISSVRVEDGG 75
                            90
                    ....*....|....*....
gi 1958765569  4736 DYECVVANEVGKcgcvATH 4754
Cdd:cd20956      76 EYTCTATNDVGS----VSH 90
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8706-8794 1.77e-03

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 42.99  E-value: 1.77e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8706 FVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNG-VNVTASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGK 8784
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81
                            90
                    ....*....|
gi 1958765569  8785 DSCSAQILIL 8794
Cdd:cd05763      82 ISANATLTVL 91
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
1530-1597 1.77e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.98  E-value: 1.77e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  1530 GSRLEMKVRATGNPNPDIVWLKNSDIIVPHKypriRIEGTKGEA---ALKIDSTISQDSAWYTATAINKAG 1597
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEH----RIGGTKVEEkgwSLIIERAIPRDKGKYTCIVENEYG 85
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
19431-19490 1.78e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 42.57  E-value: 1.78e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19431 EAHVYGKPNPICKWKKGEDDVVTSSHLAIHKADSSSVLiikDVTRKDSGYYSLTAENSSG 19490
Cdd:cd05723      18 ECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVL---GLVKSDEGFYQCIAENDVG 74
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7765-7852 1.78e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.87  E-value: 1.78e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7765 FVKRLADTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSI-LEILESTIEDYAQYACLIENEAGQ 7843
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRAGE 82

                    ....*....
gi 1958765569  7844 DICEALVSV 7852
Cdd:cd05744      83 NSFNAELVV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
26313-26391 1.80e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 42.79  E-value: 1.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26313 VKAGEVLKINADIAGRPLPVISWAKDGVEIEERA---KTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNC 26389
Cdd:cd20951      12 VWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASV 91

                    ..
gi 1958765569 26390 KV 26391
Cdd:cd20951      92 VV 93
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
5701-5787 1.80e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.61  E-value: 1.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5701 KKPSPVLVLRNGQSTTFECQVTGtPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCearnDAGTAS 5780
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC----VAGGEK 75

                    ....*..
gi 1958765569  5781 CSIELKV 5787
Cdd:cd20967      76 CSFELFV 82
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
13066-13135 1.80e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 42.70  E-value: 1.80e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 13066 FISKPQNLEILEGEKAEFVCTISKESF-EVQWKRDDQTLESG----DKYDIIADGkkrvLVVKDATLQDMGTYVV 13135
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQpNVTWHFNGQPISASvadmSKYRILADG----LLINKVTQDDTGEYTC 72
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
8907-8975 1.81e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 42.78  E-value: 1.81e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8907 GLPVVFECAVSGSEPISVSWYKDGKPLkdsPNVQTSFLDNIATLNIFKTDRSLAGQYSCTVTNPIGSAS 8975
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIKLGGEL---PKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSAR 75
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
9295-9380 1.81e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 42.57  E-value: 1.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9295 EPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGkwrqlnqgGRILI----HQKGDESKLEIRDTTKTDSGLYRCVAFNKHG 9370
Cdd:cd05723       3 KPSNIYAHESMDIVFECEVTGKPTPTVKWVKN--------GDVVIpsdyFKIVKEHNLQVLGLVKSDEGFYQCIAENDVG 74
                            90
                    ....*....|
gi 1958765569  9371 EIESNVNLQV 9380
Cdd:cd05723      75 NAQASAQLII 84
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
33698-33787 1.82e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 43.31  E-value: 1.82e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33698 PSFISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSR-----NMYTLEIRNA--SVSDSGKYTV 33770
Cdd:cd07693       1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRIvlpsgSLFFLRVVHGrkGRSDEGVYVC 80
                            90
                    ....*....|....*...
gi 1958765569 33771 KAKNFRGQC-SATASLTV 33787
Cdd:cd07693      81 VAHNSLGEAvSRNASLEV 98
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
7591-7656 1.82e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 42.48  E-value: 1.82e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7591 GASVVLECRVSGSAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAG 7656
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRG 66
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
4295-4381 1.83e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.98  E-value: 1.83e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4295 KRRIEPLEValGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSI-RSSNYISSLEILRTQVVDCGEYTCKASNEYGSV 4373
Cdd:cd05729      10 EEREHALPA--ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGtKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSI 87

                    ....*...
gi 1958765569  4374 SCTATLTV 4381
Cdd:cd05729      88 NHTYDVDV 95
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
6264-6349 1.83e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.38  E-value: 1.83e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6264 KLEASKI-VKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYqmtFIDSVAVmqmnslgtEDSGDFICEAQNPAGS-T 6341
Cdd:pfam13895     3 VLTPSPTvVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF---FTLSVSA--------EDSGTYTCVARNGRGGkV 71

                    ....*...
gi 1958765569  6342 SCSTKVIV 6349
Cdd:pfam13895    72 SNPVELTV 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2329-2403 1.83e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.88  E-value: 1.83e-03
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   2329 EGDIVQLEVKVS-LENVEGVWMKDGQE-VQHSDRVHIVIDKQSHMLLIEDMTKEDAGNYSFTIPALGLSTSGNVSVY 2403
Cdd:smart00410     8 EGESVTLSCEASgSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33441-33505 1.84e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 42.86  E-value: 1.84e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33441 GEPQPTVTWTKDGKAIAQSSKYKLSN-DKEEFILEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd20959      29 GDLPLNIRWTLDGQPISDDLGITVSRlGRRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7670-7760 1.84e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 43.11  E-value: 1.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7670 PSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSR--ELESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTND 7747
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  7748 AGSASCTTHLFVK 7760
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5980-6066 1.84e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.77  E-value: 1.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5980 IEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMsfENNvaSFRIQSVMKQDSGQYTFKVENDFGSSS 6059
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEIL--DDH--SLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  6060 CDAYLRV 6066
Cdd:cd05725      77 ASATLTV 83
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
4588-4653 1.84e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 42.48  E-value: 1.84e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAG 4653
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRG 66
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
5619-5684 1.85e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.98  E-value: 1.85e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5619 TRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWK-DDTSTILELFSAKAADSGTYICQLSNDVGT 5684
Cdd:cd05729      20 NKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKvEEKGWSLIIERAIPRDKGKYTCIVENEYGS 86
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5799-5871 1.86e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.57  E-value: 1.86e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  5799 PVEVVKDSDVELECEV-MGTTPFEVTWLKNNKEIRSGKKYTMSEKM-SVFYLHITKCAPSDVGEYQCIIANEGGS 5871
Cdd:pfam00047     5 TVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRtTQSSLLISNVTKEDAGTYTCVVNNPGGS 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
20506-20584 1.86e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 1.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20506 AKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDT-RVSVEstAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKV 20584
Cdd:cd20976      13 AVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAdRSTCE--AGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
16629-16732 1.86e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.02  E-value: 1.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16629 PPSI-ELKEFMEVEEGTDVNIVAKIKGVPFPTLTWFKAppkkpdsKEPVVYDTHVNKQVVDDTCTLVIPQSRRSDTGLYS 16707
Cdd:cd05762       1 PPQIiQFPEDMKVRAGESVELFCKVTGTQPITCTWMKF-------RKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYT 73
                            90       100
                    ....*....|....*....|....*
gi 1958765569 16708 ITAVNNLGTASKEMRLNVLGRPGPP 16732
Cdd:cd05762      74 LEVENKLGSRQAQVNLTVVDKPDPP 98
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
23466-23549 1.86e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.02  E-value: 1.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23466 IRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSSFTS--LVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRVL 23543
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSskLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*.
gi 1958765569 23544 DTPSPP 23549
Cdd:cd05762      93 DKPDPP 98
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
7589-7670 1.87e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 43.31  E-value: 1.87e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7589 TLGASVVLECRVS--GSAPISVGWFLDGNEI----ISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQDESSA 7662
Cdd:cd04970      15 TVGENATLQCHAShdPTLDLTFTWSFNGVPIdlekIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSDSASA 94

                    ....*...
gi 1958765569  7663 LLTVQEPP 7670
Cdd:cd04970      95 TLVVRGPP 102
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
4387-4466 1.88e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 42.92  E-value: 1.88e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4387 PTFLSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQK---DGTALSPSPDCRITD--ADNKHSLELSNLTVQDRGVYSCKA 4461
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKqvpGKENLIMRPNHVRGNvvVTNIGQLVIYNAQPQDAGLYTCTA 80

                    ....*
gi 1958765569  4462 SNKFG 4466
Cdd:cd05765      81 RNSGG 85
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
9109-9173 1.88e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.87  E-value: 1.88e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  9109 VAGSQPI-TIAWYKNNVEIhPTSNCEITFKNNALLlQVKKASMADAGLYTCKATNDAGSALCTSSI 9173
Cdd:cd20952      22 QATGEPVpTISWLKDGVPL-LGKDERITTLENGSL-QIKGAEKSDTGEYTCVALNLSGEATWSAVL 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4667-4747 1.88e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 42.76  E-value: 1.88e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4667 PSFIKTLEPAHIVRGA-NALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTfvfLEITSFNSADIGDYECVVANEV 4745
Cdd:cd20978       1 PKFIQKPEKNVVVKGGqDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGT---LTIINVQPEDTGYYGCVATNEI 77

                    ..
gi 1958765569  4746 GK 4747
Cdd:cd20978      78 GD 79
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
5150-5215 1.89e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.88  E-value: 1.89e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5150 GDATQLVCKVTGTPPIKITWFANDRELRESSKhKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAG 5215
Cdd:cd20970      17 GENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTTLTIRNIRRSDMGIYLCIASNGVP 81
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
13066-13135 1.89e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.83  E-value: 1.89e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 13066 FISKPQNLEILEGEKAEFVCTISKE-SFEVQWKRDDQTLE-SGDKYDIIADGKKRV-LVVKDATLQDMGTYVV 13135
Cdd:cd05892       3 FIQKPQNKKVLEGDPVRLECQISAIpPPQIFWKKNNEMLQyNTDRISLYQDNCGRIcLLIQNANKKDAGWYTV 75
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
4770-4844 1.89e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.57  E-value: 1.89e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4770 TALAGQTVTLQAAVRGSEP-ISVMWMKGQEVIKEDGKIKMSF-SSGVAVLTISDVQIGLGGKYTCLAENEAGSQTSV 4844
Cdd:pfam00047     7 TVLEGDSATLTCSASTGSPgPDVTWSKEGGTLIESLKVKHDNgRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLS 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5052-5129 1.89e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.57  E-value: 1.89e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5052 DVLPGSAV---ClkSAFQGSTPLTIRWFKGDKELVSG-GSCYITKEASESSLELYAVKTTDSGTYTCKVSNVAGSVECSA 5127
Cdd:pfam00047     7 TVLEGDSAtltC--SASTGSPGPDVTWSKEGGTLIESlKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84

                    ..
gi 1958765569  5128 NL 5129
Cdd:pfam00047    85 SL 86
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
28480-28558 1.90e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 42.56  E-value: 1.90e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28480 LVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEIT-DVLGSTSLFVRDATRDHRGVYTVEAKNVSG--STKAEI 28556
Cdd:cd20973       7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGeaTCSAEL 86

                    ..
gi 1958765569 28557 TV 28558
Cdd:cd20973      87 TV 88
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8058-8137 1.91e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 42.86  E-value: 1.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8058 DLALGESGSFKCHVT-GTAPIKITWAKDNREIRPGGNYKMTLVEN-TATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQL 8135
Cdd:cd20959      13 AAQVGMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGRrSSILSIDSLEASHAGNYTCHARNSAGSASYTAPL 92

                    ..
gi 1958765569  8136 GV 8137
Cdd:cd20959      93 TV 94
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7484-7570 1.91e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.87  E-value: 1.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7484 VEKPEPMTVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHItFVRNLA--SLKIPSAEMNDKGLYSFEVENSVGK 7561
Cdd:cd05744       4 LQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM-LVRENGrhSLIIEPVTKRDAGIYTCIARNRAGE 82

                    ....*....
gi 1958765569  7562 SSCTVSVHV 7570
Cdd:cd05744      83 NSFNAELVV 91
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
5229-5309 1.92e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.98  E-value: 1.92e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEY----DVMLLAEVAGTPPFEITWFKDNTTL-RSGRKYKTFIQDQLVSLQILKFVASDAGEYQCRV 5303
Cdd:cd05729       1 PRFTDTEKMEEREHALpaanKVRLECGAGGNPMPNITWLKDGKEFkKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIV 80

                    ....*.
gi 1958765569  5304 TNEVGS 5309
Cdd:cd05729      81 ENEYGS 86
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
33435-33505 1.92e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 42.62  E-value: 1.92e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 33435 FVIK--VTGEPQPTVTWTKDGKAIaQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd20976      19 FVAQcsARGKPVPRITWIRNAQPL-QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
12986-13044 1.93e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 42.58  E-value: 1.93e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12986 VSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIETGRFEILTDGRKRILIIQNAQLEDAGSY 13044
Cdd:cd05748       4 VRAGESLRLDIPIKgRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKY 63
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
5808-5871 1.94e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.92  E-value: 1.94e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5808 VELECEVMGTTPFEVTWLKNNKEIRS-----GKKYtmseKMSVFYLHITKCAPSDVGEYQCIIANEGGS 5871
Cdd:cd05857      22 VKFRCPAAGNPTPTMRWLKNGKEFKQehrigGYKV----RNQHWSLIMESVVPSDKGNYTCVVENEYGS 86
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
8797-8886 1.96e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.98  E-value: 1.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFV---KQLEPLK-VTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMH-FKNNVATLVFTQVDSNDSGEYICRA 8871
Cdd:cd05729       1 PRFTdteKMEEREHaLPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTkVEEKGWSLIIERAIPRDKGKYTCIV 80
                            90
                    ....*....|....*
gi 1958765569  8872 ENSVGEVSSSTFLTV 8886
Cdd:cd05729      81 ENEYGSINHTYDVDV 95
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
5322-5412 1.97e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 42.79  E-value: 1.97e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5322 PSFIKKIETTSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIR-MTFEN--NVASLYLSGIEVKHDGKYVCQAKN 5398
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGkYKIESeyGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|....
gi 1958765569  5399 DAGIQRCSALLSVK 5412
Cdd:cd20951      81 IHGEASSSASVVVE 94
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6258-6349 1.98e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 42.93  E-value: 1.98e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6258 PPKFVKKLEaSKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQM-TFI--DSVAVMQMN--SLGTEDSGDFIC 6332
Cdd:cd20956       1 APVLLETFS-EQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgDYVtsDGDVVSYVNisSVRVEDGGEYTC 79
                            90
                    ....*....|....*..
gi 1958765569  6333 EAQNPAGSTSCSTKVIV 6349
Cdd:cd20956      80 TATNDVGSVSHSARINV 96
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
29567-29649 1.98e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 42.76  E-value: 1.98e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29567 DLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDlceKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVM 29646
Cdd:cd20978       9 KNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ---GPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTETL 85

                    ...
gi 1958765569 29647 VKV 29649
Cdd:cd20978      86 LHV 88
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
6367-6433 1.98e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.92  E-value: 1.98e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6367 NTeVSLECELSGTPPFEVVWYKDKRQLRSSKK---YKIasKNFHASIHILNVDSTDIGEYHCKAQNEVGS 6433
Cdd:cd05857      20 NT-VKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKV--RNQHWSLIMESVVPSDKGNYTCVVENEYGS 86
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
5522-5602 1.98e-03

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409398  Cd Length: 101  Bit Score: 43.25  E-value: 1.98e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5522 SIKGSFIDLECIVAGSHPISIQWFKDDQEISASD--KYKFSFHDN----TAFLEISQLEGTDSGTYTCSATNKAGHSQCS 5595
Cdd:cd05735      15 ATKGQKKEMSCTAHGEKPIIVRWEKEDTIINPSEmsRYLVTTKEVgdevISTLQILPTVREDSGFFSCHAINSYGEDRGI 94

                    ....*..
gi 1958765569  5596 GHLTVKE 5602
Cdd:cd05735      95 IQLTVQE 101
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2404-2481 1.98e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.52  E-value: 1.98e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  2404 SVDVITPLKDVNVieGTKAVLECKVSVPDVTSVKWYLNDEQIKPDDRVQSIVkgtKQRLVINRTHASDEGPYKLMVGR 2481
Cdd:cd20957       3 SATIDPPVQTVDF--GRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILS---EDVLVIPSVKREDKGMYQCFVRN 75
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12369-12426 1.99e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.32  E-value: 1.99e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12369 AKFECEVSREPK-TFRWLKGTQEIAGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAE 12426
Cdd:cd00096       1 VTLTCSASGNPPpTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
20520-20587 1.99e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.00  E-value: 1.99e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 20520 GKPAPSVSWKKGEDPLAT-DTRVSVESTAvnTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKVVGK 20587
Cdd:cd05730      29 GFPEPTMTWTKDGEPIESgEEKYSFNEDG--SEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFAK 95
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
16640-16725 2.00e-03

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 43.07  E-value: 2.00e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16640 VEEGTDVNIVAKIKGVPFPTLTWFKAPPKKPDSKEPVVYDTHVNkqvVDDTCTLVIPQSRRSDTGLYSITAVNNLGTA-S 16718
Cdd:cd20954      13 VAAGQDVMLHCQADGFPTPTVTWKKATGSTPGEYKDLLYDPNVR---ILPNGTLVFGHVQKENEGHYLCEAKNGIGSGlS 89

                    ....*..
gi 1958765569 16719 KEMRLNV 16725
Cdd:cd20954      90 KVIFLKV 96
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
7856-7937 2.02e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.92  E-value: 2.02e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7856 PYFIEPLE-----HVEAAiGEPTTLQCKVDGTPEIRISWYKEHTKLRSAP---AYKmqFKNNVASLVINKVDHSDVGEYT 7927
Cdd:cd05857       1 PYWTNPEKmekklHAVPA-ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHrigGYK--VRNQHWSLIMESVVPSDKGNYT 77
                            90
                    ....*....|
gi 1958765569  7928 CKAENSVGAV 7937
Cdd:cd05857      78 CVVENEYGSI 87
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
33703-33785 2.02e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.52  E-value: 2.02e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33703 QPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRnmyTLEIRNASVSDSGKYTVKAKNFRGQCSAT 33782
Cdd:cd20957       7 DPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQAT 83

                    ...
gi 1958765569 33783 ASL 33785
Cdd:cd20957      84 AEL 86
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6268-6339 2.03e-03

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 42.73  E-value: 2.03e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  6268 SKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAG 6339
Cdd:cd05747      12 SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
1801-1880 2.03e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 42.92  E-value: 2.03e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1801 PDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNW--YLNGQ--LIRKSKRFR--VRYDGIHYLDIVDCKSYDTGEVKVTA 1874
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWekQVPGKenLIMRPNHVRgnVVVTNIGQLVIYNAQPQDAGLYTCTA 80

                    ....*.
gi 1958765569  1875 ENPEGV 1880
Cdd:cd05765      81 RNSGGL 86
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
17738-17808 2.03e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.02  E-value: 2.03e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 17738 REQHIKVGDTLRLSAIIKGVPFPKVTWKKEDREAPTK--AQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAG 17808
Cdd:cd05736       8 EFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKlsKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
30-97 2.03e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.88  E-value: 2.03e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569    30 SGSPVPEVSWFRDGQVISTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATSTAELLV 97
Cdd:cd05750      25 SENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7022-7098 2.04e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.52  E-value: 2.04e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7022 QTV--GLPVTLTCRLNGSaPIH-VCWYRDGVLLRDDENLQMSFVDnvaTLKILQTDLSHSGQYSCSASNPLGTASSTARL 7098
Cdd:cd20957      11 QTVdfGRTAVFNCSVTGN-PIHtVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQATAEL 86
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
2038-2128 2.06e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 42.76  E-value: 2.06e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2038 PKIFERIQSQTVG-QGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYwpEDNVceLVIRDVTAEDSASIMVKAINI 2116
Cdd:cd20978       1 PKFIQKPEKNVVVkGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATV--EDGT--LTIINVQPEDTGYYGCVATNE 76
                            90
                    ....*....|..
gi 1958765569  2117 AGETSSHAFLLV 2128
Cdd:cd20978      77 IGDIYTETLLHV 88
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
4588-4663 2.06e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 42.23  E-value: 2.06e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESntvRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVI 4663
Cdd:cd05745       2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVD---RRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8050-8137 2.07e-03

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 42.61  E-value: 2.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8050 FDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGG-NYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGK 8128
Cdd:cd05763       2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAArERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81

                    ....*....
gi 1958765569  8129 DSCSAQLGV 8137
Cdd:cd05763      82 ISANATLTV 90
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
5150-5216 2.09e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.59  E-value: 2.09e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5150 GDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSfvesTAVLRLTDVAIEDSGEYMCEAQNEAGS 5216
Cdd:cd05728      14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE----AGDLRITKLSLSDSGMYQCVAENKHGT 76
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
17736-17816 2.09e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.98  E-value: 2.09e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17736 MAREQHIKVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDVTPVGSK---LEIRNAAHEDGGIYSLTVENPAGS--K 17810
Cdd:cd05729      10 EEREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKgwsLIIERAIPRDKGKYTCIVENEYGSinH 89

                    ....*.
gi 1958765569 17811 TVSVKV 17816
Cdd:cd05729      90 TYDVDV 95
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
24834-24904 2.12e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.98  E-value: 2.12e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 24834 SVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATST-ILHIKESSKDDFGKYSVTATNNAGT 24904
Cdd:cd05729      15 ALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGS 86
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
18428-18510 2.14e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18428 DVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPR-VELQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd05737       9 DVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRtVYFTINGVSSEDSGKYGLVVKNKYGSETSDV 88

                    ....
gi 1958765569 18507 IVNV 18510
Cdd:cd05737      89 TVSV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2945-3009 2.15e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.93  E-value: 2.15e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2945 TITFEVTvNYEGISYKWLKNGVEIKSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVA-----GKATSTA 3009
Cdd:cd00096       2 TLTCSAS-GNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAsnsagGSASASV 70
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
908-989 2.16e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 42.57  E-value: 2.16e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   908 NVTVVEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQSGIARLMIREAfaeDSGRFTCSAVNEAGTVSTSCYL 987
Cdd:cd05723       6 NIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKS---DEGFYQCIAENDVGNAQASAQL 82

                    ..
gi 1958765569   988 AV 989
Cdd:cd05723      83 II 84
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
6271-6349 2.16e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.16e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6271 VKAGDSARLECKITGSPEIRVVWYRNEHELTASDKYQMTF-IDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTKVIV 6349
Cdd:cd05737      13 IMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVeAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8997-9080 2.17e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.02  E-value: 2.17e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8997 PVDAVV--GESADLECHVTGTQPIKVTWAKD--------NREIRSGGNYQISyleNSAHLTIVKVDKGDSGQYTCYAINE 9066
Cdd:cd05726       6 PRDQVValGRTVTFQCETKGNPQPAIFWQKEgsqnllfpYQPPQPSSRFSVS---PTGDLTITNVQRSDVGYYICQALNV 82
                            90
                    ....*....|....
gi 1958765569  9067 VGKDSCTAQLNIKE 9080
Cdd:cd05726      83 AGSILAKAQLEVTD 96
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
11630-11719 2.18e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.88  E-value: 2.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11630 VKEIKdivlTEAESVGSSAIFEC-LVSPSTAIT-TWMKDGSNI-RESPKHRFIADG-KDRKLHIIDVQLSDAGEYTCVL- 11704
Cdd:cd05750       3 LKEMK----SQTVQEGSKLVLKCeATSENPSPRyRWFKDGKELnRKRPKNIKIRNKkKNSELQINKAKLEDSGEYTCVVe 78
                            90
                    ....*....|....*.
gi 1958765569 11705 -RLGNkeKTSTAKLIV 11719
Cdd:cd05750      79 nILGK--DTVTGNVTV 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4292-4387 2.18e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.02  E-value: 2.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4292 PVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYISSLEILRTQVVDCGEYTCKASNEYG 4371
Cdd:cd05762       2 PQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLG 81
                            90
                    ....*....|....*.
gi 1958765569  4372 SVSCTATLTVTEAYPP 4387
Cdd:cd05762      82 SRQAQVNLTVVDKPDP 97
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
2045-2128 2.18e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.48  E-value: 2.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2045 QSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIE-RSDRIYwywpEDNVCELVIRDVTAEDSASIMVKAINIAGETSSH 2123
Cdd:cd20952       7 QNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLgKDERIT----TLENGSLQIKGAEKSDTGEYTCVALNLSGEATWS 82

                    ....*
gi 1958765569  2124 AFLLV 2128
Cdd:cd20952      83 AVLDV 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
1051-1128 2.19e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 42.73  E-value: 2.19e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1051 EGGSVVFECQIGGNPKPHVYWKKSG--VPLTTGYRYKVSYnkQTGECRLVISMTFADDAGEYTIVIRNKHGETSASASLL 1128
Cdd:cd20974      14 EGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISF--SDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELL 91
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
19822-19897 2.19e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.83  E-value: 2.19e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 19822 GTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGvKMAMKRNLC---TLELFSVNRKDSGDYTITAENSSGSKSATIKLKV 19897
Cdd:cd05892      15 GDPVRLECQISAIPPPQIFWKKNNEMLQYNTD-RISLYQDNCgriCLLIQNANKKDAGWYTVSAVNEAGVVSCNARLDV 92
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4297-4381 2.21e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 42.86  E-value: 2.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4297 RIEPLE-----VALGHLAKFTCEI-QGAPNVRFQWFKAGREIYESDKCSIRSSN-YISSLEILRTQVVDCGEYTCKASNE 4369
Cdd:cd20959       3 RIIPFAfgegaAQVGMRAQLHCGVpGGDLPLNIRWTLDGQPISDDLGITVSRLGrRSSILSIDSLEASHAGNYTCHARNS 82
                            90
                    ....*....|..
gi 1958765569  4370 YGSVSCTATLTV 4381
Cdd:cd20959      83 AGSASYTAPLTV 94
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
7771-7852 2.21e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 42.61  E-value: 2.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7771 DTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNcGITTTERSSILEILESTIEDYAQYACLIENEAGQDICEALV 7850
Cdd:cd05730      12 NATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHL 90

                    ..
gi 1958765569  7851 SV 7852
Cdd:cd05730      91 KV 92
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
33423-33497 2.22e-03

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 42.44  E-value: 2.22e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33423 RDTTVSSDSVAKFVIKVTGEPQPTVTWTKDGKAI-AQSSKYKLSNDKEEFILEILKteTSDGGLYSCTVANSAGSV 33497
Cdd:cd04978       7 PSLVLSPGETGELICEAEGNPQPTITWRLNGVPIePAPEDMRRTVDGRTLIFSNLQ--PNDTAVYQCNASNVHGYL 80
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
6259-6349 2.22e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 42.54  E-value: 2.22e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6259 PKFV--KKLEASKIVK-AGDSARLECKITGSPEIRVVWYRNE-----HELTASDKYQMTfidsvavMQMNSLGTEDSGDF 6330
Cdd:cd05856       1 PRFTqpAKMRRRVIARpVGSSVRLKCVASGNPRPDITWLKDNkpltpPEIGENKKKKWT-------LSLKNLKPEDSGKY 73
                            90
                    ....*....|....*....
gi 1958765569  6331 ICEAQNPAGSTSCSTKVIV 6349
Cdd:cd05856      74 TCHVSNRAGEINATYKVDV 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
21987-22063 2.23e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.92  E-value: 2.23e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 21987 AGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKL-EIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNVKV 22063
Cdd:cd05857      18 AANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIgGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 95
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
25032-25227 2.23e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 47.25  E-value: 2.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25032 QMLVQWhepvnDGGSKVIGYHLEQKeKNSILWVKLNKIPiqDTKFKTTGLDEGlEYEFRVSAENIVGI-GKPSKVSECYV 25110
Cdd:COG4733     553 TLTVSW-----DAPAGAVAYEVEWR-RDDGNWVSVPRTS--GTSFEVPGIYAG-DYEVRVRAINALGVsSAWAASSETTV 623
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25111 ARDPcDPPGRPEAIIITRN--SVTLKWKKPTYDGGSKITGYIVEKKDLPDGRWMKASFTNvveTEFTVTGLVEDQRYEFR 25188
Cdd:COG4733     624 TGKT-APPPAPTGLTATGGlgGITLSWSFPVDADTLRTEIRYSTTGDWASATVAQALYPG---NTYTLAGLKAGQTYYYR 699
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1958765569 25189 VIARNAADNFSEPsesSGAITARDEIDAPNASLDPKYRD 25227
Cdd:COG4733     700 ARAVDRSGNVSAW---WVSGQASADAAGILDAITGQILE 735
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
24150-24227 2.23e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 42.61  E-value: 2.23e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 24150 NAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDfKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNVKV 24227
Cdd:cd05730      16 NLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNED-GSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8428-8509 2.24e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.57  E-value: 2.24e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8428 PESIKVTTGDTCTLECMVS-GTPELSTKWFKDGKELTGDSKYKISFFNK-VSGLKIISVAPGDSGVYSFEVQNPVGKDSC 8505
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

                    ....
gi 1958765569  8506 TVSI 8509
Cdd:pfam00047    83 STSL 86
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
33711-33787 2.25e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 42.21  E-value: 2.25e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33711 EGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSrsrNMYTLEIRNASVSDSGKYTVKAKNFRGQCSATASLTV 33787
Cdd:cd05876       9 RGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQN---HNKTLQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8234-8314 2.26e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 42.55  E-value: 2.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8234 PPVFRkkPFPVET-LKGADVHLECELQGTPPFQVSWYKDKRELRSGKKYKIMSENLLTsihILNVDTA-DIGEYQCKATN 8311
Cdd:cd20958       1 PPFIR--PMGNLTaVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNGTLV---IENVQRSsDEGEYTCTARN 75

                    ...
gi 1958765569  8312 DVG 8314
Cdd:cd20958      76 QQG 78
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
29585-29641 2.26e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 42.39  E-value: 2.26e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 29585 GKPEPKIIWTKGDKELDLC-EKVSLQYTGKratAVIKYCDRSDSGKYTLTVKNASGTK 29641
Cdd:cd05724      24 GHPEPTVSWRKDGQPLNLDnERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGER 78
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
24559-24622 2.26e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 42.39  E-value: 2.26e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24559 PFKGRPTPEITWSKEEGEFTDK---VQIEKGINftqLSIDNCDRNDAGKYILKLENSSG---SKSAFVTV 24622
Cdd:cd05724      21 PPRGHPEPTVSWRKDGQPLNLDnerVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGereSRAARLSV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
23751-23825 2.27e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.48  E-value: 2.27e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 23751 YSVQVGQDLKIEVPISGRPKPSISWTKDGAPLKqtTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVVGQKTA 23825
Cdd:cd20952       9 QTVAVGGTVVLNCQATGEPVPTISWLKDGVPLL--GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATW 81
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
6655-6727 2.27e-03

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409398  Cd Length: 101  Bit Score: 42.86  E-value: 2.27e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6655 LECKVAGSSPISIAWFHEKTKI--VSGAKYQTTFSDN----VCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTVQE 6727
Cdd:cd05735      23 MSCTAHGEKPIIVRWEKEDTIInpSEMSRYLVTTKEVgdevISTLQILPTVREDSGFFSCHAINSYGEDRGIIQLTVQE 101
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
9090-9175 2.27e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 42.67  E-value: 2.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9090 KLSE--TIEETEGNSFKLEGRVAGSQP-ITIAWYKNNVEI---HPTSNCEITFKNNALLLQVKKASMADAGLYTCKATND 9163
Cdd:cd05895       2 KLKEmkSQEVAAGSKLVLRCETSSEYPsLRFKWFKNGKEInrkNKPENIKIQKKKKKSELRINKASLADSGEYMCKVSSK 81
                            90
                    ....*....|..
gi 1958765569  9164 AGSALCTSSIVI 9175
Cdd:cd05895      82 LGNDSASANVTI 93
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
18431-18510 2.28e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.38  E-value: 2.28e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18431 TVRVGQTIRILARVKGRPEPDITWSKEGKVLvKDKRVDLIHDlprVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVNV 18510
Cdd:cd05725       8 VVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL-PKGRYEILDD---HSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
10811-11003 2.29e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.07  E-value: 2.29e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10811 KVPEIPKKPEEKVSVPVPKKEKAPPAKVPEvPKKPVPEEKAPvpvpkkvepppakvPEVPK---KPVPEKkvpaPTPKKV 10887
Cdd:NF033839    372 PKPEVKPQPETPKPEVKPQPEKPKPEVKPQ-PEKPKPEVKPQ--------------PEKPKpevKPQPEK----PKPEVK 432
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10888 EAPPAKAPEVPPKEVTpekkvpvvppkkpeapppkvpeppkevvpekkvsmvppKRPEAPPAkvPEAskevvPEKKVsva 10967
Cdd:NF033839    433 PQPEKPKPEVKPQPEK--------------------------------------PKPEVKPQ--PET-----PKPEV--- 464
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 1958765569 10968 pKKKPEAPAVKVPEAPKKVVPEKKVPVAAPKKPEAP 11003
Cdd:NF033839    465 -KPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTP 499
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
33709-33787 2.29e-03

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 42.76  E-value: 2.29e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 33709 INEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQCSATASLTV 33787
Cdd:cd20969      14 VDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4199-4286 2.30e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 42.73  E-value: 2.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4199 PTILKPLVDTISEKGDTVHLTSSISNAK--EVNWYFKGDLVP----PGAKFQClkEENAYTLVIESVKTEDEGEYVCEAS 4272
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPvpEVSWFRDGQVIStstlPGVQISF--SDGRAKLSIPAVTKANSGRYSLTAT 78
                            90
                    ....*....|....
gi 1958765569  4273 NGNGKAMTSAKLTV 4286
Cdd:cd20974      79 NGSGQATSTAELLV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12086-12170 2.30e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 42.79  E-value: 2.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12086 LKFISPLEDQTVKEGQTATFVCELSHE-KMHVVWFKNDVKL---HTTRTVLMSSEGKTYKLEIRETTLDDISQIKAQVKN 12161
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 12162 ----LSSTANLKV 12170
Cdd:cd20951      81 ihgeASSSASVVV 93
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
5791-5878 2.30e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.45  E-value: 2.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5791 PIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGkkytmSEKMSVFY-------LHITKCAPSDVGEYQC 5863
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYN-----TDRISLYQdncgricLLIQNANKKDAGWYTV 75
                            90
                    ....*....|....*
gi 1958765569  5864 IIANEGGSCACTARV 5878
Cdd:cd05892      76 SAVNEAGVVSCNARL 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5696-5787 2.30e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 42.55  E-value: 2.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5696 PPqFIKKPSPVLVLrNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYgISFVDGlaTFQISNA-RVENSGTYVCEARN 5774
Cdd:cd20958       1 PP-FIRPMGNLTAV-AGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQ-RVFPNG--TLVIENVqRSSDEGEYTCTARN 75
                            90
                    ....*....|....
gi 1958765569  5775 DAG-TASCSIELKV 5787
Cdd:cd20958      76 QQGqSASRSVFVKV 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
2588-2649 2.31e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 42.39  E-value: 2.31e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  2588 DQTVAESQEAVFECE--VANPESEGEWLKDGKHLTLSNNFRSESDGHKrrLVIAAAKLDDIGEY 2649
Cdd:cd05724       6 DTQVAVGEMAVLECSppRGHPEPTVSWRKDGQPLNLDNERVRIVDDGN--LLIAEARKSDEGTY 67
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
8634-8701 2.31e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 42.63  E-value: 2.31e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8634 VKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEAGRASCTTQLFVK 8701
Cdd:cd05736      24 AEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVE 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
30641-30743 2.33e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.02  E-value: 2.33e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30641 EMLEYPDyelDERYQEGVFVRQGGVIRLTIPIKgkpfpiCKWTK------EGQDVSkramIATSETHTELVIKEADRNDS 30714
Cdd:cd05762       3 QIIQFPE---DMKVRAGESVELFCKVTGTQPIT------CTWMKfrkqiqEGEGIK----IENTENSSKLTITEGQQEHC 69
                            90       100
                    ....*....|....*....|....*....
gi 1958765569 30715 GTYDLVLENKCGKKTVYIKVKVIGSPNTP 30743
Cdd:cd05762      70 GCYTLEVENKLGSRQAQVNLTVVDKPDPP 98
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
24824-24906 2.33e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 42.55  E-value: 2.33e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24824 PSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATS-----TILHIKESSKDDFGKYSVTA 24898
Cdd:cd20956       2 PVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYVTSdgdvvSYVNISSVRVEDGGEYTCTA 81

                    ....*...
gi 1958765569 24899 TNNAGTAT 24906
Cdd:cd20956      82 TNDVGSVS 89
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
5909-5966 2.34e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.00  E-value: 2.34e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5909 GSPPISITWLKDDQILEENDNVHISfedsvatlqvrSVDNGHSGRYTCQAKNESGVER 5966
Cdd:pfam13895    25 GNPPPSYTWYKDGSAISSSPNFFTL-----------SVSAEDSGTYTCVARNGRGGKV 71
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
5528-5600 2.34e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 42.18  E-value: 2.34e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5528 IDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNtafLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTV 5600
Cdd:cd05723      15 IVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
26985-27065 2.35e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.17  E-value: 2.35e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26985 PPEIdmkNFPSHTVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAA 27064
Cdd:pfam13927     1 KPVI---TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

                    .
gi 1958765569 27065 N 27065
Cdd:pfam13927    78 N 78
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
25628-25705 2.35e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.57  E-value: 2.35e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25628 VVTLRASATLRLFVtIKGRPEPEVKWEKAEGILTERAQIEVTSSYTM---LVIDNVTRFDSGRYNLTLENNSGSKTAFVN 25704
Cdd:pfam00047     7 TVLEGDSATLTCSA-STGSPGPDVTWSKEGGTLIESLKVKHDNGRTTqssLLISNVTKEDAGTYTCVVNNPGGSATLSTS 85

                    .
gi 1958765569 25705 V 25705
Cdd:pfam00047    86 L 86
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6-98 2.35e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 42.55  E-value: 2.35e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQvistsTLP--GVQISFSDGraRLMIPAVTKA-NSGRYSLRA 82
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGR-----RLPlnHRQRVFPNG--TLVIENVQRSsDEGEYTCTA 73
                            90
                    ....*....|....*.
gi 1958765569    83 TNGSGQaTSTAELLVT 98
Cdd:cd20958      74 RNQQGQ-SASRSVFVK 88
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
8801-8886 2.35e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.23  E-value: 2.35e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8801 KQLEP-LKVTVGDSASLQCQLAGtPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAensvGEVS 8879
Cdd:cd20967       1 KKAQPaVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA----GGEK 75

                    ....*..
gi 1958765569  8880 SSTFLTV 8886
Cdd:cd20967      76 CSFELFV 82
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
33434-33505 2.36e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.50  E-value: 2.36e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33434 KFVIK---VTGEPQPTVTWTKDGKAI--AQSSKYKLSNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd05750      16 KLVLKceaTSENPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
16361-16427 2.36e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.02  E-value: 2.36e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 16361 KAKKAMKDGihdipEDAQLETAENSSVIVIPECTRAHSGKYSITAKNKAGQKTANCRVKVMDAPGPP 16427
Cdd:cd05762      37 KFRKQIQEG-----EGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVDKPDPP 98
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
4588-4667 2.36e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 42.92  E-value: 2.36e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4588 GESARLHCKLKGSPVIQVT--WFKNNKEL----SESNTVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEV 4661
Cdd:cd04970      17 GENATLQCHASHDPTLDLTftWSFNGVPIdlekIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSDSASATL 96

                    ....*.
gi 1958765569  4662 VIKEPP 4667
Cdd:cd04970      97 VVRGPP 102
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
27809-27872 2.36e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.36e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 27809 GRPPPTVTWRKDEKNLGSDARYSIQNTDSSSL-LVIPQVTRNDTGKYILTIENGVGQPKSS-TVSV 27872
Cdd:cd05737      27 GDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVyFTINGVSSEDSGKYGLVVKNKYGSETSDvTVSV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
15918-15998 2.37e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.48  E-value: 2.37e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15918 DTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIeKPTDALNITKEEVSRSeaktELSIPKAVREDKGTYTITASNRLGS 15997
Cdd:cd05744       8 GDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPV-RPDSAHKMLVRENGRH----SLIIEPVTKRDAGIYTCIARNRAGE 82

                    .
gi 1958765569 15998 V 15998
Cdd:cd05744      83 N 83
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
29569-29650 2.37e-03

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 42.61  E-value: 2.37e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29569 VTIRAGSDLVLDAAVGGKPEPKIIWTK-GDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMV 29647
Cdd:cd05763       9 ITIRAGSTARLECAATGHPTPQIAWQKdGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATL 88

                    ...
gi 1958765569 29648 KVL 29650
Cdd:cd05763      89 TVL 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5145-5216 2.38e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 42.63  E-value: 2.38e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  5145 QLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGS 5216
Cdd:cd05762      11 MKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGS 82
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
22670-22749 2.39e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.59  E-value: 2.39e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22670 TVLAGEDLKIDVPFIGRPTPTVTWHKDD--VPLKQTTRVNAESTENNSlLTIKEACREDVGHYTVKLTNSAGeaTETLNV 22747
Cdd:cd05891      12 TIMEGKTLNLTCTVFGNPDPEVIWFKNDqdIELSEHYSVKLEQGKYAS-LTIKGVTSEDSGKYSINVKNKYG--GETVDV 88

                    ..
gi 1958765569 22748 IV 22749
Cdd:cd05891      89 TV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5420-5491 2.39e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.57  E-value: 2.39e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5420 EAVSIDVTQGDPATLQVK-FSGTKEISAKWFKDGQELTLGPKYKISVTD-TVSILKIISTEKKDSGEYTFEVQN 5491
Cdd:pfam00047     2 APPTVTVLEGDSATLTCSaSTGSPGPDVTWSKEGGTLIESLKVKHDNGRtTQSSLLISNVTKEDAGTYTCVVNN 75
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
5610-5691 2.39e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.57  E-value: 2.39e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5610 PQSQDVNPSTRVQLKALVGGTAPMT-IKWFKDNKELHPGA-ARSVWKDDTSTILELFSAKAADSGTYICQLSNDVGTTSS 5687
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSASTGSPGPdVTWSKEGGTLIESLkVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

                    ....
gi 1958765569  5688 KATI 5691
Cdd:pfam00047    83 STSL 86
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
12889-12959 2.40e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.50  E-value: 2.40e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12889 LRPLTDLQVKEKETARFECEISKEN--VKVQWFKDGAEIKKGKKYDII---SKGAVRiLVINKCLLNDEAEYSCEV 12959
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLKCEATSENpsPRYRWFKDGKELNRKRPKNIKirnKKKNSE-LQINKAKLEDSGEYTCVV 77
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
9581-9653 2.41e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 42.38  E-value: 2.41e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  9581 PAWERHLQD-VTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLkpQGRVKTEVEHKvHKLTIADVRAEDQGRYTCK 9653
Cdd:cd20978       1 PKFIQKPEKnVVVKGGQDVTLPCQVTgVPQPKITWLHNGKPL--QGPMERATVED-GTLTIINVQPEDTGYYGCV 72
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2588-2664 2.46e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.52  E-value: 2.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2588 DQTVAESQEAVFECEV-ANPESEGEWLKDGKHLTLSNNFRSESDGhkrRLVIAAAKLDDIGEYTYKVA----TSKTSAKL 2662
Cdd:cd20957      10 VQTVDFGRTAVFNCSVtGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRndgdSAQATAEL 86

                    ..
gi 1958765569  2663 KV 2664
Cdd:cd20957      87 KL 88
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
6735-6808 2.46e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.46e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6735 PEPLEILPGKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIYFED-TVAELELFNIDVSQSGEYTCVVSNNAG 6808
Cdd:cd05737       8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYG 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
25231-25303 2.46e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 42.57  E-value: 2.46e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 25231 VRAGETFVLEADIRGKPIPDIVWSKDGNELEETaARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKT 25303
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNS-PDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDT 84
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
1807-1890 2.46e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 42.61  E-value: 2.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGihYLDIVDCKSYDTGEVKVTAENPEGVTEHK-V 1885
Cdd:cd20968       6 PTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLESG--SLRIHNVQKEDAGQYRCVAKNSLGIAYSKpV 83

                    ....*
gi 1958765569  1886 KLEIQ 1890
Cdd:cd20968      84 TIEVE 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
23478-23542 2.47e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.38  E-value: 2.47e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 23478 IKGRPTPEVKWGKVDGE--IRDAAIIDVTSsftsLVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRV 23542
Cdd:cd05725      21 VGGDPVPTVRWRKEDGElpKGRYEILDDHS----LKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
19817-19897 2.48e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.52  E-value: 2.48e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19817 LTVKAGTNVCLDATVFGKPMPTVSWKKDSTPIKQTEGVKMAMKRnlcTLELFSVNRKDSGDYTITAENSSGSKSATIKLK 19896
Cdd:cd20957      11 QTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGDSAQATAELK 87

                    .
gi 1958765569 19897 V 19897
Cdd:cd20957      88 L 88
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
7214-7294 2.48e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 42.92  E-value: 2.48e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7214 QGESIQLECKISGSP--EIKVVWFRNDSELH----ESWKYNMSFVNSVALLTINEASVEDTGDYICEAHNGVGHASCSTA 7287
Cdd:cd04970      16 VGENATLQCHASHDPtlDLTFTWSFNGVPIDlekiEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSDSASAT 95

                    ....*..
gi 1958765569  7288 LKVKAPP 7294
Cdd:cd04970      96 LVVRGPP 102
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
7485-7570 2.49e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.23  E-value: 2.49e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7485 EKPEP-MTVTTGNPFTLECVVAGtPELSAKWLKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEvensVGKSS 7563
Cdd:cd20967       1 KKAQPaVQVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV----AGGEK 75

                    ....*..
gi 1958765569  7564 CTVSVHV 7570
Cdd:cd20967      76 CSFELFV 82
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
4390-4476 2.51e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 42.18  E-value: 2.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4390 LSRPKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRITDadnKHSLELSNLTVQDRGVYSCKASNKFGADI 4469
Cdd:cd05723       1 LKKPSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVK---EHNLQVLGLVKSDEGFYQCIAENDVGNAQ 77

                    ....*..
gi 1958765569  4470 CQAELTI 4476
Cdd:cd05723      78 ASAQLII 84
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8434-8511 2.51e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 42.48  E-value: 2.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8434 TTGDTCTLECMVS-GTPELSTKWFKDGKELTGDSKYKISFFN-KVSGLKIISVAPGDSGVYSFEVQNPVGKDSCTVSIQV 8511
Cdd:cd20959      15 QVGMRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSRLGrRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
3020-3102 2.51e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 42.73  E-value: 2.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3020 FRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQ--ELQIVDRIKIQKEKYVHRLLIPSARMSDAGKYTVVA----G 3092
Cdd:cd20974       3 FTQPLQSVVVLEGSTATFEAHVSgKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTAtngsG 82
                            90
                    ....*....|
gi 1958765569  3093 GNMSTANLFV 3102
Cdd:cd20974      83 QATSTAELLV 92
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
5155-5227 2.51e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 42.23  E-value: 2.51e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5155 LVCKVTGTPPIKITWFANDRELRESSKhkMSFVESTAvLRLTDVAIEDSGEYMCEAQNEAGSDHCTSIVIVKE 5227
Cdd:cd20968      19 LPCTTMGNPKPSVSWIKGDDLIKENNR--IAVLESGS-LRIHNVQKEDAGQYRCVAKNSLGIAYSKPVTIEVE 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8141-8218 2.51e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.45  E-value: 2.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8141 PRFIKKLDQSRIVKQDEyTRYECKIGGSPEIKVLWYKD-EVEIQESSKFRMSFEDSVAI-LEMHNLSVEDSGDYTCEARN 8218
Cdd:cd05892       1 PMFIQKPQNKKVLEGDP-VRLECQISAIPPPQIFWKKNnEMLQYNTDRISLYQDNCGRIcLLIQNANKKDAGWYTVSAVN 79
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
1265-1329 2.52e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 42.92  E-value: 2.52e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  1265 TFHCKMSGYPLPKIAWYKDGKRI---RRGERYQMDFLQDGraSLRIPVVLP-----EDEGIYTAFASNIKGNA 1329
Cdd:cd07693      19 TLNCKAEGRPTPTIQWLKNGQPLetdKDDPRSHRIVLPSG--SLFFLRVVHgrkgrSDEGVYVCVAHNSLGEA 89
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
19420-19491 2.52e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.45  E-value: 2.52e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 19420 ITIKAGKKLRVEAHVYGKPNPICKWKKGEDDVVTSSHLAIhKADSSsvLIIKDVTRKDSGYYSLTAENSSGT 19491
Cdd:cd04969      12 ILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICI-LPDGS--LKIKNVTKSDEGKYTCFAVNFFGK 80
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
5530-5590 2.52e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 42.63  E-value: 2.52e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  5530 LECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAG 5590
Cdd:cd05736      20 LRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
21591-21667 2.53e-03

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 42.68  E-value: 2.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21591 AGDNIKVEIPVLGRPKPTVTWKK--GDQI-----LKQTQRVNVENTATSTILNINEcvrSDSGAYPLTAKNTVGE-VGDV 21662
Cdd:cd20954      15 AGQDVMLHCQADGFPTPTVTWKKatGSTPgeykdLLYDPNVRILPNGTLVFGHVQK---ENEGHYLCEAKNGIGSgLSKV 91

                    ....*
gi 1958765569 21663 ITIQV 21667
Cdd:cd20954      92 IFLKV 96
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
3199-3288 2.53e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 42.39  E-value: 2.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3199 PQVLQELQPVTVQSGKPARFCAVIAGRPQPKISWYKEEQLLSTGFKCKFL-HDGQEYTLLLIEAFPEDAAVYTCEAKNDY 3277
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLvRENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569  3278 GVATTSASLSV 3288
Cdd:cd20990      81 GQNSFNLELVV 91
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2670-2752 2.54e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.23  E-value: 2.54e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2670 KKTLRNLTVTETQDAIFSVELTHPDVKgVQWIKNGVVLDSNDKYEISVKGTLYSLKIKNCAMADESVYGFKLGRLGASAR 2749
Cdd:cd20967       1 KKAQPAVQVSKGHKIRLTVELADPDAE-VKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFE 79

                    ...
gi 1958765569  2750 LHV 2752
Cdd:cd20967      80 LFV 82
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
30265-30340 2.56e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.56e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 30265 GRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHT-KVAKLTIRETTIRDTGEYMLELKNVTGttSETIKVVI 30340
Cdd:cd05737      16 GKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYG--SETSDVTV 90
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
14207-14292 2.56e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.59  E-value: 2.56e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14207 KLLAGL----TVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIE-NVPKKSTVTITDSKRSDTGTYIIEAVNVC 14281
Cdd:cd05891       2 KVIGGLpdvvTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKlEQGKYASLTIKGVTSEDSGKYSINVKNKY 81
                            90
                    ....*....|.
gi 1958765569 14282 GRATAVVEVNV 14292
Cdd:cd05891      82 GGETVDVTVSV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
9099-9176 2.57e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 42.19  E-value: 2.57e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9099 EGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATNDAGSAlcTSSIVIR 9176
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEK--SATINVK 81
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
3591-3660 2.57e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 42.54  E-value: 2.57e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  3591 GIPAVFEYLVHGEPAPTVLWFKEDMPLYTNVCYTIIHN---PDGSGTF---IVNDPQRGDSGLYICKAENLWGTST 3660
Cdd:cd07693      15 GDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRivlPSGSLFFlrvVHGRKGRSDEGVYVCVAHNSLGEAV 90
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5253-5316 2.57e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 42.55  E-value: 2.57e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5253 AGTPPFEITWFKDNTTL-RSGR----KYKTfIQDQLVS-LQILKFVASDAGEYQCRVTNEVGSSTCSARV 5316
Cdd:cd20956      26 SGNPLPQITWTLDGFPIpESPRfrvgDYVT-SDGDVVSyVNISSVRVEDGGEYTCTATNDVGSVSHSARI 94
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
8809-8888 2.58e-03

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409398  Cd Length: 101  Bit Score: 42.86  E-value: 2.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8809 TVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNN------VATLVFTQVDSNDSGEYICRAENSVGEVSSST 8882
Cdd:cd05735      16 TKGQKKEMSCTAHGEKPIIVRWEKEDTIINPSEMSRYLVTTKevgdevISTLQILPTVREDSGFFSCHAINSYGEDRGII 95

                    ....*.
gi 1958765569  8883 FLTVQE 8888
Cdd:cd05735      96 QLTVQE 101
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
2582-2664 2.58e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 42.38  E-value: 2.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2582 ISKPLTDQTVAESQEAVFECEVA-NPESEGEWLKDGKHLTlSNNFRseSDGHKRRLVIAAAKLDDIGEYTYkVATS---- 2656
Cdd:cd20978       4 IQKPEKNVVVKGGQDVTLPCQVTgVPQPKITWLHNGKPLQ-GPMER--ATVEDGTLTIINVQPEDTGYYGC-VATNeigd 79

                    ....*....
gi 1958765569  2657 -KTSAKLKV 2664
Cdd:cd20978      80 iYTETLLHV 88
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
23452-23535 2.60e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.45  E-value: 2.60e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23452 PDIDLDlELRKVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSSfTSLVLDNVNRYDSGKYTLTLENSS 23531
Cdd:cd04969       1 PDFELN-PVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPD-GSLKIKNVTKSDEGKYTCFAVNFF 78

                    ....
gi 1958765569 23532 GTKS 23535
Cdd:cd04969      79 GKAN 82
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
12003-12067 2.60e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 42.18  E-value: 2.60e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 12003 PLKDVTVPEKRQARFECVLTREAN--VIWSKGPDIIKASDKFDIIADGKKHI-LVINDSQFDDEGVYT 12067
Cdd:cd20973       3 TLRDKEVVEGSAARFDCKVEGYPDpeVKWMKDDNPIVESRRFQIDQDEDGLCsLIISDVCGDDSGKYT 70
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
24548-24618 2.62e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 42.54  E-value: 2.62e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 24548 VRAGGSARIHIPFKGRPTPEITWSK----EEGEFTDKVQIEKGI---NFTQLSIDNCDRNDAGKYILKLENSSGSKSA 24618
Cdd:cd05765      12 VKVGETASFHCDVTGRPQPEITWEKqvpgKENLIMRPNHVRGNVvvtNIGQLVIYNAQPQDAGLYTCTARNSGGLLRA 89
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8235-8325 2.63e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 42.34  E-value: 2.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKR--ELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATND 8312
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                            90
                    ....*....|...
gi 1958765569  8313 VGSDTCVGSVTLK 8325
Cdd:cd20974      81 SGQATSTAELLVL 93
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
20506-20582 2.65e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.50  E-value: 2.65e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20506 AKENSNFRLKIPIKGKPAPSVSWK-KGEDPLATDTRVSVESTavNTTLVVYDCQKSDAGKYTITLKNVAG---TKEGTLS 20581
Cdd:cd20970      14 AREGENATFMCRAEGSPEPEISWTrNGNLIIEFNTRYIVREN--GTTLTIRNIRRSDMGIYLCIASNGVPgsvEKRITLQ 91

                    .
gi 1958765569 20582 I 20582
Cdd:cd20970      92 V 92
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
8535-8607 2.66e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 42.18  E-value: 2.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8535 VVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNtcaLTVNMLEDADAGDYTCIATNVAGSDECSAPLTV 8607
Cdd:cd05723      15 IVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2674-2737 2.66e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 2.66e-03
                             10        20        30        40        50        60
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569   2674 RNLTVTETQDAIFSVELTHPDVKGVQWIKNG-VVLDSNDKYEISVKGTLYSLKIKNCAMADESVY 2737
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTY 66
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
32223-32293 2.66e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 32223 TITVHPEPRVTWYKSGQKIKPGDddkKYTFESDKGLY-QLTINSVTTDDDAEYAVVARNKHGEDSCKAKLTV 32293
Cdd:cd05737      24 NVWGDPPPEVSWLKNDQALAFLD---HCNLKVEAGRTvYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
25228-25303 2.67e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 42.32  E-value: 2.67e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 25228 VIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEiKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGTKT 25303
Cdd:cd20949       8 VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMS-KYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
21980-22063 2.67e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.59  E-value: 2.67e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21980 KDTITLKAGEAFKLEADVSGRPPPTMEWAKDGKELEGTGKLEI-KIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHI 22058
Cdd:cd05729      11 EREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGtKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHT 90

                    ....*
gi 1958765569 22059 FNVKV 22063
Cdd:cd05729      91 YDVDV 95
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
3602-3667 2.70e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.45  E-value: 2.70e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  3602 GEPAPTVLWFKEDMPLYTN--VCYTiihnPDGSgTFIVNdPQRGDSGLYICKAENLWGTSTCTAELLV 3667
Cdd:cd04969      28 ASPKPTISWSKGTELLTNSsrICIL----PDGS-LKIKN-VTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
26985-27070 2.70e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 42.55  E-value: 2.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26985 PPEIdMKNFPSHTVyvRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRF--NTEITAENLTI---NLKESVTADAGKY 27059
Cdd:cd20956       1 APVL-LETFSEQTL--QPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFrvGDYVTSDGDVVsyvNISSVRVEDGGEY 77
                            90
                    ....*....|.
gi 1958765569 27060 EITAANSSGTT 27070
Cdd:cd20956      78 TCTATNDVGSV 88
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
33705-33787 2.71e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 42.67  E-value: 2.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33705 RSQNINEGQNVLFSCEISGE-PSPEIEWFKN-------NLPISISSNISVSRSRnmytLEIRNASVSDSGKYTVKAKNFR 33776
Cdd:cd05895       7 KSQEVAAGSKLVLRCETSSEyPSLRFKWFKNgkeinrkNKPENIKIQKKKKKSE----LRINKASLADSGEYMCKVSSKL 82
                            90
                    ....*....|.
gi 1958765569 33777 GQCSATASLTV 33787
Cdd:cd05895      83 GNDSASANVTI 93
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
33891-33985 2.71e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 42.92  E-value: 2.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33891 PPKIEALPSDISIAEGKVLTVACAFTGEPTPEIT--WSCGGRRIQSQEQQGRFH-IENTDDLTTLIIMDVQKQDGGLYTL 33967
Cdd:cd04970       2 ATRITLAPSNADITVGENATLQCHASHDPTLDLTftWSFNGVPIDLEKIEGHYRrRYGKDSNGDLEIVNAQLKHAGRYTC 81
                            90
                    ....*....|....*...
gi 1958765569 33968 SLGNEFGSDSATVNINIR 33985
Cdd:cd04970      82 TAQTVVDSDSASATLVVR 99
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
6929-6998 2.71e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.71e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  6929 GDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYF-TNNVATLVFNKVGINDSGEYTCVAENSIGTAAS 6998
Cdd:cd05737      16 GKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVeAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETS 86
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5042-5132 2.71e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 42.34  E-value: 2.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5042 PSFVTKPESRDVLPGSAVCLKSAFQGSTPLTIRWFKgDKELVSGGS---CYITKEASESSLELYAVKTTDSGTYTCKVSN 5118
Cdd:cd20974       1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFR-DGQVISTSTlpgVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                            90
                    ....*....|....
gi 1958765569  5119 VAGSVECSANLFVK 5132
Cdd:cd20974      80 GSGQATSTAELLVL 93
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
32900-32975 2.71e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 42.33  E-value: 2.71e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32900 GQNTRFILNVQS-KPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAVCTNYKGEASDYATLDV 32975
Cdd:cd20927      14 GGHVKYVCKIENyDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
10925-11455 2.72e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 2.72e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10925 EPPKEVV-----PEKKVSMVPPKR-------------------PEAPPAKVPEASKEVVPEKKvsvaPKKKPEAPAVKVP 10980
Cdd:PHA03247   2510 PAPSRLApailpDEPVGEPVHPRMltwirgleelasddagdppPPLPPAAPPAAPDRSVPPPR----PAPRPSEPAVTSR 2585
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10981 EAPKKVVPEK---KVPVAAPKKPEAPAAEVPEVPKAAVPQKKIPEavppkpespppevyeepaeeivpeeppeevveepe 11057
Cdd:PHA03247   2586 ARRPDAPPQSarpRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS----------------------------------- 2630
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11058 papppkvtvpPKKPVPEKKAPPAVVKKPEPPPAKAPEVPKEAPPEKKVPSVVPKKPEAPPA--KVPEVPKEVVPEKKVAV 11135
Cdd:PHA03247   2631 ----------PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrpRRRAARPTVGSLTSLAD 2700
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11136 PKkpevPPAKVPEVPKKPVVEEKPVieekPAIPVAEKVESPPTEVYEEPEEVAAQEEEPAPVVEEEEYEAPPPPAPEIPV 11215
Cdd:PHA03247   2701 PP----PPPPTPEPAPHALVSATPL----PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPP 2772
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11216 PQVPEEPKKVVPEKKYPVIKKPEPPPPKVPEVSKKPAPMkkvpvvkkpeppEAEVPEVPKKLAPVKKEPVPVTKKPEVLP 11295
Cdd:PHA03247   2773 AAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAV------------LAPAAALPPAASPAGPLPPPTSAQPTAPP 2840
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11296 EKVPEAPKKITPEKRESAPVPEEPEAPPAPVEEIPeetiyEEKATITIGRKETPPVeEREIERFIQP-EEPGMEPQPEET 11374
Cdd:PHA03247   2841 PPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKP-----AAPARPPVRRLARPAV-SRSTESFALPpDQPERPPQPQAP 2914
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11375 PVQEPEPEKKVIEKPKLKPRPPIRAPSPPKEDVkekifQLKAVSKKKVPEKPEVVEKVEPTPLKVPtaekkvRKLLPEPK 11454
Cdd:PHA03247   2915 PPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTT-----DPAGAGEPSGAVPQPWLGALVPGRVAVP------RFRVPQPA 2983

                    .
gi 1958765569 11455 P 11455
Cdd:PHA03247   2984 P 2984
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
2764-2839 2.72e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.23  E-value: 2.72e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  2764 VTALENATVAFEVSvSHDTvPVKWFHKNVEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVVGQLECKAKLFV 2839
Cdd:cd20967       9 VSKGHKIRLTVELA-DPDA-EVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
15200-15310 2.74e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 2.74e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  15200 SLEVKRGDEIALDATISGSPYPTITWIKDENVIVPEeikkrvappvrrkkgeaeeeepftlplTERLSINNSKqGESQLR 15279
Cdd:smart00410     3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAE---------------------------SGRFSVSRSG-STSTLT 54
                             90       100       110
                     ....*....|....*....|....*....|.
gi 1958765569  15280 VRDSLRPDHGQYMIKVENDHGVAKAPCTVSV 15310
Cdd:smart00410    55 ISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
32319-32396 2.74e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.74e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 32319 EGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDYYALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:cd05737      15 EGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
26709-26786 2.74e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 2.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26709 TVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLrtrAYID------STDSRTSLTIENANRNDSGKYTLTIQNVLSAASMTF 26782
Cdd:cd05737      12 TIMEGKTLNLTCNVWGDPPPEVSWLKNDQAL---AFLDhcnlkvEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDV 88

                    ....
gi 1958765569 26783 VVKV 26786
Cdd:cd05737      89 TVSV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
18723-18805 2.76e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 2.76e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18723 LTVKAGDTIRLEAGVRGKPFPEVAWTkdKDATDLTRSP-RVKIDtsAESSKFSLTKAKRSDGGKYVVTATNPAGSFVAYA 18801
Cdd:cd20976      11 LEAVEGQDFVAQCSARGKPVPRITWI--RNAQPLQYAAdRSTCE--AGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSA 86

                    ....
gi 1958765569 18802 TVNV 18805
Cdd:cd20976      87 WVTV 90
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
28467-28564 2.78e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 42.63  E-value: 2.78e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28467 PPTVEFGPeyfDGLVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAK 28546
Cdd:cd05762       1 PPQIIQFP---EDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVE 77
                            90
                    ....*....|....*...
gi 1958765569 28547 NVSGSTKAEITVKVQDTP 28564
Cdd:cd05762      78 NKLGSRQAQVNLTVVDKP 95
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
1038-1127 2.78e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 42.46  E-value: 2.78e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1038 PFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRyKVSYNKQTGECRLVISMTFADDAGEYTIVIRNK 1117
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQR-RFAEEAEGGLCRLRILAAERGDAGFYTCKAVNE 79
                            90
                    ....*....|
gi 1958765569  1118 HGETSASASL 1127
Cdd:cd20975      80 YGARQCEARL 89
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
9196-9262 2.78e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.53  E-value: 2.78e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9196 GDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRC-SFSFASGTAVLELKDTAKADSGDYVCKASNVAGS 9262
Cdd:cd05857      19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIgGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGS 86
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
12530-12614 2.80e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.48  E-value: 2.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12530 PYFTGKLQDYTGVEKDEVVLQCEISKADAP-VKWFKDGKEIKP-SKNAVIKADGKKRMLILKKALKSDIGQYTC----DC 12603
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPdLFWQLNGKPVRPdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCiarnRA 80
                            90
                    ....*....|.
gi 1958765569 12604 GTDQTSGKLDI 12614
Cdd:cd05744      81 GENSFNAELVV 91
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
9590-9665 2.80e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 42.23  E-value: 2.80e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  9590 VTLKEGQTCTMTCQFSVPNVKSEWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGRYTCKHEDLETSAELRI 9665
Cdd:cd20967       7 VQVSKGHKIRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFELFV 82
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
12801-12870 2.81e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.00  E-value: 2.81e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 12801 KPLEDQTVEEEATAVLECEVSRENA-KVKWFKNGTEILKSKkYEIVADgrvRKLIIHGCTPEDIKTYTCDA 12870
Cdd:cd05725       2 KRPQNQVVLVDDSAEFQCEVGGDPVpTVRWRKEDGELPKGR-YEILDD---HSLKIRKVTAGDMGSYTCVA 68
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
7308-7382 2.81e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 42.13  E-value: 2.81e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7308 GSDVILQCEISGTPPFEVVWVKDRKQVRSSK-KFKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCACTVK 7382
Cdd:cd05894      10 GNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVK 85
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
8910-8973 2.81e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.53  E-value: 2.81e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8910 VVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSFLDN----IATLNIFKTDRslaGQYSCTVTNPIGS 8973
Cdd:cd05857      22 VKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNqhwsLIMESVVPSDK---GNYTCVVENEYGS 86
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
6360-6435 2.81e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 42.29  E-value: 2.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6360 PVVETLKNTEVS------LECE-LSGTPPFEVVWYKDKRQLRSSKK---YKIASKNFHASIHILNVDSTDIGEYHCKAQN 6429
Cdd:cd05895       1 PKLKEMKSQEVAagsklvLRCEtSSEYPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSS 80

                    ....*.
gi 1958765569  6430 EVGSDT 6435
Cdd:cd05895      81 KLGNDS 86
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
23755-23829 2.83e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.20  E-value: 2.83e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 23755 VGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSldltTLSIKETHKDDGGHYGITVANVVGQKTAAIEI 23829
Cdd:cd05728      13 IGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAG----DLRITKLSLSDSGMYQCVAENKHGTIYASAEL 83
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
6266-6350 2.83e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 42.01  E-value: 2.83e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6266 EASKIVKAGDSARLECKITGSPEIRVVWYRNEHEL----TASDKYQMTF-IDSVAvmqmnslgTEDSGDFICEAQNPAGS 6340
Cdd:cd05731       2 ESSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGELpkgrTKFENFNKTLkIENVS--------EADSGEYQCTASNTMGS 73
                            90
                    ....*....|
gi 1958765569  6341 TSCSTKVIVK 6350
Cdd:cd05731      74 ARHTISVTVE 83
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
5712-5787 2.84e-03

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 42.38  E-value: 2.84e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5712 GQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARNDAGTASCSIELKV 5787
Cdd:cd20969      17 GHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
25219-25310 2.84e-03

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 42.38  E-value: 2.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25219 ASLDPKYRDVIIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMEIKsTLQKTTLTVKDCIRTDGGQYTLKLSNV 25298
Cdd:cd20969       2 AAIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLT-VFPDGTLEVRYAQVQDNGTYLCIAANA 80
                            90
                    ....*....|..
gi 1958765569 25299 GGTKTIPITVKV 25310
Cdd:cd20969      81 GGNDSMPAHLHV 92
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
21286-21366 2.86e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.59  E-value: 2.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21286 PDFELDAELRRTLVVR-AGLSIRIFVPIKGRPAPEVTWTKDNINLKHRANIENTE----SFTLLI---IPEcnryDTGKF 21357
Cdd:cd05729       1 PRFTDTEKMEEREHALpAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKveekGWSLIIeraIPR----DKGKY 76

                    ....*....
gi 1958765569 21358 VMTIENPAG 21366
Cdd:cd05729      77 TCIVENEYG 85
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
4495-4569 2.88e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.20  E-value: 2.88e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4495 KKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIYFED-KIASLEIPLAKLKDSGTYSCTASNEAGSSSSSATVAV 4569
Cdd:cd05891      17 KTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
5523-5590 2.88e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.20  E-value: 2.88e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5523 IKGSFIDLECIVAGSHPISIQWFKDDQEISASDKYKFSFHDNT-AFLEISQLEGTDSGTYTCSATNKAG 5590
Cdd:cd05891      14 MEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYG 82
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
28079-28164 2.90e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 42.39  E-value: 2.90e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28079 EIPGaQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKI-TLSIKNVKKENGGKYTVILDNAVCRN 28157
Cdd:cd20990       5 QAPG-DLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVhSLIIEPVTSRDAGIYTCIATNRAGQN 83

                    ....*..
gi 1958765569 28158 SFPITII 28164
Cdd:cd20990      84 SFNLELV 90
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
23752-23822 2.92e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.59  E-value: 2.92e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 23752 SVQVGQDLKIEVPISGRPKPSISWTKDGAPLKQTTRINVIDSLDLT-TLSIKETHKDDGGHYGITVANVVGQ 23822
Cdd:cd05729      15 ALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGS 86
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
9590-9651 2.94e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.20  E-value: 2.94e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  9590 VTLKEGQTCTMTCQ-FSVPNVKSEWFRNGRVLKPQGRVKTEVEH-KVHKLTIADVRAEDQGRYT 9651
Cdd:cd05891      11 VTIMEGKTLNLTCTvFGNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYS 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
25932-25987 2.94e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.18  E-value: 2.94e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 25932 GRPQATVAWKKDGQVLRETTRVNVSS-SKIVTTLSIKEASREDVGTYeLCVSNTAGS 25987
Cdd:pfam00047    23 GSPGPDVTWSKEGGTLIESLKVKHDNgRTTQSSLLISNVTKEDAGTY-TCVVNNPGG 78
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
32076-32170 2.95e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.06  E-value: 2.95e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32076 SIEIGPVSGQImhaIGEEGGYVKYVCKIENYDQSTqVTWYFGVRQLENSEKYEITyEDGvaTMYVKDITKFDDGTYRCKV 32155
Cdd:cd04969       2 DFELNPVKKKI---LAAKGGDVIIECKPKASPKPT-ISWSKGTELLTNSSRICIL-PDG--SLKIKNVTKSDEGKYTCFA 74
                            90
                    ....*....|....*
gi 1958765569 32156 VNDYGEDSSYAELFV 32170
Cdd:cd04969      75 VNFFGKANSTGSLSV 89
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
14217-14283 2.95e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 41.71  E-value: 2.95e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 14217 GTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGR 14283
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGM 67
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
18428-18510 2.95e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 42.13  E-value: 2.95e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18428 DVITVRVGQTIRILARVKGRPEPDITWSK--------EGKVLVkDKRVDlihdlpRVELQIKEAVRADHGKYIISAKNSS 18499
Cdd:cd05894       3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRgdkaftatEGRVRV-ESYKD------LSSFVIEGAEREDEGVYTITVTNPV 75
                            90
                    ....*....|.
gi 1958765569 18500 GHAQGSAIVNV 18510
Cdd:cd05894      76 GEDHASLFVKV 86
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5251-5317 2.98e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.00  E-value: 2.98e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5251 EVAGTPPFEITWFKDNTTLRSGRkykTFIQDQlVSLQILKFVASDAGEYQCRVTNEVGSSTCSARVT 5317
Cdd:cd05725      20 EVGGDPVPTVRWRKEDGELPKGR---YEILDD-HSLKIRKVTAGDMGSYTCVAENMVGKIEASATLT 82
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2245-2311 2.99e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.13  E-value: 2.99e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  2245 ELECIISPENI-EGKWYHNDVELKSNGKYSITSRrgrQNLTVKDVTKEDQGEY-CFV---VDGKKTTCKLKM 2311
Cdd:cd20957      20 VFNCSVTGNPIhTVLWMKDGKPLGHSSRVQILSE---DVLVIPSVKREDKGMYqCFVrndGDSAQATAELKL 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
23052-23145 3.01e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 3.01e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23052 PPRISMDPKykDTVVVQaGESFKIDADIYGKPIPTTQWVKGDQELS-STARLeikTTDFATS-LSVKDAVRVDSGNYILK 23129
Cdd:cd20976       1 APSFSSVPK--DLEAVE-GQDFVAQCSARGKPVPRITWIRNAQPLQyAADRS---TCEAGVGeLHIQDVLPEDHGTYTCL 74
                            90
                    ....*....|....*.
gi 1958765569 23130 AKNVAGEKSVTVNVKV 23145
Cdd:cd20976      75 AKNAAGQVSCSAWVTV 90
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
32885-32977 3.01e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 42.54  E-value: 3.01e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32885 APRITLRMRSHRVPCGQNTRFILNVQSKPTAEVK--WYHNGVELQ-ESSKIHYTNTSGVLT---LEILDCQTEDSGTYRA 32958
Cdd:cd04970       2 ATRITLAPSNADITVGENATLQCHASHDPTLDLTftWSFNGVPIDlEKIEGHYRRRYGKDSngdLEIVNAQLKHAGRYTC 81
                            90
                    ....*....|....*....
gi 1958765569 32959 VCTNYKGEASDYATLDVTG 32977
Cdd:cd04970      82 TAQTVVDSDSASATLVVRG 100
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7011-7098 3.02e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.45  E-value: 3.02e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVA--TLKILQTDLSHSGQYSCSASNP 7088
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGriCLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|
gi 1958765569  7089 LGTASSTARL 7098
Cdd:cd05892      81 AGVVSCNARL 90
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
7864-7937 3.03e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 42.54  E-value: 3.03e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7864 HVEAAIGEPTTLQCKVDGTPEIRISWYK-----EHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAV 7937
Cdd:cd05765       9 HQTVKVGETASFHCDVTGRPQPEITWEKqvpgkENLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGLL 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4203-4286 3.04e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 42.18  E-value: 3.04e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4203 KPLVDTISEKGDTVHLTSSISNAK--EVNWYFKGDLVPPGAKFQCLKEENAY-TLVIESVKTEDEGEYVCEASNGNGKAM 4279
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPdpEVKWMKDDNPIVESRRFQIDQDEDGLcSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569  4280 TSAKLTV 4286
Cdd:cd20973      82 CSAELTV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7492-7570 3.05e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 42.34  E-value: 3.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7492 VTTGNPFTLECVVAGTPELSAKWLKDGR--ELSSGSRHHITFVRNLASLKIPSAEMNDKGLYSFEVENSVGKSSCTVSVH 7569
Cdd:cd20974      12 VLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELL 91

                    .
gi 1958765569  7570 V 7570
Cdd:cd20974      92 V 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
15624-15705 3.05e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.10  E-value: 3.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15624 GGIQIMAGKTLRIPAVVTGRPVPTKVWTIEeGEL---DKERVVIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAA 15700
Cdd:cd05744       8 GDLEVQEGRLCRFDCKVSGLPTPDLFWQLN-GKPvrpDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFN 86

                    ....*
gi 1958765569 15701 ARVEV 15705
Cdd:cd05744      87 AELVV 91
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
8808-8886 3.06e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.20  E-value: 3.06e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8808 VTVGDSASLQCQLAGTPEIGVSWYKGDTKLrpTTTCKMHFKNnvATLVFTQVDSNDSGEYICRAENSVGEVSSSTFLTV 8886
Cdd:cd05728      11 ADIGSSLRWECKASGNPRPAYRWLKNGQPL--ASENRIEVEA--GDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
7866-7945 3.06e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.20  E-value: 3.06e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7866 EAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPayKMQFKNnvASLVINKVDHSDVGEYTCKAENSVGAVASSAVLVI 7945
Cdd:cd05728      10 EADIGSSLRWECKASGNPRPAYRWLKNGQPLASEN--RIEVEA--GDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
12986-13046 3.09e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 42.54  E-value: 3.09e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12986 VSEGDTIKLVCEVS-KPGAEVTWYK---GDEEVIET-----GRFEILTDGRkriLIIQNAQLEDAGSYNC 13046
Cdd:cd05765      12 VKVGETASFHCDVTgRPQPEITWEKqvpGKENLIMRpnhvrGNVVVTNIGQ---LVIYNAQPQDAGLYTC 78
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
9305-9380 3.12e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.21  E-value: 3.12e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  9305 TTATFIAKVGGDPIPNVKWTKGKwRQLNQGGRILIHQ-KGDESKLEIRDTTKTDSGLYRCVAFNKHGEIESNVNLQV 9380
Cdd:cd05729      20 NKVRLECGAGGNPMPNITWLKDG-KEFKKEHRIGGTKvEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
5802-5881 3.12e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 42.01  E-value: 3.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5802 VVKDSDVELECEVMGT-TPfEVTWLKNNKEIRSGKKYTMSEKMSvfyLHITKCAPSDVGEYQCIIANEGGSCACTARVAL 5880
Cdd:cd05731       7 VLRGGVLLLECIAEGLpTP-DIRWIKLGGELPKGRTKFENFNKT---LKIENVSEADSGEYQCTASNTMGSARHTISVTV 82

                    .
gi 1958765569  5881 K 5881
Cdd:cd05731      83 E 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
6-97 3.12e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.06  E-value: 3.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFT--QPLQSVVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTlpgvQISFSDGRArLMIPAVTKANSGRYSLRAT 83
Cdd:cd04969       1 PDFElnPVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS----RICILPDGS-LKIKNVTKSDEGKYTCFAV 75
                            90
                    ....*....|....
gi 1958765569    84 NGSGQATSTAELLV 97
Cdd:cd04969      76 NFFGKANSTGSLSV 89
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
4962-5038 3.14e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.00  E-value: 3.14e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4962 VGGACRLDCKIAGSLPMRVSWFKDGKEIAASDRYQIafvegtasleiSRVDMNDAGNFTCRATNSVGSKDSRGALIV 5038
Cdd:pfam13895    13 EGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFT-----------LSVSAEDSGTYTCVARNGRGGKVSNPVELT 78
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7015-7099 3.16e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.00  E-value: 3.16e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7015 RQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDG-------VLLRDDEnlqmsfvdnvaTLKILQTDLSHSGQYSCSASN 7087
Cdd:cd05725       2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDgelpkgrYEILDDH-----------SLKIRKVTAGDMGSYTCVAEN 70
                            90
                    ....*....|..
gi 1958765569  7088 PLGTASSTARLT 7099
Cdd:cd05725      71 MVGKIEASATLT 82
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
7956-8039 3.18e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.20  E-value: 3.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7956 RKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNLQMSfvhhVATLQILQTDQSHVGQYNCSASNPLGTASS 8035
Cdd:cd05728       4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE----AGDLRITKLSLSDSGMYQCVAENKHGTIYA 79

                    ....
gi 1958765569  8036 SAKL 8039
Cdd:cd05728      80 SAEL 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6181-6250 3.18e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 41.81  E-value: 3.18e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6181 STVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCQVTNDVGSDSCT 6250
Cdd:cd05748       8 ESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSAT 77
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
5229-5318 3.20e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 42.39  E-value: 3.20e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5229 PYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQ--DQLVSLQILKFVASDAGEYQCRVTNE 5306
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRdlDGTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  5307 VGSSTCSARVTL 5318
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
6915-7000 3.21e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.06  E-value: 3.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6915 PYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVA--TLVFNKVGINDSGEYTCVAENS 6992
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGriCLLIQNANKKDAGWYTVSAVNE 80

                    ....*...
gi 1958765569  6993 IGTAASKT 7000
Cdd:cd05892      81 AGVVSCNA 88
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
6649-6712 3.21e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.18  E-value: 3.21e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  6649 LGTSCVLECKV-AGSSPISIAWFHEKTKIVSGAKYQTTFSDN-VCTLQLNSLDSSDMGSYTCVAAN 6712
Cdd:pfam00047    10 EGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNN 75
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8797-8886 3.23e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 42.39  E-value: 3.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTT-----------TCKMHfkNNVATLvftqvdsNDSG 8865
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSdhytiqrdldgTCSLH--TTASTL-------DDDG 71
                            90       100
                    ....*....|....*....|.
gi 1958765569  8866 EYICRAENSVGEVSSSTFLTV 8886
Cdd:cd05893      72 NYTIMAANPQGRISCTGRLMV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1678-1741 3.24e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.78  E-value: 3.24e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  1678 GPAHFECRLTpiGDPTMVVEWLHDGKPLEAANRLRLINEFGYCSLDYEAAYSRDSGVITCRATN 1741
Cdd:pfam13927    17 ETVTLTCEAT--GSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
7761-7843 3.25e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.21  E-value: 3.25e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7761 EPATFVKRLadTSVETGSPIVLEATYSGTPPIAVSWLKNEYPLSQSPNCGITTTERSSILEILESTI-EDYAQYACLIEN 7839
Cdd:cd05729       5 DTEKMEERE--HALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIpRDKGKYTCIVEN 82

                    ....
gi 1958765569  7840 EAGQ 7843
Cdd:cd05729      83 EYGS 86
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
8428-8513 3.28e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 42.25  E-value: 3.28e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8428 PESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKYKISFFNKVSGLKIISVAPGDSGVYSFEVQNPVGKDSCTV 8507
Cdd:cd05736       7 PEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDIS 86

                    ....*.
gi 1958765569  8508 SIQVSD 8513
Cdd:cd05736      87 SLFVED 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4852-4949 3.28e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 42.25  E-value: 3.28e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4852 PAKIIERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEV 4931
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*...
gi 1958765569  4932 GSSSCETTFTVLDRDIAP 4949
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPP 98
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
32320-32396 3.28e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 42.01  E-value: 3.28e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 32320 GQSVCFEIRVSGIPAPTLKWEKDGQPLSLGphieivHEGLDYY--ALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQV 32396
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIKLGGELPKG------RTKFENFnkTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
33898-33984 3.29e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.10  E-value: 3.29e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRfhienTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDS 33977
Cdd:cd20952       6 PQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERIT-----TLENGSLQIKGAEKSDTGEYTCVALNLSGEAT 80

                    ....*..
gi 1958765569 33978 ATVNINI 33984
Cdd:cd20952      81 WSAVLDV 87
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
18723-18805 3.30e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 42.41  E-value: 3.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18723 LTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATD-LTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVVTATNPAGSFVAYA 18801
Cdd:cd20951      10 HTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDpSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSA 89

                    ....
gi 1958765569 18802 TVNV 18805
Cdd:cd20951      90 SVVV 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
20508-20584 3.30e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.10  E-value: 3.30e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 20508 ENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVS--VESTAVNTtLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKV 20584
Cdd:cd05744      14 EGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmlVRENGRHS-LIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
21592-21659 3.30e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.10  E-value: 3.30e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21592 GDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVN--VENTATSTILnINECVRSDSGAYPLTAKNTVGEV 21659
Cdd:cd05744      15 GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmlVRENGRHSLI-IEPVTKRDAGIYTCIARNRAGEN 83
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
4854-4897 3.31e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 42.54  E-value: 3.31e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1958765569  4854 KIIERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASK 4897
Cdd:cd07693       2 RIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDK 45
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
32222-32293 3.31e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 41.84  E-value: 3.31e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 32222 VTITVH---PEPRVTWYKSGQKIKpgdDDKKYTFESDKGLYQLTINSVTTDDDAEYAVVArnkhGEDSCKAKLTV 32293
Cdd:cd20967      15 IRLTVEladPDAEVKWYKDGQELQ---SSSKVIFESIGAKRTLTVQQASLADAGEYQCVA----GGEKCSFELFV 82
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
21584-21659 3.31e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.21  E-value: 3.31e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 21584 QKLVIAR-AGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNV-ENTATSTILNINECVRSDSGAYPLTAKNTVGEV 21659
Cdd:cd05729      10 EEREHALpAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGtKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSI 87
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
7870-7937 3.32e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 41.71  E-value: 3.32e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  7870 GEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAV 7937
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMV 68
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
8067-8137 3.32e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.15  E-value: 3.32e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  8067 FKCHVTGTAPIKITWAKDNREIRPG---GNYKMTLveNTATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQLGV 8137
Cdd:cd05857      24 FRCPAAGNPTPTMRWLKNGKEFKQEhriGGYKVRN--QHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 95
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2228-2296 3.33e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 42.41  E-value: 3.33e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  2228 EFVKELQDIEVPESYSGELECIISPE-NIEGKWYHNDVELKSN---GKYSITSRRGRQNLTVKDVTKEDQGEY 2296
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQGKpDPEVKWYKNGVPIDPSsipGKYKIESEYGVHVLHIRRVTVEDSAVY 74
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
8532-8607 3.34e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 41.84  E-value: 3.34e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8532 GSSVVMECKVFGsPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCiatnVAGSDECSAPLTV 8607
Cdd:cd20967      12 GHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC----VAGGEKCSFELFV 82
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
12804-12872 3.35e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 42.25  E-value: 3.35e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 12804 EDQTVEEEATAVLECEVSRE-NAKVKWFKNGTEIL--KSKKYEIVADGrvRKLIIHGCTPEDIKTYTCDAKD 12872
Cdd:cd05736       8 EFQAKEPGVEASLRCHAEGIpLPRVQWLKNGMDINpkLSKQLTLIANG--SELHISNVRYEDTGAYTCIAKN 77
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
14-92 3.35e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 42.01  E-value: 3.35e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569    14 SVVVLEGSAATFEAHISGSPVPEVSWFRDGqvistSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATST 92
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLG-----GELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHT 77
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8706-8793 3.36e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 42.39  E-value: 3.36e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8706 FVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGVNVtaSQRCNITTTEK----SAILEILSSTVEDSGQYNCYIENA 8781
Cdd:cd05893       3 FEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQI--SPKSDHYTIQRdldgTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|..
gi 1958765569  8782 SGKDSCSAQILI 8793
Cdd:cd05893      81 QGRISCTGRLMV 92
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
5791-5878 3.36e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 42.39  E-value: 3.36e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5791 PIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIR-SGKKYTMSEKMS-VFYLHITKCAPSDVGEYQCIIANE 5868
Cdd:cd05893       1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDLDgTCSLHTTASTLDDDGNYTIMAANP 80
                            90
                    ....*....|
gi 1958765569  5869 GGSCACTARV 5878
Cdd:cd05893      81 QGRISCTGRL 90
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
15-90 3.37e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.20  E-value: 3.37e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569    15 VVVLEGSAATFEAHISGSPVPEVSWFRDGQVISTSTlpGVQISFSDGR-ARLMIPAVTKANSGRYSLRATNGSGQAT 90
Cdd:cd05891      11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSE--HYSVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYGGET 85
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
8158-8218 3.37e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 41.94  E-value: 3.37e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  8158 YTRYECKIGGSPE-IKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:cd20927      16 HVKYVCKIENYDQsTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVN 77
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
24835-24920 3.38e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 42.25  E-value: 3.38e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24835 VQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVIVL 24914
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*.
gi 1958765569 24915 EKPGPP 24920
Cdd:cd05762      93 DKPDPP 98
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
33712-33787 3.39e-03

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 41.93  E-value: 3.39e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 33712 GQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSrnmyTLEIRNASVSDSGKYTVKAKNFRGQCSATASLTV 33787
Cdd:cd05851      16 GQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSGA----VLKIFNIQPEDEGTYECEAENIKGKDKHQARVYV 87
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5066-5131 3.43e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 42.09  E-value: 3.43e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5066 QGSTPLTIRWFKGDKELVSGGSCYITKEASESS-LELYAVKTTDSGTYTCKVSNVAGSVECSANLFV 5131
Cdd:cd20959      28 GGDLPLNIRWTLDGQPISDDLGITVSRLGRRSSiLSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
28101-28161 3.43e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 41.84  E-value: 3.43e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 28101 GKPKPSISWLKDGLPLKESEYVRFSKTENkitLSIKNVKKENGGKYtvildNAVCRNSFPI 28161
Cdd:cd20968      25 GNPKPSVSWIKGDDLIKENNRIAVLESGS---LRIHNVQKEDAGQY-----RCVAKNSLGI 77
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5439-5504 3.45e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 3.45e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  5439 SGTKEISAKWFKDGQELTLGP--KYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKASINV 5504
Cdd:cd05750      25 SENPSPRYRWFKDGKELNRKRpkNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
28485-28550 3.47e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.06  E-value: 3.47e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 28485 GDSLRIKALVQGRPVPRVTWFKDGVEIER---RMNMEiTDVLGSTSLFVRDATRDHRGVYTVEAKNVSG 28550
Cdd:cd05892      15 GDPVRLECQISAIPPPQIFWKKNNEMLQYntdRISLY-QDNCGRICLLIQNANKKDAGWYTVSAVNEAG 82
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4480-4559 3.47e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 42.17  E-value: 3.47e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVqSAI-NKKIHLECQVDEDRKVSITWSKDGQKLPAGKDYKIyFEDkiASLEI-PLAKLKDSGTYSCTASNE 4557
Cdd:cd20958       1 PPFIRPMGNL-TAVaGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRV-FPN--GTLVIeNVQRSSDEGEYTCTARNQ 76

                    ..
gi 1958765569  4558 AG 4559
Cdd:cd20958      77 QG 78
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
32893-32959 3.48e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 41.84  E-value: 3.48e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32893 RSHRVPCGQNTRFILNVqSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDSGTYRAV 32959
Cdd:cd20967       5 PAVQVSKGHKIRLTVEL-ADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV 70
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
5237-5319 3.48e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 42.01  E-value: 3.48e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5237 SIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRkykTFIQDQLVSLQILKFVASDAGEYQCRVTNEVGSSTCSARV 5316
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGR---TKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISV 80

                    ...
gi 1958765569  5317 TLR 5319
Cdd:cd05731      81 TVE 83
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
31549-31630 3.49e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 3.49e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31549 VHALRGEVVSIKIPFSGKPDPVITW-QKGQDLIDNNGHYqvIVTRSFTSLVFPNgVERKDAGFYVVCAKNR-FGIDQKTV 31626
Cdd:cd20970      12 VTAREGENATFMCRAEGSPEPEISWtRNGNLIIEFNTRY--IVRENGTTLTIRN-IRRSDMGIYLCIASNGvPGSVEKRI 88

                    ....
gi 1958765569 31627 ELDV 31630
Cdd:cd20970      89 TLQV 92
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
16630-16725 3.49e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 42.01  E-value: 3.49e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16630 PSIELK-EFMEVEEGTDVNIVAKIKGVPFPTLTWFKAPPK-KPDSkepvvyDTHVNKQVVDDTCTLVIPQSRRSDTGLYS 16707
Cdd:cd05893       1 PFFEMKlKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQiSPKS------DHYTIQRDLDGTCSLHTTASTLDDDGNYT 74
                            90
                    ....*....|....*...
gi 1958765569 16708 ITAVNNLGTASKEMRLNV 16725
Cdd:cd05893      75 IMAANPQGRISCTGRLMV 92
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
13511-13598 3.49e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.13  E-value: 3.49e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13511 PPKIKTSDQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTKTVDTTAEQTSFRILEAKKEDKGRYKIVLQNKHGKA 13590
Cdd:cd20957       1 PLSATIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSA 80

                    ....*...
gi 1958765569 13591 EGFINLQV 13598
Cdd:cd20957      81 QATAELKL 88
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
28478-28560 3.50e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.20  E-value: 3.50e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28478 DGLVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGS-TSLFVRDATRDHRGVYTVEAKNVSGSTKAEI 28556
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYGGETVDV 88

                    ....
gi 1958765569 28557 TVKV 28560
Cdd:cd05891      89 TVSV 92
I-set pfam07679
Immunoglobulin I-set domain;
11734-11812 3.51e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 41.86  E-value: 3.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11734 VTVVKGQPLYLSCEL--NKERDVVWRKDGKivvekpgRIVPGVIGLMRA------LTINDADDTDAGTYTVTVEN-ANNL 11804
Cdd:pfam07679    10 VEVQEGESARFTCTVtgTPDPEVSWFKDGQ-------PLRSSDRFKVTYeggtytLTISNVQPDDSGKYTCVATNsAGEA 82

                    ....*...
gi 1958765569 11805 ECSSCVKV 11812
Cdd:pfam07679    83 EASAELTV 90
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
7588-7666 3.51e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 41.84  E-value: 3.51e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  7588 ATLGASVVLECRVSGsAPISVGWFLDGNEIISSPKCQPSFADNVCTLTLSSLEPSDTGAYTCvaanVAGQDESSALLTV 7666
Cdd:cd20967       9 VSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC----VAGGEKCSFELFV 82
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
11644-11719 3.51e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.06  E-value: 3.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11644 VGSSAIFECL--VSPSTAITtWMKDGSNIRESPKHRFIADGKdrkLHIIDVQLSDAGEYTC--VLRLGNKEktSTAKLIV 11719
Cdd:cd04969      16 KGGDVIIECKpkASPKPTIS-WSKGTELLTNSSRICILPDGS---LKIKNVTKSDEGKYTCfaVNFFGKAN--STGSLSV 89
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
9186-9261 3.53e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 42.23  E-value: 3.53e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  9186 QHLTPVTASEGDFLQLSCHVQG-SEPIrIQWLRAGREIKPSDRcSFSFASGTAVLELKDTAKADSGDYVCKASNVAG 9261
Cdd:cd05730       8 QSEVNATANLGQSVTLACDADGfPEPT-MTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAG 82
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
9296-9380 3.55e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 42.15  E-value: 3.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9296 PQSIRVVEktTATFIAKVGGDPIPNVKWTKgkwrQLNQGGRILI---HQKGDE-----SKLEIRDTTKTDSGLYRCVAFN 9367
Cdd:cd05765       9 HQTVKVGE--TASFHCDVTGRPQPEITWEK----QVPGKENLIMrpnHVRGNVvvtniGQLVIYNAQPQDAGLYTCTARN 82
                            90
                    ....*....|...
gi 1958765569  9368 KHGEIESNVNLQV 9380
Cdd:cd05765      83 SGGLLRANFPLSV 95
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
26696-26786 3.55e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 42.15  E-value: 3.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26696 PAFDVDSEMRKTLTVK-AGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRTSLTIENANRNDSGKYTLTIQNV 26774
Cdd:cd05856       1 PRFTQPAKMRRRVIARpVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSNR 80
                            90
                    ....*....|..
gi 1958765569 26775 LSAASMTFVVKV 26786
Cdd:cd05856      81 AGEINATYKVDV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
15193-15310 3.55e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 42.15  E-value: 3.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15193 PKVILRTSLEVKRGDEIALDATISGSPYPTITWIKDENVIVPEEIKKRvappvRRKKgeaeeeepFTLPLTerlsinnsk 15272
Cdd:cd05856       6 PAKMRRRVIARPVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGEN-----KKKK--------WTLSLK--------- 63
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1958765569 15273 qgesqlrvrdSLRP-DHGQYMIKVENDHGVAKAPCTVSV 15310
Cdd:cd05856      64 ----------NLKPeDSGKYTCHVSNRAGEINATYKVDV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7386-7477 3.56e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 42.18  E-value: 3.56e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7386 PPRFVKKLSDVSTLIGDPVELQAVVEGFQPISVVWLKDkGEVIRESENVRISFVDNIATLQLGSPEASHSGKYVCQIKND 7465
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCE-GKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                            90
                    ....*....|..
gi 1958765569  7466 AGMRECSALLTV 7477
Cdd:cd20972      80 VGSDTTSAEIFV 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7298-7373 3.58e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 42.00  E-value: 3.58e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  7298 QKPPPVGALKGSDVILQCEIS-GTPPFEVVWVKDRKQVRSSKKFKVTSKnfDTSLHIFNLEAPDIGEYHCKATNEVG 7373
Cdd:cd05724       2 VEPSDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDNERVRIVD--DGNLLIAEARKSDEGTYKCVATNMVG 76
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
19411-19500 3.59e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 41.85  E-value: 3.59e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19411 PPKIL-MPEQITIKAGKKLRVEAHVYGKPNPICKW-KKGEDDVVTSSHLAIHKAdsSSVLIIKDVTRKDSGYYSLTAENS 19488
Cdd:cd20976       1 APSFSsVPKDLEAVEGQDFVAQCSARGKPVPRITWiRNAQPLQYAADRSTCEAG--VGELHIQDVLPEDHGTYTCLAKNA 78
                            90
                    ....*....|..
gi 1958765569 19489 SGTDTQKIKVTV 19500
Cdd:cd20976      79 AGQVSCSAWVTV 90
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
15906-15997 3.60e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 42.18  E-value: 3.60e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 15906 PPTIKLRLAVRgdtiKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIEKPTDaLNITKEEVSRSeakteLSIPKAVREDKG 15985
Cdd:cd20972       1 PPQFIQKLRSQ----EVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPD-IQIHQEGDLHS-----LIIAEAFEEDTG 70
                            90
                    ....*....|..
gi 1958765569 15986 TYTITASNRLGS 15997
Cdd:cd20972      71 RYSCLATNSVGS 82
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
27399-27474 3.60e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.06  E-value: 3.60e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 27399 GTSVKLRAGISGKPEPTIEWYKDDKELQ--TNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRVQI 27474
Cdd:cd05892      15 GDPVRLECQISAIPPPQIFWKKNNEMLQynTDRISLYQDNCGRICLLIQNANKKDAGWYTVSAVNEAGVVSCNARLDV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
9581-9652 3.62e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 41.85  E-value: 3.62e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  9581 PAWERHLQDVTLKEGQTCTMTCQFS---VPNVKseWFRNGRVLKPQGRvKTEVEHKVHKLTIADVRAEDQGRYTC 9652
Cdd:cd20976       2 PSFSSVPKDLEAVEGQDFVAQCSARgkpVPRIT--WIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTC 73
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
1814-1889 3.64e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 41.46  E-value: 3.64e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  1814 EGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIhyLDIVDCKSYDTGEVKVTAENPEGVTEHKVKLEI 1889
Cdd:cd05745       1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSGT--LRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
31-100 3.64e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 42.23  E-value: 3.64e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    31 GSPVPEVSWFRDGQVISTSTlpgVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATSTAELLVTAE 100
Cdd:cd05730      29 GFPEPTMTWTKDGEPIESGE---EKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFAK 95
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
6086-6149 3.65e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.80  E-value: 3.65e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6086 LGSSIHMECKVS-GSLPINAQWFKDGKEISTSAKYRLvcHENTV---SLEVSNLELEDTANYTCKVSN 6149
Cdd:pfam00047    10 EGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKH--DNGRTtqsSLLISNVTKEDAGTYTCVVNN 75
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
32900-32975 3.66e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 3.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32900 GQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVlTLEILDCQTEDSGTYRAVCTN-YKGEASDYATLDV 32975
Cdd:cd20970      17 GENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGT-TLTIRNIRRSDMGIYLCIASNgVPGSVEKRITLQV 92
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7020-7098 3.69e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 42.16  E-value: 3.69e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7020 IEQTV--GLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMS-FV----DNVATLKILQTDLSHSGQYSCSASNPLGTA 7092
Cdd:cd20956       9 SEQTLqpGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGdYVtsdgDVVSYVNISSVRVEDGGEYTCTATNDVGSV 88

                    ....*.
gi 1958765569  7093 SSTARL 7098
Cdd:cd20956      89 SHSARI 94
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
7305-7381 3.70e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 41.82  E-value: 3.70e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  7305 ALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKkfkVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCACTV 7381
Cdd:cd05876       7 ALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDR---VKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSARHAYYV 80
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
1807-1879 3.70e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.19  E-value: 3.70e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  1807 PEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIHY--LDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd05737       8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTvyFTINGVSSEDSGKYGLVVKNKYG 82
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
21592-21659 3.71e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.06  E-value: 3.71e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 21592 GDNIKVEIPVLGRPKPTVTWKKGDQILKQ-TQRVNV--ENTATSTILnINECVRSDSGAYPLTAKNTVGEV 21659
Cdd:cd05892      15 GDPVRLECQISAIPPPQIFWKKNNEMLQYnTDRISLyqDNCGRICLL-IQNANKKDAGWYTVSAVNEAGVV 84
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
9588-9656 3.72e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.80  E-value: 3.72e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  9588 QDVTLKEGQTCTMTC--QFSVPNVKSEWFRNGRVLK-PQGRVKTEVEHKVHKLTIADVRAEDQGRYTCKHED 9656
Cdd:pfam00047     4 PTVTVLEGDSATLTCsaSTGSPGPDVTWSKEGGTLIeSLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNN 75
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
1815-1879 3.72e-03

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 41.80  E-value: 3.72e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  1815 GETARFRCRVTGYPQPKVNWYLNGQLIR---KSKRFRVRYDGihyLDIVDCKSYDTGEVKVTAENPEG 1879
Cdd:cd05867      14 GETARLDCQVEGIPTPNITWSINGAPIEgtdPDPRRHVSSGA---LILTDVQPSDTAVYQCEARNRHG 78
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
6168-6255 3.74e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 41.71  E-value: 3.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6168 FLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDV-ELVSGPKCFIGLEGStsfLNLYSVDASKTGQYTCQVTNDVGS 6246
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVpLLGKDERITTLENGS---LQIKGAEKSDTGEYTCVALNLSGE 78

                    ....*....
gi 1958765569  6247 DSCTTMLLV 6255
Cdd:cd20952      79 ATWSAVLDV 87
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
8997-9078 3.74e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.80  E-value: 3.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8997 PVDAVVGESADL--ECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENsahLTIVKVDKGDSGQYTCYAINEVGKDSCTA 9074
Cdd:cd05723       4 PSNIYAHESMDIvfECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVGNAQASA 80

                    ....
gi 1958765569  9075 QLNI 9078
Cdd:cd05723      81 QLII 84
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
4585-4663 3.75e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.20  E-value: 3.75e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4585 MLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFANSE-AILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVI 4663
Cdd:cd05891      13 IMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
8899-8980 3.75e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 41.82  E-value: 3.75e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8899 LRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNVQTSfldnIATLNIFKTDRSLAGQYSCTVTNPIGSASSSA 8978
Cdd:cd05728       6 ISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE----AGDLRITKLSLSDSGMYQCVAENKHGTIYASA 81

                    ..
gi 1958765569  8979 KL 8980
Cdd:cd05728      82 EL 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
6366-6433 3.76e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.06  E-value: 3.76e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  6366 KNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKnfhASIHILNVDSTDIGEYHCKAQNEVGS 6433
Cdd:cd04969      16 KGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPD---GSLKIKNVTKSDEGKYTCFAVNFFGK 80
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
32306-32396 3.77e-03

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 42.07  E-value: 3.77e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32306 PMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHiEIVHEGL--DYYALHIRDTLPEDTGYYRVTATN 32383
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGL-KYRIQEFkgGYHQLIIASVTDDDATVYQVRATN 80
                            90
                    ....*....|...
gi 1958765569 32384 TAGSTSCQAHLQV 32396
Cdd:cd20971      81 QGGSVSGTASLEV 93
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7294-7376 3.78e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 42.01  E-value: 3.78e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFK-VTSKNFDTSLHIFNLEAPDIGEYHCKATNEV 7372
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKmLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80

                    ....
gi 1958765569  7373 GSDT 7376
Cdd:cd20990      81 GQNS 84
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
16640-16725 3.78e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.06  E-value: 3.78e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16640 VEEGTDVNIVAKIKGVPFPTLTWFKappkkpdSKEPVVYDTHVNKQVVDDT--CTLVIPQSRRSDTGLYSITAVNNLGTA 16717
Cdd:cd05892      12 VLEGDPVRLECQISAIPPPQIFWKK-------NNEMLQYNTDRISLYQDNCgrICLLIQNANKKDAGWYTVSAVNEAGVV 84

                    ....*...
gi 1958765569 16718 SKEMRLNV 16725
Cdd:cd05892      85 SCNARLDV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
5053-5132 3.80e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 41.75  E-value: 3.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5053 VLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSG-GSCYITKEASESSLELYAVKTTDSGTYTCKVSNVAGsvECSANLFV 5131
Cdd:cd05894       7 VVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATeGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVG--EDHASLFV 84

                    .
gi 1958765569  5132 K 5132
Cdd:cd05894      85 K 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
14-97 3.80e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 41.75  E-value: 3.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569    14 SVVVLEGSAATFEAHISGSPVPEVSWFRDGQVIsTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATSTA 93
Cdd:cd05894       4 TIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAF-TATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                    ....
gi 1958765569    94 ELLV 97
Cdd:cd05894      83 FVKV 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
23466-23535 3.81e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.80  E-value: 3.81e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 23466 IRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSS--FTSLVLDNVNRYDSGKYTLTLENSSGTKS 23535
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEgdLHSLIIAEAFEEDTGRYSCLATNSVGSDT 84
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
4228-4286 3.82e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.80  E-value: 3.82e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4228 VNWYFKGDLVPPGAKFQCLKEENaytLVIESVKTEDEGEYVCEASNGNGKAMTSAKLTV 4286
Cdd:cd05723      29 VKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
30674-30736 3.82e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 42.23  E-value: 3.82e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 30674 GKPFPICKWTKEGQDV-SKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVKV 30736
Cdd:cd05730      29 GFPEPTMTWTKDGEPIeSGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
6635-6729 3.83e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 42.25  E-value: 3.83e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6635 PPSFTRRLKDIGGVLGTSCVLECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVA 6714
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*
gi 1958765569  6715 GSDECRALLTVQEPP 6729
Cdd:cd05762      81 GSRQAQVNLTVVDKP 95
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6457-6536 3.84e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 42.00  E-value: 3.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6457 VVAGEPAELQASI-EGAPPISVHWLKEKEEVVRESENVRISFVNNvatLQFAKAEPANAGKYICQVKNDGGVRE-NMASL 6534
Cdd:cd05724       9 VAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGEREsRAARL 85

                    ..
gi 1958765569  6535 TV 6536
Cdd:cd05724      86 SV 87
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
7305-7375 3.84e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 42.13  E-value: 3.84e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7305 ALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKK-----FKVTSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSD 7375
Cdd:cd05732      13 AVELEQITLTCEAEGDPIPEITWRRATRGISFEEGdldgrIVVRGHARVSSLTLKDVQLTDAGRYDCEASNRIGGD 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
31551-31630 3.86e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.06  E-value: 3.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31551 ALRGEVVSIKIPFSGKPDPVITWQKGQDLI-----------DNNGHYQVIVtrsftslvfpNGVERKDAGFYVVCAKNRF 31619
Cdd:cd05892      12 VLEGDPVRLECQISAIPPPQIFWKKNNEMLqyntdrislyqDNCGRICLLI----------QNANKKDAGWYTVSAVNEA 81
                            90
                    ....*....|.
gi 1958765569 31620 GIDQKTVELDV 31630
Cdd:cd05892      82 GVVSCNARLDV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
11629-11719 3.86e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.10  E-value: 3.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11629 FVKEIKDIVLTEaesvGSSAIFECLVS--PSTAITtWMKDGSNIRESPKHRFIADGKDR-KLHIIDVQLSDAGEYTCVLR 11705
Cdd:cd05744       3 FLQAPGDLEVQE----GRLCRFDCKVSglPTPDLF-WQLNGKPVRPDSAHKMLVRENGRhSLIIEPVTKRDAGIYTCIAR 77
                            90
                    ....*....|....
gi 1958765569 11706 LGNKEKTSTAKLIV 11719
Cdd:cd05744      78 NRAGENSFNAELVV 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
28098-28154 3.88e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 42.00  E-value: 3.88e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 28098 PYKGKPKPSISWLKDGLPLKE-SEYVRFSKTENkitLSIKNVKKENGGKYTVILDNAV 28154
Cdd:cd05724      21 PPRGHPEPTVSWRKDGQPLNLdNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMV 75
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
5149-5217 3.88e-03

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 41.76  E-value: 3.88e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5149 KGDATQLVCKVTGTPPIKITWfandRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSD 5217
Cdd:cd04968      15 KGQTVTLECFALGNPVPQIKW----RKVDGSPSSQWEITTSEPVLEIPNVQFEDEGTYECEAENSRGKD 79
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
30660-30736 3.89e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.79  E-value: 3.89e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 30660 VRQGGVIRLTIPIKGKPFPICKWTKEGQDV--SKRAMIATSETHT-ELVIKEADRNDSGTYDLVLENKCGKKTVYIKVKV 30736
Cdd:cd20973       9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIveSRRFQIDQDEDGLcSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
3198-3290 3.90e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 41.78  E-value: 3.90e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3198 PPQVlQELQPVTVQSGKPARF-CAViAGRPQPKISWYKEEQLLSTGFKCKFLHDGqeyTLLLIEAFP-EDAAVYTCEAKN 3275
Cdd:cd20958       1 PPFI-RPMGNLTAVAGQTLRLhCPV-AGYPISSITWEKDGRRLPLNHRQRVFPNG---TLVIENVQRsSDEGEYTCTARN 75
                            90
                    ....*....|....*
gi 1958765569  3276 DYGvatTSASLSVEV 3290
Cdd:cd20958      76 QQG---QSASRSVFV 87
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
8802-8886 3.91e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 3.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8802 QLEPLK---VTVGDSASLQCQLAG-TPEIGVSWYKGDTKLRPTTTCKMHFKNN--VATLVFTQVDSNDSGEYICRAENSV 8875
Cdd:cd05750       2 KLKEMKsqtVQEGSKLVLKCEATSeNPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENIL 81
                            90
                    ....*....|.
gi 1958765569  8876 GEVSSSTFLTV 8886
Cdd:cd05750      82 GKDTVTGNVTV 92
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8052-8135 3.93e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 41.75  E-value: 3.93e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8052 LKPVSVDLALGESGSFKCHVTGTaPIK-ITWAKDNREIrPGGNYKMTLVENtaTLTVLKVAKGDAGQYTCYASNVAGKDS 8130
Cdd:cd20957       6 IDPPVQTVDFGRTAVFNCSVTGN-PIHtVLWMKDGKPL-GHSSRVQILSED--VLVIPSVKREDKGMYQCFVRNDGDSAQ 81

                    ....*
gi 1958765569  8131 CSAQL 8135
Cdd:cd20957      82 ATAEL 86
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
27797-27874 3.94e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 41.78  E-value: 3.94e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 27797 AGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARysiQNTDSSSLLVIPQVTRN-DTGKYILTIENGVGQPKSSTVSVKV 27874
Cdd:cd20958      14 AGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR---QRVFPNGTLVIENVQRSsDEGEYTCTARNQQGQSASRSVFVKV 89
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
4862-4942 3.96e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 41.85  E-value: 3.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4862 IQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKyRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFT 4941
Cdd:cd20976      11 LEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVT 89

                    .
gi 1958765569  4942 V 4942
Cdd:cd20976      90 V 90
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
25236-25300 3.96e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 42.13  E-value: 3.96e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25236 TFVLEADirGKPIPDIVW--SKDGNELEETA--ARMEIKSTLQKTTLTVKDCIRTDGGQYTLKLSN-VGG 25300
Cdd:cd05732      20 TLTCEAE--GDPIPEITWrrATRGISFEEGDldGRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNrIGG 87
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
29967-30036 3.96e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 3.96e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 29967 TVIIRAGASLRLMVSVSGRPSPVITWSKKG---IDLANRAIIdnTESYSLLIVDKVNRYDAGKYTIEAENQSG 30036
Cdd:cd20970      11 TVTAREGENATFMCRAEGSPEPEISWTRNGnliIEFNTRYIV--RENGTTLTIRNIRRSDMGIYLCIASNGVP 81
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4583-4663 3.96e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 42.01  E-value: 3.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4583 YLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESN---TVRMSFaNSEAILDITDVKVDDSGTYSCEATNDAGSDSCST 4659
Cdd:cd05893      10 YKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSdhyTIQRDL-DGTCSLHTTASTLDDDGNYTIMAANPQGRISCTG 88

                    ....
gi 1958765569  4660 EVVI 4663
Cdd:cd05893      89 RLMV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
12890-12970 3.96e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.79  E-value: 3.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12890 RPLTDLQVKEKETARFECEISKE-NVKVQWFKDGAEIKKGKKYDIISKG-AVRILVINKCLLNDEAEYSC----EVRTAR 12963
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYpDPEVKWMKDDNPIVESRRFQIDQDEdGLCSLIISDVCGDDSGKYTCkavnSLGEAT 81

                    ....*..
gi 1958765569 12964 TSGMLTV 12970
Cdd:cd20973      82 CSAELTV 88
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
127-193 3.97e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.80  E-value: 3.97e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   127 VTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAypeDSGTYSVNATNSVGRATSTADLLV 193
Cdd:cd05723      21 VTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKS---DEGFYQCIAENDVGNAQASAQLII 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
18721-18805 3.97e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.10  E-value: 3.97e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18721 GVLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDAtdLTRSPRVKIdTSAESSKFSL--TKAKRSDGGKYVVTATNPAGSFV 18798
Cdd:cd05744       8 GDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKP--VRPDSAHKM-LVRENGRHSLiiEPVTKRDAGIYTCIARNRAGENS 84

                    ....*..
gi 1958765569 18799 AYATVNV 18805
Cdd:cd05744      85 FNAELVV 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
2048-2128 4.00e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 4.00e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2048 TVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYwpEDNVCELVIRDVTAEDSASIMVKAIN-IAGETSSHAFL 2126
Cdd:cd20970      13 TAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIV--RENGTTLTIRNIRRSDMGIYLCIASNgVPGSVEKRITL 90

                    ..
gi 1958765569  2127 LV 2128
Cdd:cd20970      91 QV 92
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
25229-25301 4.02e-03

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 41.67  E-value: 4.02e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 25229 IIVRAGETFVLEADIRGKPIPDIVWSKDGNELEETAARMeiKSTLQKTTLTVKDCIRTDGGQYTLKLSNVGGT 25301
Cdd:cd04978       9 LVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDM--RRTVDGRTLIFSNLQPNDTAVYQCNASNVHGY 79
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
6359-6433 4.05e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.80  E-value: 4.05e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6359 PPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNfhaSIHILNVDSTDIGEYHCKAQNEVGS 6433
Cdd:cd05723       4 PSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEH---NLQVLGLVKSDEGFYQCIAENDVGN 75
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2772-2828 4.07e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.16  E-value: 4.07e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  2772 VAFEVSVSHDTVP-VKWFHKNVEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVV 2828
Cdd:cd00096       1 VTLTCSASGNPPPtITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVA 58
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
116-194 4.07e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 41.86  E-value: 4.07e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569   116 RQGSQARLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTADLLVQ 194
Cdd:cd05736      13 EPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVE 91
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
16634-16725 4.07e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 41.68  E-value: 4.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16634 LKEFMEVEEGTDVNIVAKIKGVPFPTLTWFKAppkkpdsKEPVVYDTHVNkqVVDDTcTLVIPQSRRSDTGLYSITAVNN 16713
Cdd:cd04969       8 VKKKILAAKGGDVIIECKPKASPKPTISWSKG-------TELLTNSSRIC--ILPDG-SLKIKNVTKSDEGKYTCFAVNF 77
                            90
                    ....*....|..
gi 1958765569 16714 LGTASKEMRLNV 16725
Cdd:cd04969      78 FGKANSTGSLSV 89
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
14213-14282 4.07e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 42.07  E-value: 4.07e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 14213 TVKAGTKIELPATVTGKPEPKITWTKADTLLRPDQRITIENVPKK-STVTITDSKRSDTGTYIIEAVNVCG 14282
Cdd:cd20975      11 SVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGlCRLRILAAERGDAGFYTCKAVNEYG 81
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7200-7290 4.08e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 42.01  E-value: 4.08e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDTSKVAkQGESIQLECKISGSPEIKVVWFRNDSELH-ESWKYNMSF-VNSVALLTINEASVEDTGDYICEAHN 7277
Cdd:cd05893       1 PFFEMKLKHYKIF-EGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRdLDGTCSLHTTASTLDDDGNYTIMAAN 79
                            90
                    ....*....|...
gi 1958765569  7278 GVGHASCSTALKV 7290
Cdd:cd05893      80 PQGRISCTGRLMV 92
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
7294-7374 4.11e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.21  E-value: 4.11e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7294 PVFTQ--------KPPPVGalkgSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTS-KNFDTSLHIFNLEAPDIGEY 7364
Cdd:cd05729       1 PRFTDtekmeereHALPAA----NKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKvEEKGWSLIIERAIPRDKGKY 76
                            90
                    ....*....|
gi 1958765569  7365 HCKATNEVGS 7374
Cdd:cd05729      77 TCIVENEYGS 86
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
3037-3091 4.11e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.15  E-value: 4.11e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  3037 FECEVSE-PDITVQWMKDGQELQIVDRIKIQKEKYVH-RLLIPSARMSDAGKYTVVA 3091
Cdd:cd05857      24 FRCPAAGnPTPTMRWLKNGKEFKQEHRIGGYKVRNQHwSLIMESVVPSDKGNYTCVV 80
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
29973-30046 4.12e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.79  E-value: 4.12e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 29973 GASLRLMVSVSGRPSPVITWSKKG--IDLANRAIIDNTESY--SLLIVDKVNRyDAGKYTIEAENQSGKKSATVLVKV 30046
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDnpIVESRRFQIDQDEDGlcSLIISDVCGD-DSGKYTCKAVNSLGEATCSAELTV 88
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
13068-13137 4.14e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.80  E-value: 4.14e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 13068 SKPQNLEILEGEKAEFVCTISKES--FEVQWKRDDQTLESGDKYDIIADGKKR-VLVVKDATLQDMGTYVVMV 13137
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSASTGSpgPDVTWSKEGGTLIESLKVKHDNGRTTQsSLLISNVTKEDAGTYTCVV 73
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7971-8034 4.14e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.93  E-value: 4.14e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  7971 FECRINGSEPLQVSWYKDGQLLKDDSNLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLGTAS 8034
Cdd:cd20949      19 ILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
28479-28556 4.14e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.93  E-value: 4.14e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 28479 GLVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGsTKAEI 28556
Cdd:cd20949       8 VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS-IASDM 84
PTZ00121 PTZ00121
MAEBL; Provisional
405-734 4.15e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.15e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   405 AEAVTTGAKEVKQETDKSAAVATVVAAVDMARVREPVISAVEQTAQRTTTTAVHVQPAQKQMRKEAEKTAVTKVVVAADK 484
Cdd:PTZ00121   1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   485 AKEQELRLRTREEIITKQEQTHIAHEQIRKETEKAFVPKVvisatKAKEQETRITGEITTKQEQKRITQETITKETRKTV 564
Cdd:PTZ00121   1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA-----KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   565 VPKVIVATPKIKEQDVVSRSREAITTKRDQVQITQEKKRKETEttalstiavaTTKAKEQETVLRSREAMTTRqehiqvt 644
Cdd:PTZ00121   1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE----------AKKAEEAKKADEAKKAEEAK------- 1534
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   645 hgKVGVGKKAEAVATVVAAVDQARVREPREPRHVEESYSQQTTLEYGYKEHISATKVPEQPQRPASEPHVVPKAVKPVVI 724
Cdd:PTZ00121   1535 --KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
                           330
                    ....*....|
gi 1958765569   725 QAPSETHIKA 734
Cdd:PTZ00121   1613 KKAEEAKIKA 1622
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
31059-31132 4.20e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.15  E-value: 4.20e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRFGKELVQSRK---YKMSSdgRTHTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:cd05857      19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKVRN--QHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHL 93
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
23742-23830 4.21e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 42.01  E-value: 4.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23742 PDVRPAFSSYSVQVGQDLKIEVPISGRPKPSISWTKDGAPLK-QTTRINVIDSLDLTTLSIKETHKDDGGHYGITVANVV 23820
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRpDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|
gi 1958765569 23821 GQKTAAIEII 23830
Cdd:cd20990      81 GQNSFNLELV 90
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
28884-28957 4.21e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.82  E-value: 4.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28884 GASIRLFIAYQGRPTPTAVWSKPDSNL------SIRADihtTDSFSTLTVENCNRNDAGKYTLTVENNSGRKSITFTVKV 28957
Cdd:cd05891      16 GKTLNLTCTVFGNPDPEVIWFKNDQDIelsehySVKLE---QGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4294-4379 4.25e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 41.75  E-value: 4.25e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4294 IKRRIEP--LEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNyisSLEILRTQVVDCGEYTCKASNEYG 4371
Cdd:cd20957       2 LSATIDPpvQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDGD 78

                    ....*...
gi 1958765569  4372 SVSCTATL 4379
Cdd:cd20957      79 SAQATAEL 86
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
28086-28152 4.28e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.15  E-value: 4.28e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 28086 SVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENK-ITLSIKNVKKENGGKYTVILDN 28152
Cdd:cd05857      15 AVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQhWSLIMESVVPSDKGNYTCVVEN 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
11998-12081 4.29e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 42.02  E-value: 4.29e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 11998 LDFAVPLKDVTVPEKRQARFECVLTREAN--VIWSKGPDIIKASD---KFDIIADGKKHILVINDSQFDDEGVYTAEVEG 12072
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDpeVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|...
gi 1958765569 12073 K----KTSAQLFV 12081
Cdd:cd20951      81 IhgeaSSSASVVV 93
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6267-6349 4.32e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 41.61  E-value: 4.32e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6267 ASKIVKAGDSARLECKITGSPEIRVVWYRNEHELTASdKYQMTFIDSvavMQMNSLGTEDSGDFICEAQNPAGSTSCSTK 6346
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEASAT 80

                    ...
gi 1958765569  6347 VIV 6349
Cdd:cd05725      81 LTV 83
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
12981-13046 4.32e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 42.13  E-value: 4.32e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 12981 LANLEVSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIET-----GRFEILTDGRKRILIIQNAQLEDAGSYNC 13046
Cdd:cd05732       8 LENQTAVELEQITLTCEAEgDPIPEITWRRATRGISFEegdldGRIVVRGHARVSSLTLKDVQLTDAGRYDC 79
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7296-7374 4.33e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 41.87  E-value: 4.33e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7296 FTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQV--------RSSKKFKVTSKNfdtSLHIFNLEAPDIGEYHCK 7367
Cdd:cd05726       2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNllfpyqppQPSSRFSVSPTG---DLTITNVQRSDVGYYICQ 78

                    ....*..
gi 1958765569  7368 ATNEVGS 7374
Cdd:cd05726      79 ALNVAGS 85
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
3022-3087 4.37e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.90  E-value: 4.37e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  3022 KHIKDIKVLEKKRAMFECE-VSE-PDITVQWMKDGQELQIVDR---IKIQKEKYVHRLLIPSARMSDAGKY 3087
Cdd:cd05895       4 KEMKSQEVAAGSKLVLRCEtSSEyPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEY 74
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7855-7953 4.40e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 42.25  E-value: 4.40e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7855 PPYFIEPLEHVEAAIGEPTTLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSV 7934
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*....
gi 1958765569  7935 GAVASSAVLVIKERKLPPS 7953
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPPA 99
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
4394-4466 4.43e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143278 [Multi-domain]  Cd Length: 98  Bit Score: 41.89  E-value: 4.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4394 KSLTTFVGKAAKFLCTVSGTPVIETIWQK--DGTALS---PSPDCRI--TDADNKHSLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:cd05870       9 KNETTVENGAATLSCKAEGEPIPEITWKRasDGHTFSegdKSPDGRIevKGQHGESSLHIKDVKLSDSGRYDCEAASRIG 88
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4666-4746 4.44e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.86  E-value: 4.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4666 PPSFIKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRLFTQKTFVFLEITSFNSADIGDYECVVANEV 4745
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80

                    .
gi 1958765569  4746 G 4746
Cdd:cd05762      81 G 81
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
5610-5695 4.44e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 41.86  E-value: 4.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5610 PQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSNDVGTTSSKA 5689
Cdd:cd05736       7 PEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDEDIS 86

                    ....*.
gi 1958765569  5690 TIFVKE 5695
Cdd:cd05736      87 SLFVED 92
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
115-178 4.44e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 41.46  E-value: 4.44e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569   115 VRQGSQARLQVRVTGIPTPVvKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNA 178
Cdd:cd20967       9 VSKGHKIRLTVELADPDAEV-KWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA 71
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
5800-5871 4.46e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.81  E-value: 4.46e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5800 VEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMS-EKMSVFYLHITKCAPSDVGEYQCIIANEGGS 5871
Cdd:cd05737      11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKvEAGRTVYFTINGVSSEDSGKYGLVVKNKYGS 83
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
7491-7570 4.47e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 41.84  E-value: 4.47e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7491 TVTTGNPFTLECVVAGTPELSAKWLKDGRELSSGSRHHItFVRNLASLKIPSAEMNDKGLYSFEVENSVGKSSCTVSVHV 7570
Cdd:cd05730      14 TANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYS-FNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
5143-5216 4.47e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 41.23  E-value: 4.47e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5143 PSQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKhkmSFVEStavlrltdVAIEDSGEYMCEAQNEAGS 5216
Cdd:pfam13895     7 SPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN---FFTLS--------VSAEDSGTYTCVARNGRGG 69
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
33074-33162 4.48e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.86  E-value: 4.48e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33074 RILTKPRSITVHEGESARFSCDTDGEPVPTVTWLRGGQVVSTSARHQVTTAKYKSTFEISSVQASDEGNYSVVVENTDGK 33153
Cdd:cd05762       3 QIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGS 82

                    ....*....
gi 1958765569 33154 QEAQFTLTV 33162
Cdd:cd05762      83 RQAQVNLTV 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5909-5973 4.49e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 41.62  E-value: 4.49e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  5909 GSPPISITWLKDDQILEENDN-VHISFEDSVATLQVRSVDnghSGRYTCQAKNESGV-ERCYAFLLV 5973
Cdd:cd05724      24 GHPEPTVSWRKDGQPLNLDNErVRIVDDGNLLIAEARKSD---EGTYKCVATNMVGErESRAARLSV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
5036-5131 4.50e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 41.71  E-value: 4.50e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5036 LIVQEPPSFVtkpesrdVLPGSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITKEasESSLELYAVKTTDSGTYTCK 5115
Cdd:cd20952       1 IILQGPQNQT-------VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLE--NGSLQIKGAEKSDTGEYTCV 71
                            90
                    ....*....|....*.
gi 1958765569  5116 VSNVAGSVECSANLFV 5131
Cdd:cd20952      72 ALNLSGEATWSAVLDV 87
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
12986-13046 4.50e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 41.75  E-value: 4.50e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 12986 VSEGDTIKLVCEVS-KPGAEVTWYKGDEEVIETGRFEILTDGRkriLIIQNAQLEDAGSYNC 13046
Cdd:cd20957      13 VDFGRTAVFNCSVTgNPIHTVLWMKDGKPLGHSSRVQILSEDV---LVIPSVKREDKGMYQC 71
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
33701-33788 4.57e-03

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 41.67  E-value: 4.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33701 ISQPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPiSISSNISVSRSRNMYTLEIRNASVSDSGKYTVKAKNFRGQCS 33780
Cdd:cd04978       3 IIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVP-IEPAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHGYLL 81

                    ....*...
gi 1958765569 33781 ATASLTVL 33788
Cdd:cd04978      82 ANAFLHVL 89
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
4856-4935 4.57e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.55  E-value: 4.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4856 IERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSS 4935
Cdd:cd20949       3 TENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
13151-13227 4.57e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.40  E-value: 4.57e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 13151 KLRIVVPLKDTKVKEQQEAVFNCEVNTEG-AKAKWFRNDEAIFDSSKYIILQKDLVYTLRIRDARLDDQANFSVSLTN 13227
Cdd:pfam13927     1 KPVITVSPSSVTVREGETVTLTCEATGSPpPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
4393-4476 4.59e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.81  E-value: 4.59e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4393 PKSLTTFVGKAAKFLCTVSGTPVIETIWQKDGTALSPSPDCRI-TDADNKHSLELSNLTVQDRGVYSCKASNKFGADICQ 4471
Cdd:cd05737       8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLkVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSD 87

                    ....*
gi 1958765569  4472 AELTI 4476
Cdd:cd05737      88 VTVSV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4201-4286 4.60e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 41.64  E-value: 4.60e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4201 ILKPLVDTISEKGDtVHLTSSISN--AKEVNWYFKGDLVPP---GAKFQCLKEENAYTLVIESVKTEDEGEYVCEASNGN 4275
Cdd:cd20951       4 IIRLQSHTVWEKSD-AKLRVEVQGkpDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIH 82
                            90
                    ....*....|.
gi 1958765569  4276 GKAMTSAKLTV 4286
Cdd:cd20951      83 GEASSSASVVV 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
13337-13406 4.60e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.71  E-value: 4.60e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 13337 FVEHLEDQTVTEFDDAVFSCQLS-REKANVKWYRNGREIKEGKKYK-FEKDGSIHRLIIKDCRLEDECEYAC 13406
Cdd:cd05744       3 FLQAPGDLEVQEGRLCRFDCKVSgLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTC 74
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
1255-1329 4.60e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 41.84  E-value: 4.60e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  1255 NYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRRGERyqMDFLQDGraSLRIPVVLPEDEGIYTAFASNIKGNA 1329
Cdd:cd20968       8 NVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNR--IAVLESG--SLRIHNVQKEDAGQYRCVAKNSLGIA 78
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
28087-28172 4.61e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.86  E-value: 4.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28087 VRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNVKKENGGKYTVILDNAVCRNSFPITIITL 28166
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*.
gi 1958765569 28167 GPPSKP 28172
Cdd:cd05762      93 DKPDPP 98
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
25918-26003 4.61e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.86  E-value: 4.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25918 VKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIVL 25997
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*.
gi 1958765569 25998 DRPGPP 26003
Cdd:cd05762      93 DKPDPP 98
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
23461-23542 4.62e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.82  E-value: 4.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23461 RKVINIRAGGSLRLFVPIKGRPTPEVKW---GKVDGEIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAF 23537
Cdd:cd05729      11 EREHALPAANKVRLECGAGGNPMPNITWlkdGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHT 90

                    ....*
gi 1958765569 23538 VTVRV 23542
Cdd:cd05729      91 YDVDV 95
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
1515-1607 4.62e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.78  E-value: 4.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1515 KPAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNsDIIVPhKYPRIRIEGTKGEAA-----LKIDSTISQDSAWYT 1589
Cdd:cd20956       1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLD-GFPIP-ESPRFRVGDYVTSDGdvvsyVNISSVRVEDGGEYT 78
                            90
                    ....*....|....*...
gi 1958765569  1590 ATAINKAGRDTTRCKVNI 1607
Cdd:cd20956      79 CTATNDVGSVSHSARINV 96
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
22685-22749 4.67e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.77  E-value: 4.67e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 22685 GRPTPTVTWHKDDVPLkqTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNVIV 22749
Cdd:cd05856      30 GNPRPDITWLKDNKPL--TPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
11644-11702 4.68e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 41.72  E-value: 4.68e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 11644 VGSSAIFECLVSPSTA-ITTWMKDGSNIRE-SPKHRFIADGKDrkLHIIDVQLSDAGEYTC 11702
Cdd:cd20970      16 EGENATFMCRAEGSPEpEISWTRNGNLIIEfNTRYIVRENGTT--LTIRNIRRSDMGIYLC 74
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
6925-6989 4.71e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 41.46  E-value: 4.71e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6925 EASVGDSVSLQCQVAGtPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVGINDSGEYTCVA 6989
Cdd:cd20967       8 QVSKGHKIRLTVELAD-PDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA 71
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
6271-6353 4.71e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 42.15  E-value: 4.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6271 VKAGDSARLECKITGSP--EIRVVWYRNEHELTAS---DKYQMTF-IDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCS 6344
Cdd:cd04970      14 ITVGENATLQCHASHDPtlDLTFTWSFNGVPIDLEkieGHYRRRYgKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSDSAS 93

                    ....*....
gi 1958765569  6345 TKVIVKEPP 6353
Cdd:cd04970      94 ATLVVRGPP 102
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7018-7099 4.71e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 41.62  E-value: 4.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7018 KDIEQTVGLPVTLTCrlngSAPI-----HVCWYRDGVLLRDDeNLQMSFVDNvATLKILQTDLSHSGQYSCSASNPLGT- 7091
Cdd:cd05724       5 SDTQVAVGEMAVLEC----SPPRghpepTVSWRKDGQPLNLD-NERVRIVDD-GNLLIAEARKSDEGTYKCVATNMVGEr 78

                    ....*...
gi 1958765569  7092 ASSTARLT 7099
Cdd:cd05724      79 ESRAARLS 86
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
9581-9653 4.71e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 41.69  E-value: 4.71e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  9581 PAWERHLQDVTLKEGQTCTMTCQFS-VPNVKSEWFRNGRVLKP-QGRVKTEVEHKVHKLTIADVRAEDQGRYTCK 9653
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQgEPKPVVSWLRNRQPVRPdQRRFAEEAEGGLCRLRILAAERGDAGFYTCK 75
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
5522-5600 4.72e-03

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 41.76  E-value: 4.72e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5522 SIKGSFIDLECIVAGSHPISIQWFKDDQEISAsdkyKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTV 5600
Cdd:cd04968      13 ALKGQTVTLECFALGNPVPQIKWRKVDGSPSS----QWEITTSEPVLEIPNVQFEDEGTYECEAENSRGKDTVQGRIIV 87
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8235-8318 4.74e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 41.68  E-value: 4.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8235 PVFRKKPFPVETLKGADVHLECELQGTPPFQVSWYKDKRELR-SGKKYKIMSENL-LTSIHILNVDTADIGEYQCKATND 8312
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNCgRICLLIQNANKKDAGWYTVSAVNE 80

                    ....*.
gi 1958765569  8313 VGSDTC 8318
Cdd:cd05892      81 AGVVSC 86
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
29970-30046 4.80e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.55  E-value: 4.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29970 IRAGASLRLMVSVSGRPSPVITWSKKGIDLANRAIID---NTESYSLLIvDKVNRYDAGKYTIEAENQSGKKSATVLVKV 30046
Cdd:cd20949      11 VKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMskyRILADGLLI-NKVTQDDTGEYTCRAYQVNSIASDMQERTV 89
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
4760-4849 4.80e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 41.68  E-value: 4.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4760 PTF----VKKVDdfTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSSGVAVLTISDVQIGlggKYTCLAE 4835
Cdd:cd04969       1 PDFelnpVKKKI--LAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGSLKIKNVTKSDEG---KYTCFAV 75
                            90
                    ....*....|....
gi 1958765569  4836 NEAGSQTSVGELIV 4849
Cdd:cd04969      76 NFFGKANSTGSLSV 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
13070-13148 4.81e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 41.62  E-value: 4.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13070 PQNLEILEGEKAEFVCTISKESFE--VQWKRDDQTL-ESGDKYDIIADGKkrvLVVKDATLQDMGTYVV----MVGAAR- 13141
Cdd:cd05724       4 PSDTQVAVGEMAVLECSPPRGHPEptVSWRKDGQPLnLDNERVRIVDDGN---LLIAEARKSDEGTYKCvatnMVGEREs 80

                    ....*..
gi 1958765569 13142 AAAHLTV 13148
Cdd:cd05724      81 RAARLSV 87
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
7859-7935 4.81e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 41.74  E-value: 4.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7859 IEPLEHVEAAIGEPTTLQCKVDGTPEIRISW---YKEHTKLRSAPAYKMQFKNN--VASLVINKVDHSDVGEYTCKAENS 7933
Cdd:cd05732       5 ITYLENQTAVELEQITLTCEAEGDPIPEITWrraTRGISFEEGDLDGRIVVRGHarVSSLTLKDVQLTDAGRYDCEASNR 84

                    ..
gi 1958765569  7934 VG 7935
Cdd:cd05732      85 IG 86
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
6839-6901 4.83e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.41  E-value: 4.83e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  6839 IILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKtciLEILTSTKGDAGHYSCEIENEAG 6901
Cdd:cd05723      15 IVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVG 74
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8613-8700 4.86e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 41.71  E-value: 4.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8613 FVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFK-GSSELVPGARC----NVSLQDSVAELelfdvdtSQSGDYTCIVSN 8687
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKdGVPLLGKDERIttleNGSLQIKGAEK-------SDTGEYTCVALN 74
                            90
                    ....*....|...
gi 1958765569  8688 EAGRASCTTQLFV 8700
Cdd:cd20952      75 LSGEATWSAVLDV 87
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
33703-33787 4.87e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.41  E-value: 4.87e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33703 QPRSQNINEGQNVLFSCEISGEPSPEIEWFKNNLPISISSNISVSRSRNmytLEIRNASVSDSGKYTVKAKNFRGQCSAT 33782
Cdd:cd05723       3 KPSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHN---LQVLGLVKSDEGFYQCIAENDVGNAQAS 79

                    ....*
gi 1958765569 33783 ASLTV 33787
Cdd:cd05723      80 AQLII 84
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
6929-6994 4.88e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.82  E-value: 4.88e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  6929 GDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYF-TNNVATLVFNKVGINDSGEYTCVAENSIG 6994
Cdd:cd05891      16 GKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLeQGKYASLTIKGVTSEDSGKYSINVKNKYG 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
25629-25694 4.89e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.40  E-value: 4.89e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 25629 VTLRASATLRLFVTIKGRPEPEVKWEKAEGILTERAQI--EVTSSYTMLVIDNVTRFDSGRYNLTLEN 25694
Cdd:pfam13927    11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRsrSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
1264-1327 4.89e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.82  E-value: 4.89e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  1264 VTFHCKMSGYPLPKIAWYKDGKRIRRGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05729      22 VRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVENEYG 85
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
9182-9271 4.90e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 41.69  E-value: 4.90e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9182 PVFDQHLTPVTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRcsfSFAS----GTAVLELKDTAKADSGDYVCKAS 9257
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQR---RFAEeaegGLCRLRILAAERGDAGFYTCKAV 77
                            90
                    ....*....|....
gi 1958765569  9258 NVAGSDTSKCKVTI 9271
Cdd:cd20975      78 NEYGARQCEARLEV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
21591-21658 4.92e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 41.64  E-value: 4.92e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 21591 AGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQ---RVNVENTATSTILNINECVRSDSGAYPLTAKNTVGE 21658
Cdd:cd20951      14 EKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGE 84
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
7866-7945 4.96e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.90  E-value: 4.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7866 EAAIGEPTTLQCK-VDGTPEIRISWYK---EHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSA 7941
Cdd:cd05895      10 EVAAGSKLVLRCEtSSEYPSLRFKWFKngkEINRKNKPENIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSASA 89

                    ....
gi 1958765569  7942 VLVI 7945
Cdd:cd05895      90 NVTI 93
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6449-6536 4.96e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.41  E-value: 4.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6449 ISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVresENVRISFVNN---VATLQFAKAEPANAGKYICQVKNDG 6525
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIV---ESRRFQIDQDedgLCSLIISDVCGDDSGKYTCKAVNSL 77
                            90
                    ....*....|.
gi 1958765569  6526 GVRENMASLTV 6536
Cdd:cd20973      78 GEATCSAELTV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2844-2912 4.99e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.40  E-value: 4.99e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2844 ITKTMRNIEVPETKAASFECEVSHFNVPSM-WLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYT 2912
Cdd:pfam13927     4 ITVSPSSVTVREGETVTLTCEATGSPPPTItWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYT 73
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
17048-17115 5.07e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.71  E-value: 5.07e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 17048 VHAGGVIRIIAYVSGKPPPTVTWNMNERALPQEATI-----ETTaiSSSMVIKNCQRSHQGVYSLLAKNEGGE 17115
Cdd:cd05744      12 VQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHkmlvrENG--RHSLIIEPVTKRDAGIYTCIARNRAGE 82
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
9289-9380 5.10e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 41.89  E-value: 5.10e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9289 KLFFVSEPQSIRVVEKTTATfiAKVGGDPIPNVKWTKGKwRQLNQ-----GGRILIHQKGDESKLEIRDTTKTDSGLYRC 9363
Cdd:cd05869       4 KITYVENQTAMELEEQITLT--CEASGDPIPSITWRTST-RNISSeektlDGHIVVRSHARVSSLTLKYIQYTDAGEYLC 80
                            90
                    ....*....|....*..
gi 1958765569  9364 VAFNKHGEIESNVNLQV 9380
Cdd:cd05869      81 TASNTIGQDSQSMYLEV 97
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
25627-25705 5.11e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 41.72  E-value: 5.11e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25627 KVVTLRASATLRLFVTikGRPEPEVKWEKAEGILTERAQ-IEVTSSYTMLVIDNVTRFDSGRYNLTLENNSG---SKTAF 25702
Cdd:cd20970      12 VTAREGENATFMCRAE--GSPEPEISWTRNGNLIIEFNTrYIVRENGTTLTIRNIRRSDMGIYLCIASNGVPgsvEKRIT 89

                    ...
gi 1958765569 25703 VNV 25705
Cdd:cd20970      90 LQV 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8424-8511 5.11e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 41.33  E-value: 5.11e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8424 IVEKPESIKVTTGDTCTLECMVSGTPELSTKWFKDGKELTGDSKyKISFFNKVSgLKIISVAPGDSGVYSFEVQNPVGKD 8503
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDE-RITTLENGS-LQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569  8504 SCTVSIQV 8511
Cdd:cd20952      80 TWSAVLDV 87
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
32201-32293 5.12e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 41.62  E-value: 5.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32201 PEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDDKKYTFESdkGLYQLTINSVTTDDDAEYAVVARN 32280
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVREN--GVHSLIIEPVTSRDAGIYTCIATN 78
                            90
                    ....*....|...
gi 1958765569 32281 KHGEDSCKAKLTV 32293
Cdd:cd20990      79 RAGQNSFNLELVV 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8426-8501 5.15e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 41.62  E-value: 5.15e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8426 EKPESIKVTTGDTCTLECMVS-GTPELSTKWFKDGKELTGDSK-YKIsffnkVSG--LKIISVAPGDSGVYSFEVQNPVG 8501
Cdd:cd05724       2 VEPSDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDNErVRI-----VDDgnLLIAEARKSDEGTYKCVATNMVG 76
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
8718-8788 5.15e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 41.36  E-value: 5.15e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  8718 GKPLILEGTFSGTPPISVTWKKNGVNVTASQ-RCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKDSCS 8788
Cdd:cd05894      10 GNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS 81
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8532-8609 5.16e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 41.87  E-value: 5.16e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8532 GSSVVMECKVFGSPPISVLWLHDG--NAISSGRKYQTT---LTDNTCALTVNMLEDADAGDYTCIATNVAGSDECSAPLT 8606
Cdd:cd05726      14 GRTVTFQCETKGNPQPAIFWQKEGsqNLLFPYQPPQPSsrfSVSPTGDLTITNVQRSDVGYYICQALNVAGSILAKAQLE 93

                    ...
gi 1958765569  8607 VRE 8609
Cdd:cd05726      94 VTD 96
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
20525-20591 5.19e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.86  E-value: 5.19e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 20525 SVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKVVGKPGIP 20591
Cdd:cd05762      32 TCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVDKPDPP 98
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
32897-32962 5.21e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 41.36  E-value: 5.21e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 32897 VPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSgvlTLEILDCQTEDSGTYRAVCTN 32962
Cdd:cd20957      13 VDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRN 75
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
25138-25495 5.23e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 46.09  E-value: 5.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25138 PTYDGGsKITGYIVEKKDLPDgrwmkASFT--NVVETEFTVTGLVEDQRY-EFRVIARNAADNFS---EPSESSGAItAR 25211
Cdd:COG4733     276 PYWDGG-KLGVVADRPRDPPV-----ATFTpaNVVDGSFTYSYSSRKERPnAALVSFSDPDNGYQqaeEPVEDPDLI-AR 348
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25212 D-----EIDAPN-------------ASLDPKYR----------DVIIVRAGETfVLEAD--IRGKPIPDIVWSKDGN--- 25258
Cdd:COG4733     349 YgvnqtELTAPGctsrgqaqregrwALLTNRYRtrtvtfsvglDGLVATPGDV-IAVADdvLAGRRIGGRVSSVDGRvvt 427
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25259 -----ELEETAARMEI---KSTLQKTTltvkdcIRTDGGQyTLKLSNVGGTKTIPITVKVLDRPGPPEGPLKVTGVTAEK 25330
Cdd:COG4733     428 ldrpvTMEAGDRYLRVrlpDGTSVART------VQSVAGR-TLTVSTAYSETPEAGAVWAFGPDELETQLFRVVSIEENE 500
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25331 C------YLAWNP---PLQDGGA---------------SISHYIIEK---RETSRLSWTQVST----EVQ---------- 25369
Cdd:COG4733     501 DgtytitAVQHAPekyAAIDAGAfddvppqwppvnvttSESLSVVAQgtaVTTLTVSWDAPAGavayEVEwrrddgnwvs 580
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25370 -----ALNYKVTKLLPGNeYIFRVMAVNKYGVGEPLESEPVIACNpyKLPGPPSTP---EASAITkDSMVLTWTRPVDDG 25441
Cdd:COG4733     581 vprtsGTSFEVPGIYAGD-YEVRVRAINALGVSSAWAASSETTVT--GKTAPPPAPtglTATGGL-GGITLSWSFPVDAD 656
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 25442 GAEIEGYILEKRDKEGirwTKCNKKTLTDLRFRVTGLTEGHSYEFRVAAENAAG 25495
Cdd:COG4733     657 TLRTEIRYSTTGDWAS---ATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
20057-20203 5.23e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 46.09  E-value: 5.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20057 RTLKATGLQEGTEYEFRVTAINKAgPGKpsDASKAVYAQDPLYPPGPPA-------FPKVYDTT-RSSVSLSWGKPAFDg 20128
Cdd:COG4733     489 QLFRVVSIEENEDGTYTITAVQHA-PEK--YAAIDAGAFDDVPPQWPPVnvttsesLSVVAQGTaVTTLTVSWDAPAGA- 564
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 20129 gspiIGYLVEVkRADSDHWVrcNLPEKLQkTRFEVTGLMENTeYQFRVYAVNKIGY-SDPSDVPDKHCPKDILIPP 20203
Cdd:COG4733     565 ----VAYEVEW-RRDDGNWV--SVPRTSG-TSFEVPGIYAGD-YEVRVRAINALGVsSAWAASSETTVTGKTAPPP 631
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
7766-7852 5.26e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.52  E-value: 5.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7766 VKRLADTSVETGSPIVLEA-TYSGTPPIAVSWLKNEYPLSQS---PNCGITTTERSSILEILESTIEDYAQYACLIENEA 7841
Cdd:cd05895       3 LKEMKSQEVAAGSKLVLRCeTSSEYPSLRFKWFKNGKEINRKnkpENIKIQKKKKKSELRINKASLADSGEYMCKVSSKL 82
                            90
                    ....*....|.
gi 1958765569  7842 GQDICEALVSV 7852
Cdd:cd05895      83 GNDSASANVTI 93
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
6446-6536 5.27e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 41.68  E-value: 5.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESENVRISFVN-NVATLQFAKAEPANAGKYICQVKND 6524
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNcGRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  6525 GGVRENMASLTV 6536
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
7308-7373 5.30e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.77  E-value: 5.30e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  7308 GSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSKNFDTSLHifNLEAPDIGEYHCKATNEVG 7373
Cdd:cd05856      19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSLK--NLKPEDSGKYTCHVSNRAG 82
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
15628-15705 5.30e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 41.23  E-value: 5.30e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 15628 IMAGKTLRIPAVVTGRPVPTKVWTIEEGELDKERVVIENVGTkseLIIKNALRKDHGRYVITATNSCGSKFAAARVEV 15705
Cdd:cd05725       9 VLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
8530-8607 5.31e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 41.44  E-value: 5.31e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8530 LSGSSVVMECKVFGSPPISVLWLHDGNAISSGRkyqTTLTDNTCALTVNMLEDADAGDYTCIATNVAGSDECSAPLTV 8607
Cdd:cd05876       8 LRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDR---VKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
24834-24913 5.38e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.43  E-value: 5.38e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24834 SVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVE-ETATSTILHIKESSKDDFGKYSVTATNNAGTATENLSVI 24912
Cdd:cd05891      12 TIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKlEQGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVS 91

                    .
gi 1958765569 24913 V 24913
Cdd:cd05891      92 V 92
Titin_Z pfam09042
Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like ...
599-639 5.41e-03

Titin Z; The titin Z domain, that recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. This interaction is essential for sarcomere assembly.


Pssm-ID: 462662  Cd Length: 43  Bit Score: 39.87  E-value: 5.41e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1958765569   599 QEKKRKETETTALSTIAVATTKAKEQETVLRSREAMTTRQE 639
Cdd:pfam09042     1 QEKVREEDEKTAVSTVVVAVDKAKVLEPVSKSEEEIAAEQE 41
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
14907-14988 5.43e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.71  E-value: 5.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 14907 DIVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHA-DAGVYTITLENKLGSATASIN 14985
Cdd:cd05744       9 DLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKrDAGIYTCIARNRAGENSFNAE 88

                    ...
gi 1958765569 14986 VKV 14988
Cdd:cd05744      89 LVV 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5696-5791 5.45e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.86  E-value: 5.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5696 PPQFIKKPSPVLVlRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRRYGISFVDGLATFQISNARVENSGTYVCEARND 5775
Cdd:cd05762       1 PPQIIQFPEDMKV-RAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENK 79
                            90
                    ....*....|....*.
gi 1958765569  5776 AGTASCSIELKVKEPP 5791
Cdd:cd05762      80 LGSRQAQVNLTVVDKP 95
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
32890-32975 5.47e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 41.33  E-value: 5.47e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 32890 LRMRSHRVPCGQNTRFILNVQ--SKPTAEVKWYHNGVELQESSKIHYTNTSGvlTLEILDCQTEDSGTYRAVCTNYKGEA 32967
Cdd:cd20952       2 ILQGPQNQTVAVGGTVVLNCQatGEPVPTISWLKDGVPLLGKDERITTLENG--SLQIKGAEKSDTGEYTCVALNLSGEA 79

                    ....*...
gi 1958765569 32968 SDYATLDV 32975
Cdd:cd20952      80 TWSAVLDV 87
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
9085-9175 5.51e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 41.69  E-value: 5.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9085 PSFTKKLSETiEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALL-LQVKKASMADAGLYTCKATND 9163
Cdd:cd20975       1 PTFKVSLMDQ-SVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCrLRILAAERGDAGFYTCKAVNE 79
                            90
                    ....*....|..
gi 1958765569  9164 AGSALCTSSIVI 9175
Cdd:cd20975      80 YGARQCEARLEV 91
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
8810-8881 5.51e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.38  E-value: 5.51e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  8810 VGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMhfKNNVATLVFTQVDSNDSGEYICRAENSVGEVSSS 8881
Cdd:cd05856      18 VGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGEN--KKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINAT 87
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
18027-18112 5.53e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.42  E-value: 5.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18027 KLIEGL----VVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSV-LTIKNCLRKDTGEYQLTVSNAA 18101
Cdd:cd05737       2 RVLGGLpdvvTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVyFTINGVSSEDSGKYGLVVKNKY 81
                            90
                    ....*....|.
gi 1958765569 18102 GTKTVAVHLTV 18112
Cdd:cd05737      82 GSETSDVTVSV 92
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
7113-7186 5.54e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 41.46  E-value: 5.54e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  7113 PVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNtphLRILKVGKGDSGQYTCQATNDVG 7186
Cdd:cd20968       6 PTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLESGS---LRIHNVQKEDAGQYRCVAKNSLG 76
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
8436-8511 5.57e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.38  E-value: 5.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8436 GDTCTLECMVSGTPELSTKWFKDGKELT----GDSKyKISFFNKVSGLKiisvaPGDSGVYSFEVQNPVGKDSCTVSIQV 8511
Cdd:cd05856      19 GSSVRLKCVASGNPRPDITWLKDNKPLTppeiGENK-KKKWTLSLKNLK-----PEDSGKYTCHVSNRAGEINATYKVDV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
27392-27474 5.58e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.42  E-value: 5.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27392 EVVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVE-NSTDLASILIKDANRLNSGSYELKLRNAMGSASATI 27470
Cdd:cd05737       9 DVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKvEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDV 88

                    ....
gi 1958765569 27471 RVQI 27474
Cdd:cd05737      89 TVSV 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
4678-4747 5.63e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 41.33  E-value: 5.63e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4678 IVRGANALLQCEVAGTGPFEVSWFKDKKQIRSsKKYRLFTQKTFVfLEITSFNSADIGDYECVVANEVGK 4747
Cdd:cd20952      11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLG-KDERITTLENGS-LQIKGAEKSDTGEYTCVALNLSGE 78
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
25-97 5.65e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.41  E-value: 5.65e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569    25 FEAHISGSPVPEVSWFRDGQVISTSTLpgVQISfsdGRARLMIPAVTKANSGRYSLRATNGSGQATSTAELLV 97
Cdd:cd05723      17 FECEVTGKPTPTVKWVKNGDVVIPSDY--FKIV---KEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
24149-24221 5.65e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.33  E-value: 5.65e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 24149 VNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCE-IKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSF 24221
Cdd:cd05744      12 VQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSF 85
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
19130-19197 5.66e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 41.77  E-value: 5.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 19130 VRAGCPIRLFAIVRGRPAPKVTWRKV--GIDNVVRK-----GQVdLVDTMAFLVIPNSTRDDSGKYSLTLVNPAG 19197
Cdd:cd05765      12 VKVGETASFHCDVTGRPQPEITWEKQvpGKENLIMRpnhvrGNV-VVTNIGQLVIYNAQPQDAGLYTCTARNSGG 85
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
14213-14286 5.68e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 41.23  E-value: 5.68e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 14213 TVKAGTKIELPATVTGKPEPKITWTKADTLLrPDQRITIenVPKKStVTITDSKRSDTGTYIIEAVNVCGRATA 14286
Cdd:cd05725       8 VVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL-PKGRYEI--LDDHS-LKIRKVTAGDMGSYTCVAENMVGKIEA 77
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
23067-23145 5.70e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 41.64  E-value: 5.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 23067 VQAGESFKIDADIYGKPIPTTQWVKGDQELSSTA---RLEIKTTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTVNV 23143
Cdd:cd20951      12 VWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASV 91

                    ..
gi 1958765569 23144 KV 23145
Cdd:cd20951      92 VV 93
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
31057-31125 5.73e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 41.50  E-value: 5.73e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 31057 KLGEAAQLSCQIVGRPLPDIKWyRFGKELVQSRKYKMS------SDGRTHTLTVMTEEQEDEGVYTCVATNEVGE 31125
Cdd:cd05869      15 ELEEQITLTCEASGDPIPSITW-RTSTRNISSEEKTLDghivvrSHARVSSLTLKYIQYTDAGEYLCTASNTIGQ 88
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
32320-32386 5.74e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 40.94  E-value: 5.74e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 32320 GQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGlDYYALHIRDTLPEDTGYYRVTATNTAG 32386
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEG-GYGTLTIRDVKESDQGAYTCEAINTRG 66
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
25918-25996 5.75e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.41  E-value: 5.75e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 25918 VKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVSSSKIVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIV 25996
Cdd:cd20972      13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
30265-30340 5.76e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.43  E-value: 5.76e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 30265 GRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHT-KVAKLTIRETTIRDTGEYMLELKNVTGttSETIKVVI 30340
Cdd:cd05891      16 GKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYSINVKNKYG--GETVDVTV 90
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
17739-17809 5.78e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.39  E-value: 5.78e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 17739 EQHIKVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQID----VTPVG---SKLEIRNAAHEDGGIYSLTVENPAGS 17809
Cdd:cd20956      10 EQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRvgdyVTSDGdvvSYVNISSVRVEDGGEYTCTATNDVGS 87
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
3318-3391 5.80e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 41.62  E-value: 5.80e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  3318 EGRPARFQCQVSGT-DLKVSWYCRDKKIKPSRFFRMTQ--FEDTYQLEIAEAFPEDEGTYAFVANNAVGQVSSTATL 3391
Cdd:cd05893      14 EGMPVTFTCRVAGNpKPKIYWFKDGKQISPKSDHYTIQrdLDGTCSLHTTASTLDDDGNYTIMAANPQGRISCTGRL 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
13065-13148 5.81e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 41.64  E-value: 5.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13065 EFISKPQNLEILEGEKAEFVCTIS-KESFEVQWKRDDQTLES---GDKYDIIADGKKRVLVVKDATLQDMGTYVVMV--- 13137
Cdd:cd20951       2 EFIIRLQSHTVWEKSDAKLRVEVQgKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAkni 81
                            90
                    ....*....|..
gi 1958765569 13138 -GAARAAAHLTV 13148
Cdd:cd20951      82 hGEASSSASVVV 93
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
24543-24624 5.83e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.44  E-value: 5.83e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24543 RKGIVVRAGGSARIHIPFKGRPTPEITWSKEEGEFTDKVQIEKGINFTQ---LSIDNCDRNDAGKYILKLENSSGSKSAF 24619
Cdd:cd05729      11 EREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKgwsLIIERAIPRDKGKYTCIVENEYGSINHT 90

                    ....*
gi 1958765569 24620 VTVKV 24624
Cdd:cd05729      91 YDVDV 95
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
7011-7098 5.84e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 41.69  E-value: 5.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7011 PSFARQLKDIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDEN-LQMSFVDNVATLKILQTDLSHSGQYSCSASNPL 7089
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRrFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80

                    ....*....
gi 1958765569  7090 GTASSTARL 7098
Cdd:cd20975      81 GARQCEARL 89
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
5144-5225 5.85e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.52  E-value: 5.85e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5144 SQLLKKGDATQLVCKVTGT-PPIKITWFANDRELRESSKH---KMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHC 5219
Cdd:cd05895       8 SQEVAAGSKLVLRCETSSEyPSLRFKWFKNGKEINRKNKPeniKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSA 87

                    ....*.
gi 1958765569  5220 TSIVIV 5225
Cdd:cd05895      88 SANVTI 93
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
32215-32293 5.85e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 41.36  E-value: 5.85e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 32215 GENVRFGVTITVHPEPRVTWYKSGQKIKPGDDdkKYTFESDKGLYQLTINSVTTDDDAEYAVVARNKHGEDSCKAKLTV 32293
Cdd:cd05894      10 GNKLRLDVPISGEPAPTVTWSRGDKAFTATEG--RVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
29570-29649 5.86e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.41  E-value: 5.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29570 TIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMVKV 29649
Cdd:cd20972      12 EVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
28479-28558 5.89e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.41  E-value: 5.89e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28479 GLVIKSGDSLRIKALV-QGRPVPRVTWFKDG-VEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEI 28556
Cdd:pfam00047     5 TVTVLEGDSATLTCSAsTGSPGPDVTWSKEGgTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84

                    ..
gi 1958765569 28557 TV 28558
Cdd:pfam00047    85 SL 86
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
24545-24624 5.89e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.55  E-value: 5.89e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24545 GIVVRAGGSARIHIPFKGRPTPEITWSKEEGEFTDKVQIEK--GINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTV 24622
Cdd:cd20949       8 VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSkyRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQER 87

                    ..
gi 1958765569 24623 KV 24624
Cdd:cd20949      88 TV 89
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
31551-31630 5.90e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 41.74  E-value: 5.90e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 31551 ALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNN-----GHYQVIVTRSFTSLVFPNgVERKDAGFYVVCAKNRFGIDQKT 31625
Cdd:cd05732      13 AVELEQITLTCEAEGDPIPEITWRRATRGISFEegdldGRIVVRGHARVSSLTLKD-VQLTDAGRYDCEASNRIGGDQQS 91

                    ....*
gi 1958765569 31626 VELDV 31630
Cdd:cd05732      92 MYLEV 96
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7670-7759 5.93e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.33  E-value: 5.93e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7670 PSFEQTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSRELESGEACTISL-EDFVTELELLEVEPLQSGDYSCLVTNDA 7748
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVrENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                            90
                    ....*....|.
gi 1958765569  7749 GSASCTTHLFV 7759
Cdd:cd05744      81 GENSFNAELVV 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
21300-21382 5.95e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.86  E-value: 5.95e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21300 VRAGLSIRIFVPIKGRPAPEVTWTK--DNINLKHRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVNVRVL 21377
Cdd:cd05762      13 VRAGESVELFCKVTGTQPITCTWMKfrKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVV 92

                    ....*
gi 1958765569 21378 DTPGP 21382
Cdd:cd05762      93 DKPDP 97
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8729-8786 5.95e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.41  E-value: 5.95e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  8729 GTPPISVTWKKNGVNVTASQRCNITTTEKSAI-LEILSSTVEDSGQYNCYIENASGKDS 8786
Cdd:pfam00047    23 GSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSsLLISNVTKEDAGTYTCVVNNPGGSAT 81
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
6269-6340 5.95e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 41.38  E-value: 5.95e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  6269 KIVKAGDSARLECKITGSPEIRVVWYRNEHE-----LTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGS 6340
Cdd:cd05765      10 QTVKVGETASFHCDVTGRPQPEITWEKQVPGkenliMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGL 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
6369-6432 6.03e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 41.34  E-value: 6.03e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6369 EVSLECELSGTPPFEVVWYKDKRQLRS-SKKYKIASKNfhASIHILNVDSTDIGEYHCKAQNEVG 6432
Cdd:cd20970      19 NATFMCRAEGSPEPEISWTRNGNLIIEfNTRYIVRENG--TTLTIRNIRRSDMGIYLCIASNGVP 81
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
8522-8607 6.07e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 41.34  E-value: 6.07e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8522 RKLKETNGLSGSSVVMECK-VFGSPPISVLWLHDGNAISSGRKYQTTLTDN--TCALTVNMLEDADAGDYTCIATNVAGS 8598
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENILGK 83

                    ....*....
gi 1958765569  8599 DECSAPLTV 8607
Cdd:cd05750      84 DTVTGNVTV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
16629-16718 6.10e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.41  E-value: 6.10e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 16629 PPS-IELKEFMEVEEGTDVNIVAKIKGVPFPTLTWF---KAPPKKPDSKEPVVYDTHvnkqvvddtcTLVIPQSRRSDTG 16704
Cdd:cd20972       1 PPQfIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFcegKELQNSPDIQIHQEGDLH----------SLIIAEAFEEDTG 70
                            90
                    ....*....|....
gi 1958765569 16705 LYSITAVNNLGTAS 16718
Cdd:cd20972      71 RYSCLATNSVGSDT 84
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
14913-14988 6.13e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.44  E-value: 6.13e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 14913 GEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRL---TMKNDHISAHLEvpKSVHADAGVYTITLENKLGSATASINVKV 14988
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIggtKVEEKGWSLIIE--RAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4256-4286 6.13e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.39  E-value: 6.13e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1958765569  4256 IESVKTEDEGEYVCEASNGNGKAMTSAKLTV 4286
Cdd:cd20956      66 ISSVRVEDGGEYTCTATNDVGSVSHSARINV 96
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
6446-6536 6.14e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 41.30  E-value: 6.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6446 PKFISKLNSLTVVAGEPAELQASIEGAPPISVHWLKEKEEVVRESENVRISFVNNVATLQFAKAEPANAGKYICQVKNDG 6525
Cdd:cd20975       1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                            90
                    ....*....|.
gi 1958765569  6526 GVRENMASLTV 6536
Cdd:cd20975      81 GARQCEARLEV 91
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
5149-5217 6.14e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 41.36  E-value: 6.14e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  5149 KGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVE-----STAVLRLTDVAIEDSGEYMCEAQNEAGSD 5217
Cdd:cd05732      15 ELEQITLTCEAEGDPIPEITWRRATRGISFEEGDLDGRIVvrghaRVSSLTLKDVQLTDAGRYDCEASNRIGGD 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
5884-5973 6.23e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 41.29  E-value: 6.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5884 PSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEEN-DNVHISFEDS-VATLQVRSVDNGHSGRYTCQAKNE 5961
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNtDRISLYQDNCgRICLLIQNANKKDAGWYTVSAVNE 80
                            90
                    ....*....|..
gi 1958765569  5962 SGVERCYAFLLV 5973
Cdd:cd05892      81 AGVVSCNARLDV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
8532-8597 6.26e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.38  E-value: 6.26e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  8532 GSSVVMECKVFGSPPISVLWLHDGNAISS-----GRKYQTTltdntcaLTVNMLEDADAGDYTCIATNVAG 8597
Cdd:cd05856      19 GSSVRLKCVASGNPRPDITWLKDNKPLTPpeigeNKKKKWT-------LSLKNLKPEDSGKYTCHVSNRAG 82
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
17048-17114 6.31e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 41.38  E-value: 6.31e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 17048 VHAGGVIRIIAYVSGKPPPTVTWnmnERALPQE-----------ATIETTAIsSSMVIKNCQRSHQGVYSLLAKNEGG 17114
Cdd:cd05765      12 VKVGETASFHCDVTGRPQPEITW---EKQVPGKenlimrpnhvrGNVVVTNI-GQLVIYNAQPQDAGLYTCTARNSGG 85
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
14908-14981 6.31e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 6.31e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 14908 IVVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSAT 14981
Cdd:cd20949       9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
5150-5215 6.34e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 40.94  E-value: 6.34e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  5150 GDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTAVLRLTDVAIEDSGEYMCEAQNEAG 5215
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRG 66
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
33418-33505 6.34e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.42  E-value: 6.34e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33418 IVTGLRDT-TVSSDSVAKFVIKVTGEPQPTVTWTKDGKAIAQSSKYKLSNDK-EEFILEILKTETSDGGLYSCTVANSAG 33495
Cdd:cd05737       3 VLGGLPDVvTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYG 82
                            90
                    ....*....|
gi 1958765569 33496 SVSSSCKLTI 33505
Cdd:cd05737      83 SETSDVTVSV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
17338-17413 6.35e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.43  E-value: 6.35e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 17338 DKLTVRVGEAFALTGRYSGKPKPKVDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRS-DSGRYCVVVENSTGSRK 17413
Cdd:cd05891       9 DVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYASLTIKGVTSeDSGKYSINVKNKYGGET 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5604-5693 6.35e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.33  E-value: 6.35e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5604 PYFVEKPQSQDVNPSTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDT---STILELFSAKaaDSGTYICQLSN 5680
Cdd:cd05744       1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgrhSLIIEPVTKR--DAGIYTCIARN 78
                            90
                    ....*....|...
gi 1958765569  5681 DVGTTSSKATIFV 5693
Cdd:cd05744      79 RAGENSFNAELVV 91
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
6550-6619 6.37e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 41.38  E-value: 6.37e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  6550 TVTVGETCSLECKVAGTPELSVEWYK--DGK---LLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVG 6619
Cdd:cd05765      11 TVKVGETASFHCDVTGRPQPEITWEKqvPGKenlIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGG 85
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
4311-4371 6.38e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 41.50  E-value: 6.38e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4311 FTCEIQGAPNVRFQWFKAGREIYESDKC-----SIRSSNYISSLEILRTQVVDCGEYTCKASNEYG 4371
Cdd:cd05869      22 LTCEASGDPIPSITWRTSTRNISSEEKTldghiVVRSHARVSSLTLKYIQYTDAGEYLCTASNTIG 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4499-4569 6.40e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.41  E-value: 6.40e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  4499 LECQVDEDRKVSITWSKDGQKLPAGKDYKI-YFEDKIASLEIPLAKLKDSGTYSCTASNEAGSSSSSATVAV 4569
Cdd:cd20973      17 FDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
17745-17818 6.41e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.33  E-value: 6.41e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 17745 GDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQID--VTPVGS-KLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLV 17818
Cdd:cd05744      15 GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmlVRENGRhSLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7118-7196 6.44e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.39  E-value: 6.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7118 VIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTitcVGN--------TPHLRILKVGKGDSGQYTCQATNDVGKDM 7189
Cdd:cd20956      13 LQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFR---VGDyvtsdgdvVSYVNISSVRVEDGGEYTCTATNDVGSVS 89

                    ....*..
gi 1958765569  7190 CSAQLSV 7196
Cdd:cd20956      90 HSARINV 96
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
29966-30046 6.45e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 41.23  E-value: 6.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29966 KTVIIRAGASLRLMVSVSGRPSPVITWSKKGIDLA-NRAII--DNTesyslLIVDKVNRYDAGKYTIEAENQSGKKSATV 30042
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPkGRYEIldDHS-----LKIRKVTAGDMGSYTCVAENMVGKIEASA 79

                    ....
gi 1958765569 30043 LVKV 30046
Cdd:cd05725      80 TLTV 83
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
3464-3550 6.45e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 41.23  E-value: 6.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3464 IKEISDVEISIEDVAKLSVTVVGCPKPKIQWFFNGMLLtPSADYKFVFDgnnHSLIILFTRFQDEGEYTCMASNEYGRAV 3543
Cdd:cd05725       1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL-PKGRYEILDD---HSLKIRKVTAGDMGSYTCVAENMVGKIE 76

                    ....*..
gi 1958765569  3544 CSAHLKV 3550
Cdd:cd05725      77 ASATLTV 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
33704-33785 6.56e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.03  E-value: 6.56e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33704 PRSQNINEGQNVLFSCEIS-GEPSPEIEWFKNNlPISISSNISVSRSRNMY--TLEIRNASVSDSGKYTVKAKNFRGQCS 33780
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSAStGSPGPDVTWSKEG-GTLIESLKVKHDNGRTTqsSLLISNVTKEDAGTYTCVVNNPGGSAT 81

                    ....*
gi 1958765569 33781 ATASL 33785
Cdd:pfam00047    82 LSTSL 86
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
18427-18510 6.64e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.38  E-value: 6.64e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18427 RDVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDliHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd05856      11 RRVIARPVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGE--NKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATY 88

                    ....
gi 1958765569 18507 IVNV 18510
Cdd:cd05856      89 KVDV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
19129-19207 6.65e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.02  E-value: 6.65e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 19129 VVRAGCPIRLFAIVRGRPAPKVTWRKVGiDNVVRKGQVDLV---DTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNV 19205
Cdd:cd20973       8 EVVEGSAARFDCKVEGYPDPEVKWMKDD-NPIVESRRFQIDqdeDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                    ..
gi 1958765569 19206 KV 19207
Cdd:cd20973      87 TV 88
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
914-989 6.69e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.44  E-value: 6.69e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569   914 GESVTLECHISGYPSPKVTWYREDYQIESSIDFQIT-FQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAV 989
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTkVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8153-8218 6.69e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 6.69e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  8153 VKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHNLSVEDSGDYTCEARN 8218
Cdd:cd20949      11 VKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQ 76
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
33904-33974 6.69e-03

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 41.42  E-value: 6.69e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 33904 AEGKVLTVACAFTGEPTPEITWSCGGRRIQSQEQQGRFHIENtddlTTLIIMDVQKQDGGLYTLSLGNEFG 33974
Cdd:cd05867      12 GPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSS----GALILTDVQPSDTAVYQCEARNRHG 78
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
4588-4658 6.70e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 41.36  E-value: 6.70e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  4588 GESARLHCKLKGSPVIQVTWFKNNKELSESNT-------VRMSFANSEaiLDITDVKVDDSGTYSCEATNDAGSDSCS 4658
Cdd:cd05732      16 LEQITLTCEAEGDPIPEITWRRATRGISFEEGdldgrivVRGHARVSS--LTLKDVQLTDAGRYDCEASNRIGGDQQS 91
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
33906-33979 6.83e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 41.29  E-value: 6.83e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 33906 GKVLtVACAFTGEPTPEITWSCGGRRIQsqeQQGRFHIenTDDlTTLIIMDVQKQDGGLYTLSLGNEFGSDSAT 33979
Cdd:cd04969      18 GDVI-IECKPKASPKPTISWSKGTELLT---NSSRICI--LPD-GSLKIKNVTKSDEGKYTCFAVNFFGKANST 84
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
12274-12348 6.86e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 41.25  E-value: 6.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 12274 VFVGETARFEIELS-EPDVHGQWKLKGEPLTAS---PDCEIIEDGKKHVLVLYNCQLDMTGEVSFQAAN----AKSAANL 12345
Cdd:cd20951      12 VWEKSDAKLRVEVQgKPDPEVKWYKNGVPIDPSsipGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNihgeASSSASV 91

                    ...
gi 1958765569 12346 KVK 12348
Cdd:cd20951      92 VVE 94
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
33898-33982 6.88e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.03  E-value: 6.88e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33898 PSDISIAEGKVLTVAC-AFTGEPTPEITWSCGGRRIQSQEQQgrFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSD 33976
Cdd:pfam00047     3 PPTVTVLEGDSATLTCsASTGSPGPDVTWSKEGGTLIESLKV--KHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                    ....*.
gi 1958765569 33977 SATVNI 33982
Cdd:pfam00047    81 TLSTSL 86
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
8052-8137 6.90e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 41.34  E-value: 6.90e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8052 LKPV-SVDLALGESGSFKCHVTGTAP-IKITWAKDNREIRPGG--NYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAG 8127
Cdd:cd05750       3 LKEMkSQTVQEGSKLVLKCEATSENPsPRYRWFKDGKELNRKRpkNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILG 82
                            90
                    ....*....|
gi 1958765569  8128 KDSCSAQLGV 8137
Cdd:cd05750      83 KDTVTGNVTV 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
3210-3288 6.90e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 41.38  E-value: 6.90e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  3210 VQSGKPARFCAVIAGRPQPKISWYKEEQLLST-----GFKCKFlhdgQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTSA 3284
Cdd:cd05857      16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQehrigGYKVRN----QHWSLIMESVVPSDKGNYTCVVENEYGSINHTY 91

                    ....
gi 1958765569  3285 SLSV 3288
Cdd:cd05857      92 HLDV 95
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
20229-20295 6.91e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 40.84  E-value: 6.91e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20229 VKGRPPPKITWSKPNVNL---RERIgLDIKStdfdtfLRCENVNKYDAGKYILTLENSCGKKEYTIVVKV 20295
Cdd:cd05725      21 VGGDPVPTVRWRKEDGELpkgRYEI-LDDHS------LKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
7200-7280 6.92e-03

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 40.99  E-value: 6.92e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7200 PKFIKKLDTSKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNmsfvNSVALLTINEASVEDTGDYICEAHNGV 7279
Cdd:cd04968       1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPSSQWEIT----TSEPVLEIPNVQFEDEGTYECEAENSR 76

                    .
gi 1958765569  7280 G 7280
Cdd:cd04968      77 G 77
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
22660-22749 6.93e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 41.24  E-value: 6.93e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22660 PAFKLLFNTFTVLAGEDLKIDVPFIGRPTPTVTWHKDDVPLKQTTRVNAESTENN-SLLTIKEACREDVGHYTVKLTNSA 22738
Cdd:cd20990       1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGvHSLIIEPVTSRDAGIYTCIATNRA 80
                            90
                    ....*....|.
gi 1958765569 22739 GEATETLNVIV 22749
Cdd:cd20990      81 GQNSFNLELVV 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
108-193 6.96e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 41.34  E-value: 6.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   108 QRLQSMTVRQGSQARLQVRVTGI-PTPVVKFYRDGAEIQSSLDFQIS-QEGDLYS-LLIAEAYPEDSGTYSVNATNSVGR 184
Cdd:cd05750       4 KEMKSQTVQEGSKLVLKCEATSEnPSPRYRWFKDGKELNRKRPKNIKiRNKKKNSeLQINKAKLEDSGEYTCVVENILGK 83

                    ....*....
gi 1958765569   185 ATSTADLLV 193
Cdd:cd05750      84 DTVTGNVTV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
7010-7098 6.99e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 41.46  E-value: 6.99e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7010 PPSF-ARQLK-DIEQTVGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENlQMSFVDNVATLKILQTDLSHSGQYSCSASN 7087
Cdd:cd05730       1 PPTIrARQSEvNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAEN 79
                            90
                    ....*....|.
gi 1958765569  7088 PLGTASSTARL 7098
Cdd:cd05730      80 KAGEQEAEIHL 90
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
9191-9271 7.00e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.43  E-value: 7.00e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9191 VTASEGDFLQLSCHVQGSEPIRIQWLRAGREIKPSDRCSFSFASGT-AVLELKDTAKADSGDYVCKASNVAGSDTSKCKV 9269
Cdd:cd05891      11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYGGETVDVTV 90

                    ..
gi 1958765569  9270 TI 9271
Cdd:cd05891      91 SV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
3465-3537 7.02e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.03  E-value: 7.02e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  3465 KEISDVEISIEDVAKLSVTVV-GCPKPKIQWFFNGMLLTPSADYKFVFDGN-NHSLIILFTRFQDEGEYTCMASN 3537
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTtQSSLLISNVTKEDAGTYTCVVNN 75
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
5995-6056 7.03e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 41.48  E-value: 7.03e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  5995 TLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFG 6056
Cdd:cd05736      19 SLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6743-6818 7.03e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 41.04  E-value: 7.03e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6743 GKNITFTSVIRGTPPFKVGWFRGARELVKGDRCNIyfeDTVAELELFNIDVSQ---SGEYTCVVSNNAGQASCTTRLFV 6818
Cdd:cd05748       7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQI---ETTASSTSLVIKNAKrsdSGKYTLTLKNSAGEKSATINVKV 82
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
20214-20295 7.04e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 40.86  E-value: 7.04e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 20214 TLILRaGVTMRLYVPVKGRPPPKITWSKPNVNL-RERIGLDikstDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIV 20292
Cdd:cd05731       5 TMVLR-GGVLLLECIAEGLPTPDIRWIKLGGELpKGRTKFE----NFNKTLKIENVSEADSGEYQCTASNTMGSARHTIS 79

                    ...
gi 1958765569 20293 VKV 20295
Cdd:cd05731      80 VTV 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
27789-27868 7.06e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.41  E-value: 7.06e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27789 LRTSVIAKaGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDARYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSS 27868
Cdd:cd20972       8 LRSQEVAE-GSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTS 86
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
7586-7666 7.10e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 41.50  E-value: 7.10e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7586 TTATLGASVVLECRVSGSAPISVGW------------FLDGNEIISSPKcqpsfadNVCTLTLSSLEPSDTGAYTCVAAN 7653
Cdd:cd05869      12 TAMELEEQITLTCEASGDPIPSITWrtstrnisseekTLDGHIVVRSHA-------RVSSLTLKYIQYTDAGEYLCTASN 84
                            90
                    ....*....|...
gi 1958765569  7654 VAGQDESSALLTV 7666
Cdd:cd05869      85 TIGQDSQSMYLEV 97
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
17031-17124 7.12e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 41.22  E-value: 7.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 17031 IVSPDLQLDASVRDRIVVHAGgviriiayVSGKPPPTVTWNMNERALpQEATIETTAISSSMVIKNCQRSHQGVYSLLAK 17110
Cdd:cd20978       4 IQKPEKNVVVKGGQDVTLPCQ--------VTGVPQPKITWLHNGKPL-QGPMERATVEDGTLTIINVQPEDTGYYGCVAT 74
                            90
                    ....*....|....
gi 1958765569 17111 NEGGERKKTIIVDV 17124
Cdd:cd20978      75 NEIGDIYTETLLHV 88
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
2048-2128 7.16e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 7.16e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  2048 TVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRiYWYWPEDNVCELVIRDVTAEDSASIMVKAINIAGETSSHAFLL 2127
Cdd:cd20949      10 TVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVA-DMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQERT 88

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gi 1958765569  2128 V 2128
Cdd:cd20949      89 V 89
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
28101-28154 7.16e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.39  E-value: 7.16e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 28101 GKPKPSISWLKDGLPLKESEYVRFSK--TENKITLS---IKNVKKENGGKYTVILDNAV 28154
Cdd:cd20956      27 GNPLPQITWTLDGFPIPESPRFRVGDyvTSDGDVVSyvnISSVRVEDGGEYTCTATNDV 85
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
24145-24227 7.20e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.42  E-value: 7.20e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 24145 DTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFK-ALLIVKDAIRIDGGQYILRASNVAGSKSFPV 24223
Cdd:cd05737       9 DVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRtVYFTINGVSSEDSGKYGLVVKNKYGSETSDV 88

                    ....
gi 1958765569 24224 NVKV 24227
Cdd:cd05737      89 TVSV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6821-6907 7.20e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.03  E-value: 7.20e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6821 PATFVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVVITPSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEA 6900
Cdd:cd20972       1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                    ....*..
gi 1958765569  6901 GRDSCDA 6907
Cdd:cd20972      81 GSDTTSA 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
12883-12957 7.20e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.03  E-value: 7.20e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12883 PPhvEFLRPLTDLQVKEKETARFECEISKENV-KVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSC 12957
Cdd:cd20972       1 PP--QFIQKLRSQEVAEGSKVRLECRVTGNPTpVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSC 74
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
33892-33975 7.23e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 41.38  E-value: 7.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 33892 PKIEALPSDISIAEGKVLTVACAFTGEPTPEITW---SCGGRRIQSQEQQGRFHIENTdDLTTLIIMDVQKQDGGLYTLS 33968
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWekqVPGKENLIMRPNHVRGNVVVT-NIGQLVIYNAQPQDAGLYTCT 79

                    ....*..
gi 1958765569 33969 LGNEFGS 33975
Cdd:cd05765      80 ARNSGGL 86
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
33438-33505 7.25e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.38  E-value: 7.25e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 33438 KVTGEPQPTVTWTKDGKAIAQSSKYKlsNDKEEFILEILKTETSDGGLYSCTVANSAGSVSSSCKLTI 33505
Cdd:cd05856      27 VASGNPRPDITWLKDNKPLTPPEIGE--NKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
12177-12245 7.30e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 7.30e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569 12177 FTVKLHDKTGVEKDEIILKCEVSKDVP--VKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYTC 12245
Cdd:cd20949       2 FTENAYVTTVKEGQSATILCEVKGEPQpnVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTC 72
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
23469-23540 7.34e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.02  E-value: 7.34e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 23469 GGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSS---FTSLVLDNVNRYDSGKYTLTLENSSG--TKSAFVTV 23540
Cdd:cd20973      12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDedgLCSLIISDVCGDDSGKYTCKAVNSLGeaTCSAELTV 88
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4667-4753 7.34e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 41.25  E-value: 7.34e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4667 PSFIKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSK---KYRLFTQKTFVFLEITSFNSADIGDYECVVAN 4743
Cdd:cd20951       1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                            90
                    ....*....|
gi 1958765569  4744 EVGKCGCVAT 4753
Cdd:cd20951      81 IHGEASSSAS 90
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
31549-31620 7.35e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.05  E-value: 7.35e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 31549 VHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRS-FTSLVFpNGVERKDAGFYVVCAKNRFG 31620
Cdd:cd05891      11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGkYASLTI-KGVTSEDSGKYSINVKNKYG 82
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
9086-9167 7.37e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 7.37e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  9086 SFTKKLSeTIEETEGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALLLQVKKASMADAGLYTCKATNDAG 9165
Cdd:cd20949       1 TFTENAY-VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS 79

                    ..
gi 1958765569  9166 SA 9167
Cdd:cd20949      80 IA 81
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
5794-5878 7.38e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 41.34  E-value: 7.38e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5794 IRELEPVEVVKDSDVELECEVMGTTP-FEVTWLKNNKEIRSGK----KYTMSEKMSvfYLHITKCAPSDVGEYQCIIANE 5868
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLKCEATSENPsPRYRWFKDGKELNRKRpkniKIRNKKKNS--ELQINKAKLEDSGEYTCVVENI 80
                            90
                    ....*....|
gi 1958765569  5869 GGSCACTARV 5878
Cdd:cd05750      81 LGKDTVTGNV 90
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
8811-8887 7.40e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 40.86  E-value: 7.40e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8811 GDSASLQCQLAGTPEIGVSWYKgdtKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSVGEVSSSTFLTVQ 8887
Cdd:cd05731      10 GGVLLLECIAEGLPTPDIRWIK---LGGELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTVE 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
27011-27072 7.40e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 40.39  E-value: 7.40e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569 27011 PISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGKYEITAANSSGTTKT 27072
Cdd:cd00096       6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
26310-26384 7.45e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 7.45e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 26310 VIVVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRT 26384
Cdd:cd20949       8 VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
6759-6818 7.50e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 41.17  E-value: 7.50e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6759 KVGWFRGARELVKGDRCNIYFEDTVAELELFNIDVSQSGEYTCVVSNNAGQASCTTRLFV 6818
Cdd:cd20927      31 QVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 90
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
28484-28560 7.52e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.44  E-value: 7.52e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 28484 SGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGST-SLFVRDATRDHRGVYTVEAKNVSGSTKAEITVKV 28560
Cdd:cd05729      18 AANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
5246-5318 7.52e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 40.69  E-value: 7.52e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5246 VMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFIQDqlvSLQILKFVASDAGEYQCRVTNEVGSSTCSARVTL 5318
Cdd:cd05745       5 VDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSG---TLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
30260-30334 7.52e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 7.52e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 30260 IHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYMLELKNVTGTTSE 30334
Cdd:cd20949       9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASD 83
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
21584-21667 7.55e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 40.84  E-value: 7.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 21584 QKLVIARAGDNIKVEIPVLGRPKPTVTW-KKGDQILKQTQRVNVENtatsTILNINECVRSDSGAYPLTAKNTVGEVGDV 21662
Cdd:cd20978       8 EKNVVVKGGQDVTLPCQVTGVPQPKITWlHNGKPLQGPMERATVED----GTLTIINVQPEDTGYYGCVATNEIGDIYTE 83

                    ....*
gi 1958765569 21663 ITIQV 21667
Cdd:cd20978      84 TLLHV 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
9099-9175 7.56e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.02  E-value: 7.56e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  9099 EGNSFKLEGRVAGSQPITIAWYKNNVEIHPTSNCEITFKNNALL-LQVKKASMADAGLYTCKATNDAGSALCTSSIVI 9175
Cdd:cd20973      11 EGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCsLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
6353-6436 7.57e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 41.29  E-value: 7.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6353 PVFSSFPPVVETLKNTEVSLECELSGTPPFEVVWYKDKRQLR-SSKKYKIASKNF-HASIHILNVDSTDIGEYHCKAQNE 6430
Cdd:cd05892       1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNCgRICLLIQNANKKDAGWYTVSAVNE 80

                    ....*.
gi 1958765569  6431 VGSDTC 6436
Cdd:cd05892      81 AGVVSC 86
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
19833-19897 7.69e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 40.85  E-value: 7.69e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 19833 GKPMPTVSWKKDSTPIK-QTEGVKMAMKRNLCTLElfsVNRKDSGDYTITAENSSGSK-SATIKLKV 19897
Cdd:cd05724      24 GHPEPTVSWRKDGQPLNlDNERVRIVDDGNLLIAE---ARKSDEGTYKCVATNMVGEReSRAARLSV 87
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
14926-14988 7.69e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 40.84  E-value: 7.69e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 14926 PVPTVSWHKDGKEVKASdRLTMKNDHisaHLEVPKSVHADAGVYTITLENKLGSATASINVKV 14988
Cdd:cd05725      25 PVPTVRWRKEDGELPKG-RYEILDDH---SLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7024-7095 7.76e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 40.65  E-value: 7.76e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  7024 VGLPVTLTCRLNGSAPIHVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASST 7095
Cdd:cd05748       6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSAT 77
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
1429-1515 7.77e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 40.95  E-value: 7.77e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1429 LEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYThKVVIKEDGTqSLIIVPALPSDSGEWTVVAQNRAGKStisvtltve 1508
Cdd:cd20970      15 REGENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGT-TLTIRNIRRSDMGIYLCIASNGVPGS--------- 83

                    ....*..
gi 1958765569  1509 aVEHQIK 1515
Cdd:cd20970      84 -VEKRIT 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3114-3193 7.80e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.95  E-value: 7.80e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569   3114 KEVQVIEKQRAVVEFEVNED-DVDAHWYKDGIEINFQvEERHQYVVERRIHRMFISEARHSDAGEYTFVA----GRNRSS 3188
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSpPPEVTWYKQGGKLLAE-SGRFSVSRSGSTSTLTISNVTPEDSGTYTCAAtnssGSASSG 80

                     ....*
gi 1958765569   3189 VTLYV 3193
Cdd:smart00410    81 TTLTV 85
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
29967-30046 7.84e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 40.86  E-value: 7.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29967 TVIIRAGASLRLMVSVSGRPSPVITWSKKGIDL-ANRAIIDNTEsySLLIVDKVNRYDAGKYTIEAENQSGKKSATVLVK 30045
Cdd:cd05731       4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELpKGRTKFENFN--KTLKIENVSEADSGEYQCTASNTMGSARHTISVT 81

                    .
gi 1958765569 30046 V 30046
Cdd:cd05731      82 V 82
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
4862-4942 7.92e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 40.98  E-value: 7.92e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4862 IQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASK-KYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTF 4940
Cdd:cd05894       5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                    ..
gi 1958765569  4941 TV 4942
Cdd:cd05894      85 KV 86
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
24849-24916 7.94e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 41.07  E-value: 7.94e-03
                            10        20        30        40        50        60
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gi 1958765569 24849 GRPRPKISWVKDGEPLRQ-TTRVNVEETATStiLHIKESSKDDFGKYSVTATNNAGTATENLSVIVLEK 24916
Cdd:cd05730      29 GFPEPTMTWTKDGEPIESgEEKYSFNEDGSE--MTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFAK 95
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
4408-4466 7.99e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 40.91  E-value: 7.99e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  4408 CTVSGTPVIETIWQKDGTALSPSPDCRITDadnKHSLELSNLTVQDRGVYSCKASNKFG 4466
Cdd:cd04969      24 CKPKASPKPTISWSKGTELLTNSSRICILP---DGSLKIKNVTKSDEGKYTCFAVNFFG 79
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9495-9566 8.02e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 41.25  E-value: 8.02e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  9495 IKDIENQTVLKDNDAIFEIDIKiNYPEIKLSWYKGTEKLEPSN---KYEITINGDRHTLRVRNCQLKDQGNYRLV 9566
Cdd:cd20951       4 IIRLQSHTVWEKSDAKLRVEVQ-GKPDPEVKWYKNGVPIDPSSipgKYKIESEYGVHVLHIRRVTVEDSAVYSAV 77
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
6-87 8.11e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143278 [Multi-domain]  Cd Length: 98  Bit Score: 41.12  E-value: 8.11e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569     6 PTFTQpLQSVVVLEGSAATFEAHISGSPVPEVSWFR--DGQVIST--STLPG-VQISFSDGRARLMIPAVTKANSGRYSL 80
Cdd:cd05870       3 PHIIQ-LKNETTVENGAATLSCKAEGEPIPEITWKRasDGHTFSEgdKSPDGrIEVKGQHGESSLHIKDVKLSDSGRYDC 81

                    ....*..
gi 1958765569    81 RATNGSG 87
Cdd:cd05870      82 EAASRIG 88
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8610-8690 8.12e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.48  E-value: 8.12e-03
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gi 1958765569  8610 PPSFVQKPDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSLQDSVAELELFDVDTSQSGDYTCIVSNEA 8689
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80

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gi 1958765569  8690 G 8690
Cdd:cd05762      81 G 81
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
1261-1327 8.15e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.00  E-value: 8.15e-03
                            10        20        30        40        50        60        70
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gi 1958765569  1261 GMGVTFHCKMSGYPLPKIAWYKDGKRIRRGEryqmdfLQDGRA---SLRIPVVLPEDEGIYTAFASNIKG 1327
Cdd:cd05856      19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPE------IGENKKkkwTLSLKNLKPEDSGKYTCHVSNRAG 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8532-8608 8.15e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 40.65  E-value: 8.15e-03
                            10        20        30        40        50        60        70
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gi 1958765569  8532 GSSVVMECKVFGSPPISVLWLHDGNAISSGRKYQTTLTDNTCALTVNMLEDADAGDYTCIATNVAGSDecSAPLTVR 8608
Cdd:cd05748       7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEK--SATINVK 81
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
31458-31531 8.18e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 41.07  E-value: 8.18e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569 31458 TLVCKVTGHPKPIVKWYRQGKEIIADGLKYRVQEFKGgyhQLIIASVTDDDATVYQVRATNQGGSVSGTASLEV 31531
Cdd:cd05730      22 TLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDGS---EMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
8721-8793 8.19e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 40.64  E-value: 8.19e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  8721 LILEGTFSGTPPISVTWKKNGVNVTASQRCNITtteKSAILEILSSTVEDSGQYNCYIENASGKDSCSAQILI 8793
Cdd:cd05723      15 IVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIV---KEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
31055-31127 8.21e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 41.00  E-value: 8.21e-03
                            10        20        30        40        50        60        70
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gi 1958765569 31055 TTKLGEAAQLSCQIVGRPLPDIKWYRF--GKELVQSRKYKMSSD---GRTHTLTVMTEEQEDEGVYTCVATNEVGEVE 31127
Cdd:cd05765      11 TVKVGETASFHCDVTGRPQPEITWEKQvpGKENLIMRPNHVRGNvvvTNIGQLVIYNAQPQDAGLYTCTARNSGGLLR 88
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
5136-5216 8.21e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.05  E-value: 8.21e-03
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gi 1958765569  5136 TFTEKL-EPSQLLKKGDATQLVCKVTGTPPIKITWFANDRELRESSKHKMSFVESTA-VLRLTDVAIEDSGEYMCEAQNE 5213
Cdd:cd05729       4 TDTEKMeEREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENE 83

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gi 1958765569  5214 AGS 5216
Cdd:cd05729      84 YGS 86
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
3020-3102 8.26e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 40.91  E-value: 8.26e-03
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gi 1958765569  3020 FRKHIKDIKVLEKKRAMFECEVS-EPDITVQWMKDGQELQI-VDRIKIQKEKY-VHRLLIPSARMSDAGKYTV----VAG 3092
Cdd:cd05892       3 FIQKPQNKKVLEGDPVRLECQISaIPPPQIFWKKNNEMLQYnTDRISLYQDNCgRICLLIQNANKKDAGWYTVsavnEAG 82
                            90
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gi 1958765569  3093 GNMSTANLFV 3102
Cdd:cd05892      83 VVSCNARLDV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
18031-18112 8.29e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 8.29e-03
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gi 1958765569 18031 GLVVKAGTTVRFPAIIRGVPVPTAKWATDGTEITTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHL 18110
Cdd:cd20949       8 VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQER 87

                    ..
gi 1958765569 18111 TV 18112
Cdd:cd20949      88 TV 89
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7952-8039 8.33e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 40.84  E-value: 8.33e-03
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gi 1958765569  7952 PSFARK-LKDVHETLGFPVAFECRINGSEPLQVSWYKDGQLLKDDSNlqmSFVHHVATLQILQTDQSHVGQYNCSASNPL 8030
Cdd:cd20978       1 PKFIQKpEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPME---RATVEDGTLTIINVQPEDTGYYGCVATNEI 77

                    ....*....
gi 1958765569  8031 GTASSSAKL 8039
Cdd:cd20978      78 GDIYTETLL 86
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
6081-6152 8.39e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 40.99  E-value: 8.39e-03
                            10        20        30        40        50        60        70        80
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gi 1958765569  6081 KMDKVL-----GSSIHMECKVSGSLPINAQWFKDGKEISTSAK---YRLVCHENTVSLEvsNLELEDTANYTCKVSNVAG 6152
Cdd:cd05857       8 KMEKKLhavpaANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKVRNQHWSLIME--SVVPSDKGNYTCVVENEYG 85
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
31154-31231 8.39e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.00  E-value: 8.39e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31154 VGSTLRLHVMYIGRPVPAMTWYHGQKLLQNSEsiTIENTEHYTHLVMKNVQRKtHAGKYKVQLSNVFGTVDAILDVEI 31231
Cdd:cd05856      18 VGSSVRLKCVASGNPRPDITWLKDNKPLTPPE--IGENKKKKWTLSLKNLKPE-DSGKYTCHVSNRAGEINATYKVDV 92
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
8797-8880 8.39e-03

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 41.30  E-value: 8.39e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8797 PYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTklrPTTTCKMHFKNN----VATLVFTQVD-SNDSGEYICRA 8871
Cdd:cd20971       2 PHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGK---EIIADGLKYRIQefkgGYHQLIIASVtDDDATVYQVRA 78

                    ....*....
gi 1958765569  8872 ENSVGEVSS 8880
Cdd:cd20971      79 TNQGGSVSG 87
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
22378-22460 8.43e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.05  E-value: 8.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 22378 LRKVVTIRACCTLRLFVPIKGRPAPEVKWAR--EHGESLDKASIE-STSSYTLLVVGNVNRFDSGKYILTVENSSGSKSA 22454
Cdd:cd05891       7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKndQDIELSEHYSVKlEQGKYASLTIKGVTSEDSGKYSINVKNKYGGETV 86

                    ....*.
gi 1958765569 22455 FVNVRV 22460
Cdd:cd05891      87 DVTVSV 92
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
14213-14282 8.47e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 40.97  E-value: 8.47e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569 14213 TVKAGTKIELPATVTGKPEPKITWTKA-----DTLLRPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCG 14282
Cdd:cd05732      12 TAVELEQITLTCEAEGDPIPEITWRRAtrgisFEEGDLDGRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNRIG 86
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
4480-4569 8.48e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 41.08  E-value: 8.48e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4480 PHFIKELEPVQSAINKKIHLECQVDEDRKVSITWSKDGQKLPAGKDyKIYFEDKIASLEIPLAKLKDSGTYSCTASNEAG 4559
Cdd:cd20976       2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAG 80
                            90
                    ....*....|
gi 1958765569  4560 SSSSSATVAV 4569
Cdd:cd20976      81 QVSCSAWVTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
12015-12071 8.50e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 40.39  E-value: 8.50e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 12015 ARFECVLT--REANVIWSKGPDIIKASDKFDIIADGKKHILVINDSQFDDEGVYTAEVE 12071
Cdd:cd00096       1 VTLTCSASgnPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
4963-5038 8.52e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 41.17  E-value: 8.52e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  4963 GGACRLDCKIAG-SLPMRVSWFKDGKEIAASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSRGALIV 5038
Cdd:cd20927      14 GGHVKYVCKIENyDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 90
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
12982-13046 8.57e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 40.84  E-value: 8.57e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569 12982 ANLEVSEGDTIKLVCEVS-KPGAEVTWYKGDEEvIETGRFEILTDgrkRILIIQNAQLEDAGSYNC 13046
Cdd:cd05725       5 QNQVVLVDDSAEFQCEVGgDPVPTVRWRKEDGE-LPKGRYEILDD---HSLKIRKVTAGDMGSYTC 66
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6636-6712 8.61e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 41.01  E-value: 8.61e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  6636 PSFTRRLKDIGGVLGTSCVLECKVAGSsPI-SIAWFHEKTKIVSGAKyQTTFSDNvcTLQLNSLD-SSDMGSYTCVAAN 6712
Cdd:cd20958       1 PPFIRPMGNLTAVAGQTLRLHCPVAGY-PIsSITWEKDGRRLPLNHR-QRVFPNG--TLVIENVQrSSDEGEYTCTARN 75
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
31059-31132 8.68e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 40.91  E-value: 8.68e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569 31059 GEAAQLSCQIVGRPLPDIKWYRfGKELVQSRKYKMS----SDGRtHTLTVMTEEQEDEGVYTCVATNEVGEVETSSKL 31132
Cdd:cd05892      15 GDPVRLECQISAIPPPQIFWKK-NNEMLQYNTDRISlyqdNCGR-ICLLIQNANKKDAGWYTVSAVNEAGVVSCNARL 90
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
1406-1508 8.79e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.05  E-value: 8.79e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1406 TDESQLERLYKPVFVLKPASFKCLEGqtarfdlkvvGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPALPSDS 1485
Cdd:cd05729       4 TDTEKMEEREHALPAANKVRLECGAG----------GNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDK 73
                            90       100
                    ....*....|....*....|...
gi 1958765569  1486 GEWTVVAQNRAGksTISVTLTVE 1508
Cdd:cd05729      74 GKYTCIVENEYG--SINHTYDVD 94
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
13900-13994 8.81e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 40.91  E-value: 8.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 13900 DASVEPTMDLSAFKDGLEVIVPNPIKilvpstGYPRPKATWTFGDQVLEAGDRVkikTISAYAELIISPSERPDKGIYTL 13979
Cdd:cd04969       2 DFELNPVKKKILAAKGGDVIIECKPK------ASPKPTISWSKGTELLTNSSRI---CILPDGSLKIKNVTKSDEGKYTC 72
                            90
                    ....*....|....*..
gi 1958765569 13980 TLENPV--KSISGEIDV 13994
Cdd:cd04969      73 FAVNFFgkANSTGSLSV 89
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8796-8894 8.86e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.09  E-value: 8.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8796 PPYFVKQLEPLKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTCKMHFKNNVATLVFTQVDSNDSGEYICRAENSV 8875
Cdd:cd05762       1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                            90
                    ....*....|....*....
gi 1958765569  8876 GEVSSSTFLTVQEQKLPPS 8894
Cdd:cd05762      81 GSRQAQVNLTVVDKPDPPA 99
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
27002-27069 8.87e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.05  E-value: 8.87e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 27002 AGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFN-TEITAENLTINLKESVTADAGKYEITAANSSGT 27069
Cdd:cd05729      18 AANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGgTKVEEKGWSLIIERAIPRDKGKYTCIVENEYGS 86
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
24833-24904 8.89e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 40.99  E-value: 8.89e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569 24833 YSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLRQTTRVNVEETATSTILHIKESS-KDDFGKYSVTATNNAGT 24904
Cdd:cd05857      14 HAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVvPSDKGNYTCVVENEYGS 86
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
33906-33966 9.02e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 40.55  E-value: 9.02e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569 33906 GKVLTVACAFTGEPTPEITWS------CGGRRIQSQEQQGRfhientddlTTLIIMDVQKQDGGLYT 33966
Cdd:cd05743       1 GETVEFTCVATGVPTPIINWRlnwghvPDSARVSITSEGGY---------GTLTIRDVKESDQGAYT 58
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
29964-30046 9.10e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.04  E-value: 9.10e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29964 LKKTVIIRAGASLRLMVSVSGRPSPVITWSK--KGIDLANRAIID-NTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSA 30040
Cdd:cd05737       7 LPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKndQALAFLDHCNLKvEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETS 86

                    ....*.
gi 1958765569 30041 TVLVKV 30046
Cdd:cd05737      87 DVTVSV 92
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
5915-5973 9.12e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 40.79  E-value: 9.12e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569  5915 ITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGVERCYAFLLV 5973
Cdd:cd20927      32 VTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 90
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
28477-28552 9.14e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.01  E-value: 9.14e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 28477 FDGLVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGS----------TSLFVRDAtrdhrGVYTVEAK 28546
Cdd:cd20956       8 FSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYVTSdgdvvsyvniSSVRVEDG-----GEYTCTAT 82

                    ....*.
gi 1958765569 28547 NVSGST 28552
Cdd:cd20956      83 NDVGSV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8161-8218 9.19e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 40.98  E-value: 9.19e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8161 YECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDsvaILEMHNLSVEDSGDYTCEARN 8218
Cdd:cd20957      21 FNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRN 75
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
18431-18510 9.19e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 40.87  E-value: 9.19e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 18431 TVRVGQTIRILARVKGRPEPDITWSKEGkVLVKDKRVDLIHDLPRV----ELQIKEAVRADHGKYIISAKNSSGHAQGSA 18506
Cdd:cd20951      11 TVWEKSDAKLRVEVQGKPDPEVKWYKNG-VPIDPSSIPGKYKIESEygvhVLHIRRVTVEDSAVYSAVAKNIHGEASSSA 89

                    ....
gi 1958765569 18507 IVNV 18510
Cdd:cd20951      90 SVVV 93
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
6270-6349 9.21e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 40.79  E-value: 9.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6270 IVKAGDSARLECKITGSPE-IRVVWYRNEHELTASDKYQMTFIDSVAVMQMNSLGTEDSGDFICEAQNPAGSTSCSTKVI 6348
Cdd:cd20927      10 VGEEGGHVKYVCKIENYDQsTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAELF 89

                    .
gi 1958765569  6349 V 6349
Cdd:cd20927      90 V 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8243-8317 9.23e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 40.64  E-value: 9.23e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958765569  8243 PVETLKGADVHLECEL-QGTPPFQVSWYKDKRELRSGKKYKIMSENLLT-SIHILNVDTADIGEYQCKATNDVGSDT 8317
Cdd:pfam00047     5 TVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQsSLLISNVTKEDAGTYTCVVNNPGGSAT 81
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
29981-30046 9.24e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 40.96  E-value: 9.24e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 29981 SVSGRPSPVITWSKKGIDL----ANRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLVKV 30046
Cdd:cd05750      23 ATSENPSPRYRWFKDGKELnrkrPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
7700-7759 9.30e-03

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin-M1 domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409521  Cd Length: 90  Bit Score: 40.79  E-value: 9.30e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7700 KVKWFKGSRELESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTNDAGSASCTTHLFV 7759
Cdd:cd20927      31 QVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAELFV 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7301-7373 9.31e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 40.63  E-value: 9.31e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958765569  7301 PPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKVTSknfDTSLHIFNLE-APDIGEYHCKATNEVG 7373
Cdd:cd20958       8 GNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFP---NGTLVIENVQrSSDEGEYTCTARNQQG 78
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
26309-26391 9.37e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.04  E-value: 9.37e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 26309 DVIVVKAGEVLKINADIAGRPLPVISWAKD--GVEIEERAKTEiVSTDSNTTLTVKDCVRRDTGQYVLTLKNVAGTRTMA 26386
Cdd:cd05737       9 DVVTIMEGKTLNLTCNVWGDPPPEVSWLKNdqALAFLDHCNLK-VEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSD 87

                    ....*
gi 1958765569 26387 VNCKV 26391
Cdd:cd05737      88 VTVSV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
8714-8783 9.38e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.05  E-value: 9.38e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958765569  8714 SIEKGKPLILEGTFSGTPPISVTWKKNGVNVTASQRCNITTTE-KSAILEILSSTVEDSGQYNCYIENASG 8783
Cdd:cd05891      12 TIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYSINVKNKYG 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8332-8405 9.42e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 40.64  E-value: 9.42e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958765569  8332 KKLSDVSTIIGKEVQLQ-TTIEGAEPISVAWFKDKGEIVRESdniWISHSEN---VATLHFSRAEPANAGKYTCQIKN 8405
Cdd:pfam00047     1 SAPPTVTVLEGDSATLTcSASTGSPGPDVTWSKEGGTLIESL---KVKHDNGrttQSSLLISNVTKEDAGTYTCVVNN 75
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
6825-6909 9.42e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 40.96  E-value: 9.42e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6825 VKKLSDHSVEPGKSIILEGTYTGTLP-ISVTWKKDGVVIT--PSERCNIVTTEKTCILEILTSTKGDAGHYSCEIENEAG 6901
Cdd:cd05750       3 LKEMKSQTVQEGSKLVLKCEATSENPsPRYRWFKDGKELNrkRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILG 82

                    ....*...
gi 1958765569  6902 RDSCDALV 6909
Cdd:cd05750      83 KDTVTGNV 90
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
31461-31529 9.49e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 40.64  E-value: 9.49e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 31461 CKVTGHPKPIVKWYRQGKEIIADGLKYRVQEfkggyHQLIIASVTDDDATVYQVRATNQGGSVSGTASL 31529
Cdd:cd05723      19 CEVTGKPTPTVKWVKNGDVVIPSDYFKIVKE-----HNLQVLGLVKSDEGFYQCIAENDVGNAQASAQL 82
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
5807-5878 9.49e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 40.64  E-value: 9.49e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958765569  5807 DVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKcapSDVGEYQCIIANEGGSCACTARV 5878
Cdd:cd05723      14 DIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVK---SDEGFYQCIAENDVGNAQASAQL 82
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
6268-6349 9.52e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 40.96  E-value: 9.52e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  6268 SKIVKAGDSARLECKITG-SPEIRVVWYRNEHELTASD----KYQMTFIDSVavMQMNSLGTEDSGDFICEAQNPAGSTS 6342
Cdd:cd05750       8 SQTVQEGSKLVLKCEATSeNPSPRYRWFKDGKELNRKRpkniKIRNKKKNSE--LQINKAKLEDSGEYTCVVENILGKDT 85

                    ....*..
gi 1958765569  6343 CSTKVIV 6349
Cdd:cd05750      86 VTGNVTV 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
8617-8700 9.52e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 40.99  E-value: 9.52e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  8617 PDPMD-----VLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCN-VSLQDSVAELELFDVDTSQSGDYTCIVSNEAG 8690
Cdd:cd05857       6 PEKMEkklhaVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGgYKVRNQHWSLIMESVVPSDKGNYTCVVENEYG 85
                            90
                    ....*....|
gi 1958765569  8691 RASCTTQLFV 8700
Cdd:cd05857      86 SINHTYHLDV 95
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
8617-8690 9.55e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.04  E-value: 9.55e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  8617 PDPMDVLTGSNVTFTSIVKGTPPFTVSWFKGSSELVPGARCNVSL-QDSVAELELFDVDTSQSGDYTCIVSNEAG 8690
Cdd:cd05737       8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVeAGRTVYFTINGVSSEDSGKYGLVVKNKYG 82
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
32215-32283 9.61e-03

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 40.65  E-value: 9.61e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958765569 32215 GENVRFGVTITVHPEPRVTWYKSGQKIKPGDDDKKYTFESDKglyqLTINSVTTDDDAEYAVVARNKHG 32283
Cdd:cd05867      14 GETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGA----LILTDVQPSDTAVYQCEARNRHG 78
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
5994-6066 9.62e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 40.91  E-value: 9.62e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958765569  5994 VTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFEnnvASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRV 6066
Cdd:cd04969      20 VIIECKPKASPKPTISWSKGTELLTNSSRICILPD---GSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
27797-27874 9.62e-03

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 41.14  E-value: 9.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27797 AGEDVQLLIPFKGRPPPTVTWRK-------DEKNLGSDARYSIQNTDSsslLVIPQVTRNDTGKYILTIENGVGQPKSST 27869
Cdd:cd20954      15 AGQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYDPNVRILPNGT---LVFGHVQKENEGHYLCEAKNGIGSGLSKV 91

                    ....*
gi 1958765569 27870 VSVKV 27874
Cdd:cd20954      92 IFLKV 96
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
4601-4663 9.63e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 40.75  E-value: 9.63e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958765569  4601 PVIQVTWFKNNKELSESN---TVRMSFANSEAILDITDVKVDDSGTYSCEATNDAGSDSCSTEVVI 4663
Cdd:cd05895      28 PSLRFKWFKNGKEINRKNkpeNIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDSASANVTI 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
13923-13996 9.67e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.57  E-value: 9.67e-03
                             10        20        30        40        50        60        70
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958765569  13923 PIKILVPSTGYPRPKATWTF-GDQVLEAGDRVKIKTISAYAELIISPSERPDKGIYTLTLENPVKSISGEIDVNV 13996
Cdd:smart00410    11 SVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
20213-20295 9.67e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.57  E-value: 9.67e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  20213 KTLILRAGVTMRLYVPVKGRPPPKITWSKPN---VNLRERIglDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEY 20289
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgklLAESGRF--SVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                     ....*.
gi 1958765569  20290 TIVVKV 20295
Cdd:smart00410    80 GTTLTV 85
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
1417-1507 9.69e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 41.00  E-value: 9.69e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  1417 PVFVLKPASFKCLEGQTARFDLKVVGRPMPETFW---FHNGQQIV---NDYTHKVVIKEDGtqSLIIVPALPSDSGEWTV 1490
Cdd:cd05765       1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWekqVPGKENLImrpNHVRGNVVVTNIG--QLVIYNAQPQDAGLYTC 78
                            90
                    ....*....|....*..
gi 1958765569  1491 VAQNRAGKSTISVTLTV 1507
Cdd:cd05765      79 TARNSGGLLRANFPLSV 95
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7674-7759 9.74e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 40.64  E-value: 9.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  7674 QTPDSVEVLPGMSLTFTSVFRGTPPFKVKWFKGSREL-ESGEACTISLEDFVTELELLEVEPLQSGDYSCLVTNDAGSAS 7752
Cdd:cd20973       2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIvESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                    ....*..
gi 1958765569  7753 CTTHLFV 7759
Cdd:cd20973      82 CSAELTV 88
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
5056-5124 9.78e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.05  E-value: 9.78e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5056 GSAVCLKSAFQGSTPLTIRWFKGDKELVSGGSCYITK-EASESSLELYAVKTTDSGTYTCKVSNVAGSVE 5124
Cdd:cd05729      19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKvEEKGWSLIIERAIPRDKGKYTCIVENEYGSIN 88
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
27797-27863 9.80e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 40.99  E-value: 9.80e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 27797 AGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDAR---YSIQNTDSSslLVIPQVTRNDTGKYILTIENGVG 27863
Cdd:cd05857      18 AANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRiggYKVRNQHWS--LIMESVVPSDKGNYTCVVENEYG 85
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
5793-5876 9.81e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 40.91  E-value: 9.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5793 FIRELEPVevVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKcapSDVGEYQCIIANEGGSC 5872
Cdd:cd04969       7 PVKKKILA--AKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGSLKIKNVTK---SDEGKYTCFAVNFFGKA 81

                    ....
gi 1958765569  5873 ACTA 5876
Cdd:cd04969      82 NSTG 85
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
25628-25707 9.83e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 40.46  E-value: 9.83e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 25628 VVTLRASATLRlfVTIKGRPEPEVKWEKAEGILTE-RAQIEVTSSytmLVIDNVTRFDSGRYNLTLENNSGSKTAFVNVR 25706
Cdd:cd05725       8 VVLVDDSAEFQ--CEVGGDPVPTVRWRKEDGELPKgRYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEASATLT 82

                    .
gi 1958765569 25707 V 25707
Cdd:cd05725      83 V 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4670-4753 9.84e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 40.64  E-value: 9.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4670 IKTLEPAHIVRGANALLQCEVAGTGPFEVSWFKDKKQIRSSKKYRL-FTQKTFVFLEITSFNSADIGDYECVVANEVGKC 4748
Cdd:cd20973       1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                    ....*
gi 1958765569  4749 GCVAT 4753
Cdd:cd20973      81 TCSAE 85
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
5786-5871 9.86e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 40.69  E-value: 9.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  5786 KVKEPPIfirelePVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSvfyLHITKCAPSDVGEYQCII 5865
Cdd:cd20968       1 KITRPPT------NVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLESGS---LRIHNVQKEDAGQYRCVA 71

                    ....*.
gi 1958765569  5866 ANEGGS 5871
Cdd:cd20968      72 KNSLGI 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
10149-10253 9.86e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 9.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569 10149 PPAVKVPEAPKKPVPEEKKPVPIPKKEPAAPPKVPEAPKKPAPEEKTAVPVAKKKEA--------------------PPP 10208
Cdd:PHA03247   2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPArppttagppapappaapaagPPR 2781
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1958765569 10209 KVTEVQKKVVTEEKITIIPQREESPPPAVPEIPKKKVPEEKRPVP 10253
Cdd:PHA03247   2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG 2826
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
4386-4466 9.88e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 40.63  E-value: 9.88e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765569  4386 PPTFlsRP-KSLTTFVGKAAKFLCTVSGTPvIETI-WQKDGTALspsPDCRITDADNKHSLELSNLT-VQDRGVYSCKAS 4462
Cdd:cd20958       1 PPFI--RPmGNLTAVAGQTLRLHCPVAGYP-ISSItWEKDGRRL---PLNHRQRVFPNGTLVIENVQrSSDEGEYTCTAR 74

                    ....
gi 1958765569  4463 NKFG 4466
Cdd:cd20958      75 NQQG 78
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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